Product nameAnti-alpha 1 Antitrypsin antibody [EPSISR16]
See all alpha 1 Antitrypsin primary antibodies
DescriptionRabbit monoclonal [EPSISR16] to alpha 1 Antitrypsin
Tested applicationsSuitable for: WB, IPmore details
Unsuitable for: IHC-P
Species reactivityReacts with: Mouse, Rat, Human
Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) (internal sequence)
- Human platelet, fetal kidney and plasma lysates
Storage instructionsShipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Storage bufferpH: 7.20
Preservative: 0.01% Sodium azide
Constituents: 9% PBS, 40% Glycerol, 0.05% BSA, 50% Tissue culture supernatant
PurityTissue culture supernatant
Our Abpromise guarantee covers the use of ab133642 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/1000 - 1/10000. Predicted molecular weight: 46 kDa.|
|IP||1/10 - 1/100.|
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
All lanes : Anti-alpha 1 Antitrypsin antibody [EPSISR16] (ab133642) at 1/1000 dilution
Lane 1 : Human platelet lysate
Lane 2 : Fetal kidney lysate
Lane 3 : Human plasma lysate
Lysates/proteins at 10 µg per lane.
All lanes : HRP labelled goat anti-rabbit at 1/2000 dilution
Predicted band size: 46 kDa
This product has been referenced in:
- Cao J et al. Protein markers of dysfunctional HDL in scavenger receptor class B type I deficient mice. J Transl Med 16:155 (2018). WB ; Mouse . Read more (PubMed: 29879989) »
- Liu R et al. Comparative study of serum proteomes in Legg-Calve-Perthes disease. BMC Musculoskelet Disord 16:281 (2015). WB . Read more (PubMed: 26438379) »