Native Human alpha 1 Antitrypsin protein (ab77937)
Key features and details
- Expression system: Native
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE
Description
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Product name
Native Human alpha 1 Antitrypsin protein
See all alpha 1 Antitrypsin proteins and peptides -
Purity
> 95 % SDS-PAGE. -
Expression system
Native -
Protein length
Full length protein -
Animal free
No -
Nature
Native -
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Species
Human
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab77937 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
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Form
Lyophilized -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid repeated freeze / thaw cycles.
Constituents: 0.492% Sodium phosphate, 1.74% Sodium chloride
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ReconstitutionReconstitute with distilled water. Concentration is lot specific.
General Info
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Alternative names
- A1A
- A1AT
- A1AT_HUMAN
see all -
Function
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). -
Tissue specificity
Ubiquitous. Expressed in leukocytes and plasma. -
Involvement in disease
Alpha-1-antitrypsin deficiency -
Sequence similarities
Belongs to the serpin family. -
Domain
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. -
Post-translational
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 localization
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. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
References (0)
ab77937 has not yet been referenced specifically in any publications.