Abcam’s Alpha 1 Antitrypsin (SERPINA1) Dog ELISA kit is an in vitro enzyme-linked immunosorbent assay (ELISA) for the quantitative measurement of Alpha 1 Antitrypsin in biological samples of Dog.
In this assay the Alpha 1 Antitrypsin present in samples reacts with the anti- Alpha 1 Antitrypsin antibodies which have been adsorbed to the surface of polystyrene microtiter wells. After the removal of unbound proteins by washing, anti- Alpha 1 Antitrypsin antibodies conjugated with horseradish peroxidase (HRP), are added. These enzyme-labeled antibodies form complexes with the previously bound Alpha 1 Antitrypsin. Following another washing step, the enzyme bound to the immunosorbent is assayed by the addition of a chromogenic substrate, 3,3’,5,5’-tetramethylbenzidine (TMB). The quantity of bound enzyme varies directly with the concentration of Alpha 1 Antitrypsin in the sample tested; thus, the absorbance, at 450 nm, is a measure of the concentration of Alpha 1 Antitrypsin in the test sample. The quantity of Alpha 1 Antitrypsin in the test sample can be interpolated from the standard curve constructed from the standards, and corrected for sample dilution.
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. Short 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).
Ubiquitous. Expressed in leukocytes and plasma.
Involvement in disease
Belongs to the serpin family.
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.
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.
Secreted. Endoplasmic reticulum. The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum and Secreted, extracellular space, extracellular matrix.