a1-Antichymotrypsin Enzyme | SERPINA1 enzyme

a1-Antichymotrypsin, Human (AACT, Alpha1-ACT)

Cat. Num. AAA653849

• Gene Names: SERPINA1; PI; A1A; AAT; PI1; A1AT; PRO2275; alpha1AT
• Applications: ELISA
• Purity: Highly Purified; 98% No contaminants detected. Single band by SDS-PAGE, IEP, and/or RID.
• Synonyms: a1-Antichymotrypsin; Human (AACT; Alpha1-ACT); SERPINA1 enzyme

• Host: Pooled human serum or plasma
• Purity/Purification: Highly Purified; 98% No contaminants detected. Single band by SDS-PAGE, IEP, and/or RID.
• Form/Format: Lyophilized from 0.02M Tris, 0.2M sodium chloride, pH 7.5.

• Applicable Applications for SERPINA1 enzyme: ELISA (EL/EIA)
• Application Notes: Suitable for use in ELISA.
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and add glycerol (40-50%). Freeze at -20 degree C or colder. Aliquots are stable for at least 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for SERPINA1 enzyme

Alpha1-Antichymotrypsin (AACT) is a serine proteinase inhibitor and minor acute phase protein with a molecular weight of ~68kD, occurring in serum at 250-500mg/l. AACT appears to inhibit chymotrypsin specifically.

Product Categories/Family for SERPINA1 enzyme

Molecular Biology; MB-Enzymes

NCBI and Uniprot Product Information

• NCBI GI #: 189163542
• NCBI GeneID: 5265
• NCBI Accession #: NP_001121179.1
• NCBI GenBank Nucleotide #: NM_001127707.1
• UniProt Accession #: P01009; Q0PVP5; Q13672; Q53XB8; Q5U0M1; Q7M4R2; Q86U18; Q86U19; Q96BF9; Q96ES1; A6PX14; B2RDQ8
• Molecular Weight: ~68kD
• NCBI Official Full Name: alpha-1-antitrypsin
• NCBI Official Synonym Full Names: serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1
• NCBI Official Symbol: SERPINA1
• NCBI Official Synonym Symbols: PI; A1A; AAT; PI1; A1AT; PRO2275; alpha1AT
• NCBI Protein Information: alpha-1-antitrypsin; serpin A1; alpha-1-antiproteinase; alpha-1-antitrypsin null; alpha-1 protease inhibitor; protease inhibitor 1 (anti-elastase), alpha-1-antitrypsin; serine (or cysteine) proteinase inhibitor, clade A, member 1
• UniProt Protein Name: Alpha-1-antitrypsin
• Protein Family: Alpha-1-antitrypsin
• UniProt Gene Name: SERPINA1
• UniProt Synonym Gene Names: AAT; PI; SPAAT
• UniProt Entry Name: A1AT_HUMAN

NCBI Description

The protein encoded by this gene is secreted and is a serine protease inhibitor whose targets include elastase, plasmin, thrombin, trypsin, chymotrypsin, and plasminogen activator. Defects in this gene can cause emphysema or liver disease. Several transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

Function: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin. Ref.17 Ref.18 Ref.24Short peptide from AAT: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE). Ref.17 Ref.18 Ref.24

Subcellular location: Secreted Ref.24. Short peptide from AAT: Secreted › extracellular space › extracellular matrix Ref.24.

Tissue specificity: Plasma.

Domain: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.

Post-translational modification: N-glycosylated. Differential glycosylation produces a number of isoforms. N-linked glycan at Asn-107 is alternatively di-antennary, tri-antennary or tetra-antennary. The glycan at Asn-70 is di-antennary with trace amounts of tri-antennary. Glycan at Asn-271 is exclusively di-antennary. Structure of glycans at Asn-70 and Asn-271 is Hex5HexNAc4. The structure of the antennae is Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure Man(alpha1-6)[Man(alpha1-3)]Man(beta1-4)GlcNAc(beta1-4)GlcNAc. Some antennae are fucosylated, which forms a Lewis-X determinant. Ref.19 Ref.26 Ref.34Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.

Polymorphism: The sequence shown is that of the M1V allele which is the most common form of PI (44 to 49%). Other frequent alleles are: M1A 20 to 23%; M2 10 to 11%; M3 14 to 19%.

Involvement in disease: Alpha-1-antitrypsin deficiency (A1ATD) [MIM:613490]: A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.59 Ref.61 Ref.63

Miscellaneous: The aberrant form is found in the plasma of chronic smokers, and persists after smoking is ceased. It can still be found ten years after smoking has ceased.

Sequence similarities: Belongs to the serpin family.

Sequence caution: The sequence CAD62334.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence CAD62585.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.