SERPINA3
Alpha-1 AntiChymotrypsin Human Recombinant
Cat. No.
BT22806
Source
Escherichia Coli.
Synonyms
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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
SERPINA3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 421 amino acids (24-423 a.a.) and having a molecular mass of 47.6 kDa.
The SERPINA3 is purified by proprietary chromatographic techniques.
The SERPINA3 is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Alpha 1 ACT, also known as Alpha-1-antichymotrypsin (Alpha-1-ACT), is an early-stage acute-phase plasma protein belonging to the serpin family. Its primary function is to inhibit chymotrypsin, cathepsin G, and chymase, all of which are serine proteases. Alpha-1-ACT plays a crucial role in regulating serine protease activity, which is essential for various physiological processes. Studies have shown a strong association between Alpha-1-ACT and amyloid plaques in Alzheimer's disease (AD), as well as in the brains of aging humans and monkeys. This suggests its potential involvement in the pathogenesis of AD. Furthermore, Alpha-1-ACT is known to form complexes with prostate-specific antigen (PSA), a chymotrypsin-like serine protease, highlighting its significance in prostate health.
Description
This product consists of recombinant human SERPINA3, containing a 20 amino acid His tag fused at its N-terminus. It is produced in E.Coli and exists as a single, non-glycosylated polypeptide chain with a molecular weight of 47.6 kDa. The protein encompasses 421 amino acids, spanning from residue 24 to 423. Purification of SERPINA3 is achieved using proprietary chromatographic techniques, resulting in a highly pure product.
Physical Appearance
Clear and colorless solution, sterilized by filtration.
Formulation
The SERPINA3 solution is formulated in a buffer containing 20mM Tris-HCl (pH 8), 1mM DTT (dithiothreitol), and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the SERPINA3 solution should be kept at 4°C. For extended storage, it is recommended to store the solution at -20°C. To further enhance stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advisable. Repeated freezing and thawing of the solution should be avoided to maintain protein integrity.
Purity
The purity of SERPINA3 is determined by SDS-PAGE analysis and is guaranteed to be greater than 95%. This high level of purity ensures the quality and reliability of the product for various research applications.
Synonyms
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MHPNSPLDEE NLTQENQDRG THVDLGLASA NVDFAFSLYK QLVLKAPDKN VIFSPLSIST ALAFLSLGAH NTTLTEILKG LKFNLTETSE AEIHQSFQHL LRTLNQSSDE LQLSMGNAMF VKEQLSLLDR FTEDAKRLYG SEAFATDFQD SAAAKKLIND YVKNGTRGKI TDLIKDLDSQ TMMVLVNYIF FKAKWEMPFD PQDTHQSRFY LSKKKWVMVP MMSLHHLTIP YFRDEELSCT VVELKYTGNA SALFILPDQD KMEEVEAMLL PETLKRWRDS LEFREIGELY LPKFSISRDY NLNDILLQLG IEEAFTSKAD LSGITGARNL AVSQVVHKAV LDVFEEGTEA SAATAVKITL LSALVETRTI VRFNRPFLMI IVPTDTQNIF FMSKVTNPKQ A.
Product Science Overview
Structure and Function
AACT is composed of 423 amino acids and has a molecular weight of approximately 47.651 kDa . The protein structure includes an α-helix, β-folded sheets, and a reaction center loop (RCL) . As a serine protease inhibitor, AACT inhibits enzymes such as neutrophil cathepsin G and mast cell chymase, protecting cells and tissues from damage caused by proteolysis during inflammation .
Biological Roles
AACT is involved in various biological processes, including:
- Acute Phase Response: AACT levels increase during inflammation, helping to regulate the body’s response to injury or infection .
- Proteolysis Inhibition: By inhibiting proteases, AACT helps maintain intracellular homeostasis and extracellular matrix reconstruction .
- Tumor Progression and Recurrence: Dysregulation of AACT and its glycosylation levels are associated with tumor progression and recurrence, making it a potential biomarker for tumor monitoring .
Clinical Significance
AACT has been linked to several clinical conditions:
- Inflammatory Diseases: Elevated levels of AACT are observed in inflammatory conditions such as Crohn’s disease, ulcerative colitis, and burn injuries .
- Cancer: AACT expression levels can serve as diagnostic or prognostic biomarkers in various cancers. For example, decreased AACT expression is associated with poor survival in liver cancer patients, while increased expression is linked to shorter survival in pancreatic cancer patients .
- Neurodegenerative Diseases: AACT is associated with the pathogenesis of Alzheimer’s disease, as it enhances the formation of amyloid-fibrils .
Recombinant AACT
Human recombinant AACT is produced using recombinant DNA technology, allowing for the large-scale production of this protein for research and therapeutic purposes. Recombinant AACT retains the same structural and functional properties as the naturally occurring protein, making it a valuable tool in studying its biological roles and potential therapeutic applications.
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