Mastery Studying Ensures Right Private Protecting Tools Use in Simulated Medical Encounters of COVID-19
Introduction: The right use of private protecting gear (PPE) limits transmission of great communicable illnesses to healthcare employees, which is critically vital within the period of coronavirus illness 2019 (COVID-19). Nevertheless, prior research illustrated that healthcare employees continuously err throughout software and elimination of PPE. The purpose of this research was to find out whether or not a simulation-based, mastery studying intervention with deliberate follow improves right use of PPE by physicians throughout a simulated scientific encounter with a COVID-19 affected person.
Strategies:
This was a pretest-posttest research carried out within the emergency division at a big, educational tertiary care hospital between March 31-April 8, 2020. A complete of 117 topics participated, together with 56 college members and 61 resident physicians. Previous to the intervention, all members acquired institution-mandated training on PPE use by way of a web-based video and supplemental supplies.
Contributors accomplished a pretest expertise evaluation utilizing a 21-item guidelines of steps to accurately don and doff PPE. Contributors have been anticipated to fulfill a minimal passing rating (MPS) of 100%, decided by an skilled panel utilizing the Mastery Angoff and Affected person Security standard-setting strategies. Contributors that met the MPS on pretest have been exempt from the tutorial intervention.
Testing occurred earlier than and after an in-person demonstration of correct donning and doffing strategies and 20 minutes of deliberate follow. The first end result was a change in evaluation scores of right PPE use following our instructional intervention. Secondary outcomes included variations in efficiency scores between college members and resident physicians, and variations in efficiency throughout donning vs doffing sequences.
Outcomes: All members had a imply pretest rating of 73.1% (95% confidence interval [CI], 70.9-75.3%). College member and resident pretest scores have been comparable (75.1% vs 71.3%, p = 0.082). Imply pretest doffing scores have been decrease than donning scores throughout all members (65.8% vs 82.8%, p<0.001). Participant scores elevated 26.9% (95% CI of the distinction 24.7-29.1%, p<0.001) following our instructional intervention leading to all members assembly the MPS of 100%.
Conclusion: A mastery studying intervention with deliberate follow ensured the right use of PPE by doctor topics in a simulated scientific encounter of a COVID-19 affected person. Additional research of translational outcomes is required.
Description: Interleukin 4 (IL-4) is a pleiotropic cytokine produced by activated T cells, mast cells, and basophils. It was initially identified as a B cell differentiation factor (BCDF), as well as a B cell stimulatory factor (BSF1). IL-4 has since been shown to have multiple biological effects on hematopoietic and non-hematopoietic cells, including B and T cells, monocytes, macrophages, mast cells, myeloid and erythroid progenitors, fibroblasts, and endothelial cells. Rat, mouse and human IL-4 are species-specific in their activities.
Description: Interleukin-4 (IL-4), also designated B cell stimulatory factor-1, is a glycosylated cytokine secreted by activated T lymphocytes, basophils and mast cells. The secreted IL-4 protein promotes the growth and differentiation of cells that participate in immune defense by favoring such events as the expansion of the Th2 lineage relative to Th1 cells. These T helper cell subsets are defined by their pattern of cytokine secretion: Th1 cells secrete IL-2, TNFβ and IFN-γ, while Th2 cells secrete IL-4, IL-5 and IL-10. Another key immunological function of IL-4 is to induce immunoglobulin class switching. IL-4 has been shown to induce the production of IgE and enhance IgG4 secretion by B cells, but suppress the production of IgM, IgA, IgG1, IgG2, and IgG3. It has been determined that Stat6 is rapidly tyrosine phosphorylated following stimulation of IL-3 or IL-4, but is not detectably phosphorylated following stimulation with IL-2, IL-12 or erythropoietin.
Description: IL-4 is a pleiotropic cytokine that is produced by activated T cells, mast cells, and basophils. IL-4 elicits many different biological responses but has two dominant functions. The first is regulating differentiation of naïve CD4+ T cell to the Th2 type. Th2 cells produce IL-4, IL-5, IL-10, and IL-13, which tend to favor a humoral immune response while suppressing a cell-mediated immune response controlled by Th1 cells. The second is regulating IgE and IgG1 production by B cells.
Description: IL-4 is a pleiotropic cytokine that is produced by activated T cells, mast cells, and basophils. IL-4 elicits many different biological responses but has two dominant functions. The first is regulating differentiation of naïve CD4+ T cell to the Th2 type. Th2 cells produce IL-4, IL-5, IL-10, and IL-13, which tend to favor a humoral immune response while suppressing a cell-mediated immune response controlled by Th1 cells. The second is regulating IgE and IgG1 production by B cells.
