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AB283932

Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein

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Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein is a Human Full Length protein, in the 25 to 418 aa range, expressed in HEK 293 cells, <0.005 EU/µg endotoxin level, suitable for SDS-PAGE, Mass Spec, HPLC.

View Alternative Names

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

3 Images
Mass Spectrometry - Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein (AB283932)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein (AB283932)

ESI TOF analysis of ab283932.

Predicted MW is 44381.60 Da (+/1 10 Da by ESI TOF). Observed MW is 44385.50 Da.

HPLC - Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein (AB283932)
  • HPLC

Supplier Data

HPLC - Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein (AB283932)

HPLC analysis of ab283932.

SDS-PAGE - Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein (AB283932)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Serpin A1/alpha-1-Antitrypsin Protein (AB283932)

SDS-PAGE analysis of ab283932.

Key facts

Purity

undefined SDS-PAGE

Purity by HPLC =95%

Endotoxin level

<0.005 EU/µg

Expression system

HEK 293 cells

Tags

Tag free

Applications

Mass Spec, SDS-PAGE, HPLC

applications

Biologically active

No

Accession

P01009

Animal free

Yes

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 10.26% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic

storage-buffer

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Reagents, Controls & Accessories

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Prestained Protein Ladder - Broad molecular weight (11-250 kDa, 5-color, 11 bands)

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Primary Antibodies

AB207303

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Assay Kits

AB118971

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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>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"linker":null,"sequence":"EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK","proteinLength":"Full Length","predictedMolecularWeight":"44.38 kDa","actualMolecularWeight":"44.39 kDa","aminoAcidEnd":418,"aminoAcidStart":25,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P01009","tags":[]}]
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Properties and storage information

Form
Lyophilized
Shipped at conditions
Ambient - Can Ship with Ice
Appropriate long-term storage conditions
Ambient
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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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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