Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) corresponding to Human alpha 1 Antitrypsin aa 150-250.
Human plasma, serum, fetal liver and HepG2 lysates.
This product is a recombinant rabbit monoclonal antibody.
We are constantly working hard to ensure we provide our customers with best in class antibodies. As a result of this work we are pleased to now offer this antibody in purified format. We are in the process of updating our datasheets. The purified format is designated "PUR" on our product labels. If you have any questions regarding this update, please contact our Scientific Support team.
Mouse, Rat: We have preliminary internal testing data to indicate this antibody may not react with these species. Please contact us for more information.
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMab® patents
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term.
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.
Detection of alpha 1 Antitrypsin by Western Blot of Immunprecipitate.
Human plasma lysate immunoprecipitated using ab167414 at 1/10 dilution, followed by immunoblotting using HRP-conjugated anti-rabbit IgG preferentially detecting the non-reduced form of rabbit IgG.