alpha 1 Antitrypsin Recombinant Rabbit Monoclonal Antibody [JF10-03] (ET1702-87)

UNIPROT #

P01009

PROTEIN NAME

alpha 1 Antitrypsin

SYNONYMS

A1A antibody;A1AT antibody;A1AT_HUMAN antibody;AAT antibody;Alpha 1 antiproteinase antibody;Alpha 1 antitrypsin antibody;Alpha 1 antitrypsin null antibody;Alpha 1 protease inhibitor antibody;Alpha-1 protease inhibitor antibody;Alpha-1-antiproteinase antibody;alpha1 proteinase inhibitor antibody;Alpha1AT antibody;Dom1 antibody;PI antibody;PI1 antibody;PRO2275 antibody;Serine (or cysteine) proteinase inhibitor clade A member 1 antibody;Serine protease inhibitor 1-1 antibody;Serine protease inhibitor A1a antibody;Serpin A1 antibody;Serpin A1a antibody;Serpin peptidase inhibitor clade A member 1 antibody;Serpina1 antibody;Short peptide from AAT antibody;SPAAT antibody;Spi1-1 antibody

SEQUENCE SIMILARITIES

Belongs to the serpin family.

TISSUE SPECIFICITY

Ubiquitous. Expressed in leukocytes and plasma.

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.; Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.; (Microbial infection) Proteolytically processed by Staphylococcus aureus seryl, cysteinyl, and metallo-proteases.

SUBCELLULAR LOCATION

Secreted, Endoplasmic reticulum.

FUNCTION

Alpha-1 antitrypsin or α1-antitrypsin (A1AT, α1AT, A1A, or AAT) is a protein belonging to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. A protease inhibitor, it is also known as alpha1–proteinase inhibitor (A1PI) or alpha1-antiproteinase (A1AP) because it inhibits various proteases (not just trypsin). A1AT is a 52-kDa serpin and, in medicine, it is considered the most prominent serpin; the terms α1-antitrypsin and protease inhibitor (Pi) are often used interchangeably. Most serpins inactivate enzymes by binding to them covalently. These enzymes are released locally in relatively low concentrations where they are immediately cleared by proteins such as A1AT. Besides limiting elastase activity to limit tissue degradation, A1PI also acts to induce locomotion of lymphocytes through tissue including immature T cells through the thymus where immature T cells mature to become immunocompetent T cells that are released into tissue to elevate immune responsiveness. Like all serine protease inhibitors, A1AT has a characteristic secondary structure of beta sheets and alpha helices. Mutations in these areas can lead to non-functional proteins that can polymerise and accumulate in the liver (infantile hepatic cirrhosis).