SERPINA3
SERPINA3 (serpin family A member 3), also known as alpha-1-antichymotrypsin, ACT or AACT, is a secreted member of the serpin family of serine protease inhibitors. It can inhibit neutrophil cathepsin G and mast cell chymase, although its physiological function remains unclear. Browse Assay Genie's current range of SERPINA3 research reagents below, or read on for the biology behind the target.
SERPINA3 belongs to the serpin family, a group of proteins that inhibit serine proteases. The secreted SERPINA3 protein can inhibit neutrophil cathepsin G and mast cell chymase. Both of these proteases can convert angiotensin-1 to the active angiotensin-2. UniProt notes that the physiological function of the protein is still unclear, so its inhibitory activity against these two proteases is best read as a defined biochemical property rather than a settled biological role.
The SERPINA3 gene is one of a cluster of serpin genes on the q arm of chromosome 14. The encoded protein, listed under the HGNC gene group of serpin peptidase inhibitors, is also called alpha-1-antichymotrypsin. NCBI Gene reports that polymorphisms in the protein appear to be tissue specific and influence protease targeting, which makes sequence variation a relevant consideration when studying how it engages its target proteases.
SERPINA3 has been linked to several diseases. Variations in the protein sequence have been implicated in Alzheimer's disease, and deficiency has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease. Earlier names for the gene include serine (or cysteine) proteinase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3, which reflects its relationship to alpha-1-antitrypsin and the other clade A serpins. Researchers working with a SERPINA3 antibody, SERPINA3 ELISA kit or recombinant SERPINA3 protein are typically studying protease regulation or one of these disease areas.
SERPINA3 inhibits neutrophil cathepsin G and mast cell chymase, making it a subject for studies of serine protease regulation.
Variations in the SERPINA3 protein sequence have been implicated in Alzheimer's disease.
Mutations in SERPINA3 have been identified in patients with Parkinson disease, supporting genetic and mechanistic investigation.
SERPINA3 mutations occur in chronic obstructive pulmonary disease, and deficiency of the protein has been associated with liver disease.
SERPINA3 is a serpin that can inhibit neutrophil cathepsin G and mast cell chymase, two proteases that convert angiotensin-1 to active angiotensin-2. UniProt states that its physiological function is unclear, so its precise biological role is still under investigation.
SERPINA3 is also known as alpha-1-antichymotrypsin, ACT and AACT. Older names include serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3. HGNC now lists it as serpin family A member 3, in the serpin peptidase inhibitors gene group.
Yes. NCBI Gene reports that sequence variations have been implicated in Alzheimer's disease and that deficiency has been associated with liver disease. Mutations have been identified in patients with Parkinson disease and chronic obstructive pulmonary disease. Check the datasheet of any product for its validated reactivity.
Other clade A serpins from the same chromosome 14 gene cluster and related serine protease inhibitors with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P01011; product specifications from Assay Genie datasheets.