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Human Alpha 1 Antitrypsin
Native biologically active whole molecule
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Proteins Synonyms: Alpha-1 protease inhibitor, Alpha-1-antiproteinase, Alpha 1 Protease Inhibitor, Serpin A1, A1PI, A1AT, AAT, PI, PRO0684, PRO2209 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. Source: Human Plasma Purity: ≥ 95% by SDS-PAGE Physical State: Lyophilized from 30 mM Na phosphate, pH 6.5, with 300 mM NaCl Manufacturer: |
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Athens Research & Technology
Produktdetails
Synonyms
Alpha-1 protease inhibitor, Alpha-1-antiproteinase, Alpha 1 Protease Inhibitor, Serpin A1, A1PI, A1AT, AAT, PI, PRO0684, PRO2209
Description of Human Alpha 1 Antitrypsin
Human Alpha 1 Antitrypsin is a 52 kDa protein. Alpha-1 antitrypsin is a glycoprotein primarily produced by the liver and circulates in plasma at concentrations of 95–350 mg per 100 ml. As a member of the serpin superfamily, A1AT’s main function is to protect tissues, especially in the lungs, from proteolytic damage by inhibiting enzymes such as neutrophil elastase. By binding to and inactivating elastase, A1AT prevents the breakdown of elastin in connective tissue, thereby preserving lung structure and function. Deficiency of A1AT, most often due to mutations in the SERPINA1 gene, leads to unregulated elastase activity. This can cause early-onset pulmonary emphysema and chronic obstructive pulmonary disease (COPD), as well as juvenile or adult liver cirrhosis due to accumulation of abnormal A1AT in the liver. Less commonly, deficiency can result in skin disorders like panniculitis. Clinically, A1AT levels rise during inflammation, malignancy, liver disease, pregnancy, after surgery, and with oral contraceptive use. Measurement of A1AT, often alongside ceruloplasmin, aids in distinguishing different liver disorders. Therapeutically, purified A1AT is used for augmentation therapy in individuals with severe deficiency, and research continues into its broader anti-inflammatory and immunomodulatory applications.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
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.
Storage
For long term, store Human Alpha 1 Antitrypsin at ≤ -20°C.
Applications
Proteolytic Inhibition studies, Antibody detection, ELISA Standards, Potein Structure Studies, A1AT deficiency research, Antisera Production, In Vitro Diagnostics.
Citations/Publications
Schevenels, G., et al., (2024), 'A brain-specific angiogenic mechanism enabled by tip cell specialization', Nature, 628: pp 863-871. Available at https://doi.org/10.1038/s41586-024-07283-6
Hiroyuki, M. et al., (2024), 'Hair follicle aging is driven by transepidermal elimination of stem cells via COL17A1 proteolysis', Science 351: aad4395. Available at DOI:10.1126/science.aad4395
Cui, C., et al., (2021), 'Neutrophil elastase selectively kills cancer cells and attenuates tumorigenesis', Cell, 184: pp 3163–3177. Available at https://doi.org/10.1016/j.cell.2021.04.016
Geiger, S., et al., (2019), 'Alpha-1 Antitrypsin-Expressing Mesenchymal Stromal Cells Confer a Long-Term Survival Benefit in a Mouse Model of Lethal GvHD', Molecular Therapy, 27(8): pp 1436-1451. Available at https://doi.org/10.1016/j.ymthe.2019.05.007
Borel, F., et al., (2017), 'Survival Advantage of Both Human Hepatocyte Xenografts and Genome-Edited Hepatocytes for Treatment of a-1 Antitrypsin Deficiency', Molecular Therapy, 25(11): pp 2477 - 2489. Available at DOI: 10.1016/j.ymthe.2017.09.020
NCBI: https://www.ncbi.nlm.nih.gov/protein/P01009/
Shipped with ice packs
Gel Scan of Human Alpha 1 Antitrypsin
| Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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