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AB282404

Recombinant human alpha 1 Antitrypsin protein (Active)

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Recombinant human alpha 1 Antitrypsin protein (Active) is a Human Full Length protein, in the 25 to 418 aa range with >=95% purity, <= 0.005 EU/µg endotoxin level and suitable for SDS-PAGE, Functional studies, mass spectrometry and HPLC. The predicted molecular weight of ab282404 protein is 44.4 kDa.

- Save time and ensure accurate results - use our recombinant alpha 1 Antitrypsin/Serpin A1 protein
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View Alternative Names

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

4 Images
Mass Spectrometry - Recombinant human alpha 1 Antitrypsin protein (Active) (AB282404)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant human alpha 1 Antitrypsin protein (Active) (AB282404)

Mass determination by ESI-TOF.

Predicted MW is 44381.60 Da (+/- 10 Da by ESI-TOF). Observed MW is 44386.58

Functional Studies - Recombinant human alpha 1 Antitrypsin protein (Active) (AB282404)
  • FuncS

Supplier Data

Functional Studies - Recombinant human alpha 1 Antitrypsin protein (Active) (AB282404)

Fully active measured by its ability to inhibit trypsin cleavage of fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2.

ED50 for this effect is ≤18 ng/ml corresponding to a specific activity of 5.55 x 104 units/mg.

Cell based assay testing is performed on the first lot of protein only and is provided as a reference for protein activity; subsequent lots of protein must pass all biophysical quality control parameters that meet the same parameters as the first lot.

Lot GR3396379-2

SDS-PAGE - Recombinant human alpha 1 Antitrypsin protein (Active) (AB282404)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human alpha 1 Antitrypsin protein (Active) (AB282404)

SDS-page analysis of ab282404.

HPLC - Recombinant human alpha 1 Antitrypsin protein (Active) (AB282404)
  • HPLC

Supplier Data

HPLC - Recombinant human alpha 1 Antitrypsin protein (Active) (AB282404)

HPLC analysis of ab282404.

Key facts

Purity

>95% HPLC

Endotoxin level

<0.005 EU/µg

Expression system

HEK 293 cells

Tags

Tag free

Applications

FuncS, SDS-PAGE, HPLC, Mass Spec

applications

Biologically active

Yes

Biological activity

Fully active measured by its ability to inhibit trypsin cleavage of fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2.

ED50 for this effect is ≤18 ng/ml corresponding to a specific activity of 5.55 x 104 units/mg.

Accession

P01009

Animal free

Yes

Carrier free

No

Species

Human

Reconstitution

Reconstitute in PBS

Storage buffer

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

storage-buffer

Reactivity data

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

Product details

Ensure the validity of your result using our recombinant human alpha 1 Antitrypsin protein ab282404 as a control.

The ab282404 alpha 1 Antitrypsin/Serpin A1 protein is sourced from HEK293 cells and can be used as a positive control in SDS-PAGE, mass spectrometry and HPLC.

Check out our protein gel staining guide for SDS-PAGE here

Premium Bioactive Protein range

The ab282404 Serpin A1 protein is part of the premium bioactive protein range which are ideal for preclinical cell culture and functional studies. These recombinant proteins are of the highest activity, purity, and consistency, meeting rigorous biophysical characterization.

More premium bioactive proteins can be found here

Sequence info

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

Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
Ambient
Appropriate long-term storage conditions
Ambient
True

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.

Specifications

Form

Lyophilized

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.

Product protocols

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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