Description: IL-4 is a pleiotropic cytokine that is produced by activated T cells, mast cells, and basophils. IL-4 elicits many different biological responses but has two dominant functions. The first is regulating differentiation of naïve CD4+ T cell to the Th2 type. Th2 cells produce IL-4, IL-5, IL-10, and IL-13, which tend to favor a humoral immune response while suppressing a cell-mediated immune response controlled by Th1 cells. The second is regulating IgE and IgG1 production by B cells.
Description: IL-4 is a pleiotropic cytokine that is produced by activated T cells, mast cells, and basophils. IL-4 elicits many different biological responses but has two dominant functions. The first is regulating differentiation of naïve CD4+ T cell to the Th2 type. Th2 cells produce IL-4, IL-5, IL-10, and IL-13, which tend to favor a humoral immune response while suppressing a cell-mediated immune response controlled by Th1 cells. The second is regulating IgE and IgG1 production by B cells.
Description: IL-4 is a pleiotropic cytokine that is produced by activated T cells, mast cells, and basophils. IL-4 elicits many different biological responses but has two dominant functions. The first is regulating differentiation of naïve CD4+ T cell to the Th2 type. Th2 cells produce IL-4, IL-5, IL-10, and IL-13, which tend to favor a humoral immune response while suppressing a cell-mediated immune response controlled by Th1 cells. The second is regulating IgE and IgG1 production by B cells.
Description: IL-4 is a pleiotropic cytokine that is produced by activated T cells, mast cells, and basophils. IL-4 elicits many different biological responses but has two dominant functions. The first is regulating differentiation of naïve CD4+ T cell to the Th2 type. Th2 cells produce IL-4, IL-5, IL-10, and IL-13, which tend to favor a humoral immune response while suppressing a cell-mediated immune response controlled by Th1 cells. The second is regulating IgE and IgG1 production by B cells.
Description: IL-4 is a pleiotropic cytokine that is produced by activated T cells, mast cells, and basophils. IL-4 elicits many different biological responses but has two dominant functions. The first is regulating differentiation of naïve CD4+ T cell to the Th2 type. Th2 cells produce IL-4, IL-5, IL-10, and IL-13, which tend to favor a humoral immune response while suppressing a cell-mediated immune response controlled by Th1 cells. The second is regulating IgE and IgG1 production by B cells.
Description: IL-4 is a pleiotropic cytokine that is produced by activated T cells, mast cells, and basophils. IL-4 elicits many different biological responses but has two dominant functions. The first is regulating differentiation of naïve CD4+ T cell to the Th2 type. Th2 cells produce IL-4, IL-5, IL-10, and IL-13, which tend to favor a humoral immune response while suppressing a cell-mediated immune response controlled by Th1 cells. The second is regulating IgE and IgG1 production by B cells.
Description: Interleukin 4 (IL-4) is a pleiotropic cytokine produced by activated T cells, mast cells, and basophils. It was initially identified as a B cell differentiation factor (BCDF), as well as a B cell stimulatory factor (BSF1). IL-4 has since been shown to have multiple biological effects on hematopoietic and non-hematopoietic cells, including B and T cells, monocytes, macrophages, mast cells, myeloid and erythroid progenitors, fibroblasts, and endothelial cells. Rat, mouse and human IL-4 are species-specific in their activities.
Description: The protein encoded by this gene is a pleiotropic cytokine produced by activated T cells. This cytokine is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. This gene, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. IL4 is considered an important cytokine for tissue repair, counterbalancing the effects of proinflammatory type 1 cytokines, however, it also promotes allergic airway inflammation. Moreover, IL-4, a type 2 cytokine, mediates and regulates a variety of human host responses such as allergic, anti-parasitic, wound healing, and acute inflammation. This cytokine has been reported to promote resolution of neutrophil-mediated acute lung injury. In an allergic response, IL-4 has an essential role in the production of allergen-specific immunoglobin (Ig) E. This pro-inflammatory cytokine has been observed to be increased in COVID-19 (Coronavirus disease 2019) patients, but is not necessarily associated with severe COVID-19 pathology. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
Description: Interleukin 4 (IL-4) is a pleiotropic cytokine produced by activated T cells, mast cells, and basophils. It was initially identified as a B cell differentiation factor (BCDF), as well as a B cell stimulatory factor (BSF1). IL-4 has since been shown to have multiple biological effects on hematopoietic and non-hematopoietic cells, including B and T cells, monocytes, macrophages, mast cells, myeloid and erythroid progenitors, fibroblasts, and endothelial cells. Rat, mouse and human IL-4 are species-specific in their activities.
Description: Interleukin 4 (IL-4) is a pleiotropic cytokine produced by activated T cells, mast cells, and basophils. It was initially identified as a B cell differentiation factor (BCDF), as well as a B cell stimulatory factor (BSF1). IL-4 has since been shown to have multiple biological effects on hematopoietic and non-hematopoietic cells, including B and T cells, monocytes, macrophages, mast cells, myeloid and erythroid progenitors, fibroblasts, and endothelial cells. Rat, mouse and human IL-4 are species-specific in their activities.
