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CELA3B Antibody (N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P08861 |
|---|---|
| Clone Names | 100427308 |
| Gene ID | 23436 |
|---|---|
| Other Names | Chymotrypsin-like elastase family member 3B, Elastase IIIB, Elastase-3B, Protease E, CELA3B, ELA3B |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP13770a was selected from the N-term region of CELA3B. 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 | CELA3B |
|---|---|
| Synonyms | ELA3B |
| Function | Efficient protease with alanine specificity but only little elastolytic activity. |
| Tissue Location | Pancreas. Not detectable in keratinocytes. |
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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. Unlike other elastases, elastase3B has little elastolytic activity. Like most of the humanelastases, elastase 3B is secreted from the pancreas as a zymogenand, like other serine proteases such as trypsin, chymotrypsin andkallikrein, it has a digestive function in the intestine. Elastase3B preferentially cleaves proteins after alanine residues. Elastase3B may also function in the intestinal transport and metabolism ofcholesterol. Both elastase 3A and elastase 3B have been referred toas protease E and as elastase 1, and excretion of this protein infecal material is frequently used as a measure of pancreaticfunction in clinical assays.
References
Gao, J., et al. Oncol. Rep. 23(6):1683-1692(2010)Teichmann, J., et al. Eur. J. Med. Res. 13(12):563-567(2008)Hahn, J.U., et al. Pancreas 36(3):274-278(2008)Mann, S.T., et al. Eur. J. Med. Res. 13(2):68-72(2008)Vesterhus, M., et al. Diabetes Care 31(2):306-310(2008)
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