SERPINA1 Human
Alpha 1 Antitrypsin Human Recombinant
Cat. No.
BT22641
Source
Escherichia Coli.
Synonyms
Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
SERPINA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (25-418) and having a molecular mass of 44.4 kDa.
The SERPINA1 protein is purified by proprietary chromatographic techniques.
The SERPINA1 protein is purified by proprietary chromatographic techniques.
Product Specs
Introduction
SERPINA1, a secreted serine protease inhibitor, targets various enzymes including elastase, plasmin, collagenase, thrombin, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Genetic defects in SERPINA1 can lead to emphysema or liver disease. Notably, H. pylori infection specifically induces SERPINA1 expression in the antrum. Elevated serum levels of SERPINA1 are observed in lung and prostate cancers compared to healthy individuals, while breast cancer patients do not exhibit significant changes. Functionally, SERPINA1 acts as an endogenous inhibitor of serine proteases, demonstrating in vitro inhibition of human recombinant matriptase's catalytic domain. Tissue necrosis and inflammation trigger an acute phase response characterized by increased SERPINA1 levels. Mutations in SERPINA1 and SLC11A1 genes can disrupt the balance of elastase produced by leukocytes during phagocytosis.
Description
Recombinant human SERPINA1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 395 amino acids (residues 25-418). With a molecular weight of 44.4 kDa, this protein is purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The SERPINA1 protein is supplied in a solution containing 20mM Tris-HCl (pH 7.5), 1mM DTT, 10% glycerol, and 2mM EDTA.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
The purity of this protein is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms
Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330.
Source
Escherichia Coli.
Amino Acid Sequence
MEDPQGDAAQ KTDTSHHDQD HPTFNKITPN LAEFAFSLYR QLAHQSNSTN IFFSPVSIAT AFAMLSLGTK ADTHDEILEG LNFNLTEIPE AQIHEGFQEL LRTLNQPDSQ LQLTTGNGLF LSEGLKLVDK FLEDVKKLYH SEAFTVNFGD TEEAKKQIND YVEKGTQGKI VDLVKELDRD TVFALVNYIF FKGKWERPFE VKDTEEEDFH VDQVTTVKVP MMKRLGMFNI QHCKKLSSWV LLMKYLGNAT AIFFLPDEGK LQHLENELTH DIITKFLENE DRRSASLHLP KLSITGTYDL KSVLGQLGIT KVFSNGADLS GVTEEAPLKL SKAVHKAVLT IDEKGTEAAG AMFLEAIPMS IPPEVKFNKP FVFLMIDQNT KSPLFMGKVV NPTQK.
Product Science Overview
Recombinant Alpha 1 Antitrypsin
Recombinant Alpha 1 Antitrypsin (rAAT) is produced using recombinant DNA technology, typically in yeast cells. This method eliminates the risk of blood-borne infectious agents associated with plasma-derived AAT and allows for increased manufacturing efficiency . Recombinant AAT belongs to the family of serine protease inhibitors (SERPINS) and inhibits several proteases, including trypsin, cathepsin G, thrombin, tissue kallikrein, and neutrophil elastase .
Therapeutic Applications
Recombinant AAT is used in the treatment of AATD to supplement the deficient protein and control neutrophil elastase activity in the lungs. This therapy aims to prevent or slow the progression of lung damage and improve respiratory function . Studies have shown that recombinant AAT can provide greater protection against lung dysfunction and inflammation compared to plasma-derived AAT .
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