SERPINA3 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P01011 |
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Clone Names | 80917064 |
Gene ID | 12 |
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Other Names | Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, Serpin A3, Alpha-1-antichymotrypsin His-Pro-less, SERPINA3, AACT |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7314b was selected from the C-term region of human SERPINA3. 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 | SERPINA3 |
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Synonyms | AACT |
Function | Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2. |
Cellular Location | Secreted. |
Tissue Location | Plasma. Synthesized in the liver. Like the related alpha-1-antitrypsin, its concentration increases in the acute phase of inflammation or infection. Found in the amyloid plaques from the hippocampus of Alzheimer disease brains. |
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Provided below are standard protocols that you may find useful for product applications.
Background
SERPINA3 is a plasma protease inhibitor and member of the serine protease inhibitor class. Polymorphisms in this protein appear to be tissue specific and influence protease targeting. Variations in this protein's sequence have been implicated in Alzheimer's disease, and deficiency of this protein has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease.
References
Abraham,C.R., Shirahama,T. Neurobiol. Aging 11 (2), 123-129 (1990)Baumann,U., Huber,R. J. Mol. Biol. 218 (3), 595-606 (1991)Desrochers,P.E., Mookhtiar,K. J. Biol. Chem. 267 (7), 5005-5012 (1992)
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