CELA2A Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P08217 |
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Clone Names | 100430044 |
Gene ID | 63036 |
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Other Names | Chymotrypsin-like elastase family member 2A, Elastase-2A, CELA2A, ELA2A |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP14005b was selected from the C-term region of CELA2A. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | CELA2A (HGNC:24609) |
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Synonyms | ELA2A |
Function | Elastase that enhances insulin signaling and might have a physiologic role in cellular glucose metabolism. Circulates in plasma and reduces platelet hyperactivation, triggers both insulin secretion and degradation, and increases insulin sensitivity. |
Cellular Location | Secreted. |
Tissue Location | Expressed in pancreas. Not detected in keratinocytes (PubMed:10620133). Detected in exocrine secretions of the pancreas (at protein level). Also expressed in a small fraction of cells in pancreatic islets, adrenal cortex, intestinal glands and colonic lymphoid follicles (at protein level) (PubMed:31358993) Detected in plasma (PubMed:31358993). |
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Provided below are standard protocols that you may find useful for product applications.
Background
Elastases form a subfamily of serine proteases thathydrolyze many proteins in addition to elastin. Humans have sixelastase genes which encode the structurally similar proteinselastase 1, 2, 2A, 2B, 3A, and 3B. Like most of the humanelastases, elastase 2A is secreted from the pancreas as a zymogen.In other species, elastase 2A has been shown to preferentiallycleave proteins after leucine, methionine, and phenylalanineresidues.
References
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)Lamesch, P., et al. Genomics 89(3):307-315(2007)Lausen, J., et al. Oncogene 25(9):1349-1357(2006)Szepessy, E., et al. Pancreatology 6 (1-2), 117-122 (2006) :
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