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AB91136

Native human alpha 1 Antitrypsin protein (Active)

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(2 Publications)

Native human alpha 1 Antitrypsin protein (Active) is a Human Full Length A1AT/SERPIN A1 protein, with >95% purity and suitable for western blot , SDS-PAGE and Functional studies. The predicted molecular weight of ab91136 native protein is 52 kDa.

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View Alternative Names

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

2 Images
Western blot - Native human alpha 1 Antitrypsin protein (Active) (AB91136)
  • WB

Unknown

Western blot - Native human alpha 1 Antitrypsin protein (Active) (AB91136)

All lanes:

Western blot - Anti-alpha 1 Antitrypsin antibody [B9] (<a href='/en-us/products/primary-antibodies/alpha-1-antitrypsin-antibody-b9-ab9399'>ab9399</a>) at 1 µg/mL

All lanes:

Western blot - Native human alpha 1 Antitrypsin protein (Active) (ab91136) at 0.1 µg

Secondary

All lanes:

Western blot - Goat Anti-Mouse IgG H&L (HRP) preadsorbed (<a href='/en-us/products/secondary-antibodies/goat-mouse-igg-h-l-hrp-preadsorbed-ab97040'>ab97040</a>) at 1/5000 dilution

Predicted band size: 46 kDa

true

Exposure time: 30s

SDS-PAGE - Native human alpha 1 Antitrypsin protein (Active) (AB91136)
  • SDS-PAGE

Unknown

SDS-PAGE - Native human alpha 1 Antitrypsin protein (Active) (AB91136)

SDS-PAGE : 4-12% Bis-Tris NuPAGE gel

Lane 1. 5 μg ab91136 (reduced/heated)
Lane 2. 10 μg ab91136 (reduced/heated)
Lane 3. 20 μg ab91136 (reduced/heated)
Lane 4. Molecular weight markers
Lane 5. 5 μg ab91136 (non-reduced/no heat)
Lane 6. 10 μg ab91136 (non-reduced/no heat)
Lane 7. 20 μg ab91136 (non-reduced/no heat)

Key facts

Purity

>95% SDS-PAGE

Expression system

Native

Tags

Tag free

Applications

SDS-PAGE, FuncS, WB

applications

Biologically active

Yes

Biological activity

When tested with active-site titrated porcine pancreatic trypsin using Na-Benzoyl-L-Arginine-para-Nitroanilide Hydrochloride (L-BAPNA) as substrate, it is 75-100% inhibitory.

Accession

P01009

Animal free

No

Carrier free

Yes

Species

Human

Reconstitution

Reconstitute in water

Storage buffer

pH: 6.5 Constituents: 1.74% Sodium chloride, 0.492% Sodium phosphate

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>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>ab91136 can be used as a WB positive control in conjunction with <a href='/en-us/products/primary-antibodies/alpha-1-antitrypsin-antibody-b9-ab9399'>ab9399</a>.</p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

The Native human alpha 1 Antitrypsin protein (Active) ab91136 is prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.

Ensure the validity of your result using our native human alpha 1 Antitrypsin (A1AT/SERPIN A1) protein as a control in SDS-PAGE.

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

Protein Determination: Extinction Coefficient (ε) 0.1% at 280 nm, 1 cm pathway = 0.433

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"52 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Native","expressionSystem":null,"accessionNumber":"P01009","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
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

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Nature genetics 51:1233-1243 PubMed31358993

2019

CELA2A mutations predispose to early-onset atherosclerosis and metabolic syndrome and affect plasma insulin and platelet activation.

Applications

Unspecified application

Species

Unspecified reactive species

Fatemehsadat Esteghamat,James S Broughton,Emily Smith,Rebecca Cardone,Tarun Tyagi,Mateus Guerra,András Szabó,Nelson Ugwu,Mitra V Mani,Bani Azari,Gerald Kayingo,Sunny Chung,Mohsen Fathzadeh,Ephraim Weiss,Jeffrey Bender,Shrikant Mane,Richard P Lifton,Adebowale Adeniran,Michael H Nathanson,Fred S Gorelick,John Hwa,Miklós Sahin-Tóth,Renata Belfort-DeAguiar,Richard G Kibbey,Arya Mani

Journal of neuroinflammation 14:168 PubMed28835277

2017

Prophylactic inhibition of neutrophil elastase prevents the development of chronic neuropathic pain in osteoarthritic mice.

Applications

Unspecified application

Species

Unspecified reactive species

Milind M Muley,Eugene Krustev,Allison R Reid,Jason J McDougall
View all publications

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