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AB116604

Anti-alpha 1 Antitrypsin antibody [TMF1 4B5]

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(2 Publications)

Mouse Monoclonal alpha 1 Antitrypsin antibody. Suitable for IP, ELISA, RIA and reacts with Mouse, Human samples. Cited in 2 publications. Immunogen corresponding to Native Full Length Protein corresponding to Human SERPINA1.

View Alternative Names

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

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

TMF1 4B5

Isotype

IgG2a

Carrier free

No

Reacts with

Mouse, Human

Applications

RIA, ELISA, IP

applications

Immunogen

Native Full Length Protein corresponding to Human SERPINA1.

P01009

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Preservative: 0.05% Sodium azide Constituents: PBS, 0.1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
Up to 6 months
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C

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.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

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

BMC microbiology 24:364 PubMed39333864

2024

Fecal microbiota transplantation from patients with polycystic ovary syndrome induces metabolic disorders and ovarian dysfunction in germ-free mice.

Applications

Unspecified application

Species

Unspecified reactive species

Feiling Huang,Yuzhoujia Deng,Miao Zhou,Ruiyi Tang,Peng Zhang,Rong Chen

Analytical chemistry 92:8201-8208 PubMed32426967

2020

Quantitative Analysis of α-1-Antitrypsin Glycosylation Isoforms in HCC Patients Using LC-HCD-PRM-MS.

Applications

Unspecified application

Species

Unspecified reactive species

Haidi Yin,Jianhui Zhu,Mengmeng Wang,Zhong-Ping Yao,David M Lubman
View all publications

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