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AB79181

Recombinant Human alpha 1 Antitrypsin protein (Tag Free)

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Recombinant Human alpha 1 Antitrypsin protein (Tag Free) is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

AAT, PI, PRO0684, PRO2209, SERPINA1, Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, Serpin A1

1 Images
SDS-PAGE - Recombinant Human alpha 1 Antitrypsin protein (Tag Free) (AB79181)
  • SDS-PAGE

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SDS-PAGE - Recombinant Human alpha 1 Antitrypsin protein (Tag Free) (AB79181)

15% SDS-PAGE showing ab79181 at approximately 44kDa (3μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P01009

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 10% Glycerol (glycerin, glycerine), 0.242% Tris, 0.0584% EDTA, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIDQNTKSPLFMGKVVNPTQK","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P01009","tags":[]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Alpha 1 Antitrypsin also known as A1AT or alpha-1 proteinase inhibitor is a serine protease inhibitor with a molecular mass of about 52 kDa. This protein mainly expresses in the liver and found in high concentrations in the blood plasma. A1AT protects tissues from enzymes of inflammatory cells especially neutrophil elastase. Its expression level is regulated by the liver making it a significant player in maintaining tissue integrity.
Biological function summary

A1AT regulates protease activity by forming complexes with target enzymes. It specifically inhibits neutrophil elastase a powerful enzyme capable of degrading elastin an important component of connective tissues. A1AT prevents excessive tissue damage during inflammation by maintaining a balance in protease activity within connective tissues across various organs.

Pathways

Alpha 1 Antitrypsin functions within the proteolytic pathways involved in inflammatory response and tissue remodeling. A1AT is closely related to neutrophil elastase in these processes. It interacts with other protease inhibitors like alpha 2-macroglobulin reinforcing its protective role against enzymatic activity that can lead to tissue destruction under pathophysiological conditions.

Alpha 1 Antitrypsin deficiency is a genetic condition that can cause chronic obstructive pulmonary disease (COPD) and liver cirrhosis. Deficient A1AT levels result in unregulated elastase activity leading to lung tissue damage and impaired liver function. Other proteins such as MMP-9 collaborate with elastase in exacerbating tissue damage illustrating how insufficient A1AT can significantly contribute to disease development.
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Specifications

Form

Liquid

Additional notes

ab79181 is purified using conventional chromatography techniques.

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General info

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).

Sequence similarities

Belongs to the serpin family.

Post-translational modifications

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.. (Microbial infection) Proteolytically processed by Staphylococcus aureus seryl, cysteinyl, and metallo-proteases.

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Product protocols

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Target data

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).
See full target information SERPINA1
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