Medical interns’ reflections on their coaching in use of private protecting gear
Background: The present COVID-19 pandemic has demonstrated that private protecting gear (PPE) is important, to forestall the acquisition and transmission of infectious illnesses, but its use is commonly sub-optimal within the scientific setting.
Coaching and training are vital to make sure and maintain the secure and efficient use of PPE by medical interns, however present strategies are sometimes insufficient in offering the related data and expertise. The aim of this research was to discover medical graduates’ experiences of using PPE and determine alternatives for enchancment in training and coaching programmes, to enhance occupational and affected person security.
Strategies: This research was undertaken in 2018 in a big tertiary-care educating hospital in Sydney, Australia, to discover medical interns’ self-reported experiences of PPE use, at the start of their internship. Reflexive teams have been carried out instantly after theoretical and sensible PPE coaching, throughout hospital orientation. Transcripts of recorded discussions have been analysed, utilizing a thematic strategy that drew on the COM-B (functionality, alternative, motivation – behaviour) framework for behaviour.
Outcomes: 80% of 90 eligible graduates participated. Many interns had not beforehand acquired formal coaching within the particular expertise required for optimum PPE use and had developed doubtlessly unsafe habits. Their experiences as medical college students in scientific areas contrasted sharply with really useful follow taught at hospital orientation and impacted on their capability to domesticate right PPE use.
Conclusions: Undergraduate educating ought to be in keeping with greatest follow PPE use, and embody sensible coaching that embeds right and secure practices.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.
Description: DKK-1 is a protein that is a member of the dickkopf family. It is a secreted protein with two cysteine rich regions and is involved in embryonic development through its inhibition of the WNT signaling pathway. Elevated levels of DKK-1 in bone marrow plasma and peripheral blood is associated with the presence of osteolytic bone lesions in patients with multiple myeloma.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-l1 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-3 has been shown to potentiate, rather than inhibit, Wnt signaling through interactions with the high-affinity, transmembrane coreceptors Kremen-1 (Krm1) and Kremen-2 (Krm2). Recombinant human DKK-3 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 36.3 kDa and contains 329 amino acid residues. Due to glycosylation, human DKK-3 migrates at an apparent molecular weight of approximately 39-49 kDa by SDS-PAGE analysis under non-reducing conditions.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-l1 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-3 has been shown to potentiate, rather than inhibit, Wnt signaling through interactions with the high-affinity, transmembrane coreceptors Kremen-1 (Krm1) and Kremen-2 (Krm2). Recombinant human DKK-3 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 36.3 kDa and contains 329 amino acid residues. Due to glycosylation, human DKK-3 migrates at an apparent molecular weight of approximately 39-49 kDa by SDS-PAGE analysis under non-reducing conditions.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 25.8 kDa and contains 234 amino acid residues. Due to glycosylation, human DKK-2 migrates at an apparent molecular weight of approximately 31-36 kDa by SDS-PAGE analysis under non-reducing conditions.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 25.8 kDa and contains 234 amino acid residues. Due to glycosylation, human DKK-2 migrates at an apparent molecular weight of approximately 31-36 kDa by SDS-PAGE analysis under non-reducing conditions.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 fused to a C terminal His-tag derived from E. coli has a molecular weight of 26.0 kDa and contains 234 amino acid residues.
Description: The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-11 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt-regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-2 has been shown to both inhibit and enhance canonical Wnt signaling; enhancing Wnt signaling through direct high-affinity binding of DKK-2 to LRP6 during LRP6 overexpression, while inhibiting Wnt signaling and promoting LRP6 internalization through the formation of a ternary complex between DKK-2, LRP6, and Kremen-2. Recombinant Human DKK-2 fused to a C terminal His-tag derived from E. coli has a molecular weight of 26.0 kDa and contains 234 amino acid residues.
Description: Dkk1 is a Dickkopf-related protein that inhibits Wnt signaling by binding the Wnt coreceptor LRP5/6. It also binds Kremen1 and Kremen2. Dkk1 is important in embryonic development.
Description: Dkk1 is a Dickkopf-related protein that inhibits Wnt signaling by binding the Wnt coreceptor LRP5/6. It also binds Kremen1 and Kremen2. Dkk1 is important in embryonic development.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.
Description: Description of target: This gene encodes a protein that is a member of the dickkopf family. It is a secreted protein with two cysteine rich regions and is involved in embryonic development through its inhibition of the WNT signaling pathway. Elevated levels of DKK1 in bone marrow plasma and peripheral blood is associated with the presence of osteolytic bone lesions in patients with multiple myeloma.;Species reactivity: Human;Application: ELISA;Assay info: Quantitative Colorimentric Sandwich ELISA;Sensitivity: 63 pg/mL
Description: Human Dkk-1 Protein, His Tag, premium grade (DK1-H5221) is expressed from human 293 cells (HEK293). It contains AA Thr 32 - His 266 (Accession # NP_036374.1).
