SERPINA3 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, FC, E |
---|---|
Primary Accession | P01011 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 47651 Da |
Antigen Region | 282-310 aa |
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 | This SERPINA3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 282-310 amino acids from the C-terminal region of human SERPINA3. |
Dilution | WB~~1:1000 FC~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | SERPINA3 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | SERPINA3 |
---|---|
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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