Key features and details
- FITC Goat polyclonal to alpha 1 Antitrypsin
- Reacts with: Human
- Conjugation: FITC. Ex: 493nm, Em: 528nm
- Isotype: IgG
Product nameFITC Anti-alpha 1 Antitrypsin antibody
See all alpha 1 Antitrypsin primary antibodies
DescriptionFITC Goat polyclonal to alpha 1 Antitrypsin
ConjugationFITC. Ex: 493nm, Em: 528nm
SpecificityBy immunoelectrophoresis and ELISA this antibody reacts specifically with alpha 1 antitrypsin. This antibody may cross react with alpha 1 antitrypsin light chain from other species.
Species reactivityReacts with: Human
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Storage instructionsShipped at 4°C. Store at +4°C.
Storage bufferpH: 6.8
Preservative: 0.1% Sodium azide
Constituents: PBS, 0.2% BSA
Concentration information loading...
PurityImmunogen affinity purified
Purification notesab19170 was isolated by affinity chromatography using antigen coupled to agarose beads and conjugated to fluorescein isothiocyanate (FITC).
FunctionInhibitor 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).
Tissue specificityUbiquitous. Expressed in leukocytes and plasma.
Involvement in diseaseAlpha-1-antitrypsin deficiency
Sequence similaritiesBelongs to the serpin family.
DomainThe 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.
modificationsN-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.
Cellular localizationSecreted. Endoplasmic reticulum. The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum and Secreted, extracellular space, extracellular matrix.
- Information by UniProt
- A1A antibody
- A1AT antibody
- A1AT_HUMAN antibody
ab19170 has been referenced in 4 publications.
- O'Brien ME et al. Activation of complement component 3 is associated with airways disease and pulmonary emphysema in alpha-1 antitrypsin deficiency. Thorax 75:321-330 (2020). PubMed: 31959730
- Bergin DA et al. The circulating proteinase inhibitor a-1 antitrypsin regulates neutrophil degranulation and autoimmunity. Sci Transl Med 6:217ra1 (2014). PubMed: 24382893
- Carroll TP et al. Evidence for unfolded protein response activation in monocytes from individuals with alpha-1 antitrypsin deficiency. J Immunol 184:4538-46 (2010). ICC/IF ; Human . PubMed: 20228200
- Bergin DA et al. a-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8. J Clin Invest 120:4236-50 (2010). ICC/IF, Flow Cyt ; Human . PubMed: 21060150