Description: Biotinylated Human Dkk-1, Fc,Avitag (DK1-H82F5) is expressed from human 293 cells (HEK293). It contains AA Thr 32 - His 266 (Accession # O94907-1).
Description: Members of the dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK1 takes part in embryonic development through its inhibition of the WNT signaling pathway, binds to LRP6 with high affinity and prevents the Frizzled-Wnt-LRP6 complex formation in response to Wnts. DKK1 promotes LRP6 internalization and degradation when it forms a ternary complex with the cell surface receptor Kremen.DKK1 not olny functions as a head inducer during development, but also regulates joint remodeling and bone formation, which suggests roles for DKK1 in the pathogenesis of rheumatoid arthritis and multiple myeloma. More recently research reported, DKK1 impacts eye development from a defined developmental time point on, and is critical for lens separation from the surface ectoderm via beta-catenin mediated Pdgfralpha and E-cadherin expression.
Description: Members of the dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK1 takes part in embryonic development through its inhibition of the WNT signaling pathway, binds to LRP6 with high affinity and prevents the Frizzled-Wnt-LRP6 complex formation in response to Wnts. DKK1 promotes LRP6 internalization and degradation when it forms a ternary complex with the cell surface receptor Kremen.DKK1 not olny functions as a head inducer during development, but also regulates joint remodeling and bone formation, which suggests roles for DKK1 in the pathogenesis of rheumatoid arthritis and multiple myeloma. More recently research reported, DKK1 impacts eye development from a defined developmental time point on, and is critical for lens separation from the surface ectoderm via beta-catenin mediated Pdgfralpha and E-cadherin expression.
Description: A polyclonal antibody for detection of Dkk-1 from Human, Mouse, Rat. This Dkk-1 antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human Dkk-1
Description: A polyclonal antibody for detection of Dkk-1 from Human, Mouse, Rat. This Dkk-1 antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human Dkk-1
Description: A polyclonal antibody for detection of Dkk-1 from Human, Mouse, Rat. This Dkk-1 antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the C-terminal region of human Dkk-1
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.
Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 expressed in human 293 cells is a 35-40 kDa glycoprotein containing 235 amino-acid residues.
Description: Description of target: Dickkopf-related protein 3 is a protein that in humans is encoded by the DKK3 gene. This gene encodes a protein that is a member of the dickkopf family. It is mapped to 11p15.3. The secreted protein contains two cysteine rich regions and is involved in embryonic development through its interactions with the Wnt signaling pathway. The expression of this gene is decreased in a variety of cancer cell lines and it may function as a tumor suppressor gene. Members of the Dkk-related family display unique patterns of mRNA expression in human and mouse tissues, and are secreted when expressed in 293T cells. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease.;Species reactivity: Human;Application: ELISA;Assay info: Assay Methodology: Quantitative Sandwich Immunoassay;Sensitivity: <= 10 pg/mL
Description: Human Dkk-3 (R335G), His Tag (DK3-H5220) is expressed from human 293 cells (HEK293). It contains AA Ala 22 - Ile 350 (Accession # Q9UBP4-1 (R335G)).
Description: Members of the dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK1 takes part in embryonic development through its inhibition of the WNT signaling pathway, binds to LRP6 with high affinity and prevents the Frizzled-Wnt-LRP6 complex formation in response to Wnts. DKK1 promotes LRP6 internalization and degradation when it forms a ternary complex with the cell surface receptor Kremen.DKK1 not olny functions as a head inducer during development, but also regulates joint remodeling and bone formation, which suggests roles for DKK1 in the pathogenesis of rheumatoid arthritis and multiple myeloma. More recently research reported, DKK1 impacts eye development from a defined developmental time point on, and is critical for lens separation from the surface ectoderm via β-catenin mediated Pdgfrα and E-cadherin expression.
Description: Members of the dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK1 takes part in embryonic development through its inhibition of the WNT signaling pathway, binds to LRP6 with high affinity and prevents the Frizzled-Wnt-LRP6 complex formation in response to Wnts. DKK1 promotes LRP6 internalization and degradation when it forms a ternary complex with the cell surface receptor Kremen.DKK1 not olny functions as a head inducer during development, but also regulates joint remodeling and bone formation, which suggests roles for DKK1 in the pathogenesis of rheumatoid arthritis and multiple myeloma. More recently research reported, DKK1 impacts eye development from a defined developmental time point on, and is critical for lens separation from the surface ectoderm via β-catenin mediated Pdgfrα and E-cadherin expression.