alpha 1 Antitrypsin Rabbit Polyclonal Antibody (R1103-1)

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

FUNCTION

Alpha 1-Antitrypsin is a inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. It 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. Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD). 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.