SERPINA9 Mouse

Serpin Peptidase Inhibitor, Clade A Mouse Recombinant
Cat. No.
BT23766
Source
Sf9, Baculovirus cells.
Synonyms
Serpin A9, Serpina9, SERPINA9.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% 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.
Shipped with Ice Packs
In Stock

Description

SERPINA9 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 401 amino acids (26-418 a.a) and having a molecular mass of 45.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
SERPINA9 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Serpin Peptidase Inhibitor, Clade A Member 9, also known as serpin A9, is a member of the Serpin superfamily of serine protease inhibitors. Serpins are widely distributed protease inhibitors that undergo conformational changes to inhibit target enzymes. They are known to inhibit serine proteases, caspases, and papain-like cysteine proteases. Serpins are conformationally labile, and many disease-linked mutations result in misfolding or the formation of pathogenic, inactive polymers. Serpin A9 inhibits trypsin, thrombin, and plasmin, and it also binds to DNA and heparin.
Description
Recombinant Mouse SERPINA9, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 401 amino acids (26-418 a.a) with a molecular mass of 45.2kDa (appears at approximately 50-70kDa on SDS-PAGE). It has an 8 amino acid His-tag at its C-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
A sterile, colorless solution.
Formulation
The SERPINA9 protein solution (0.25mg/ml) is supplied in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For long-term storage, store frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 85.0% by SDS-PAGE analysis.
Synonyms
Serpin A9, Serpina9, SERPINA9.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
NPYNQESSHL PSMKKNPASQ VSPSNTRFSF LLYQRLAQEN PGQNILFSPV SISTSLAMLS LGARSATKTQ ILRTLGFNFT WVSEPTIHMG FEYLVRSLNK CHQGRELRMG SVLFIRKELQ LQATFLDRVK KLYGAKVFSE DFSNAATAQA QINSYVEKET KGKVVDVIQD LDSQTAMVLV NHIFFKANWT QPFSTANTNK SFPFLLSKGT TVHVPMMHQT ESFAFGVDKE LGCSILQMDY RGDAVAFFVL PGKGKMRQLE KSLSARRLRK WSRSLQKRWI KVFIPKFSIS ASYNLETILP KMGIRDAFNS NADFSGITKT HFLQVSKAAH KAVLDVSEEG TEAAAATTTK LIVRSRDTPS SIIAFKEPFL ILLLDKNTES VLFLGKVENP RKMLEHHHHH H

Product Science Overview

Introduction

Serpin Peptidase Inhibitors are a diverse group of proteins that primarily function as inhibitors of serine proteases. The term “serpin” is derived from their role as serine protease inhibitors. These proteins are found across all kingdoms of life and play crucial roles in various physiological processes, including inflammation, immune response, blood coagulation, and cellular homeostasis .

Serpin Family and Clades

The serpin superfamily is divided into several clades based on sequence similarity. In humans, there are 36 protein-coding serpin genes, while mice have 60 functional serpin genes . The clades are labeled A through P, with clade A being one of the most studied due to its involvement in numerous physiological and pathological processes .

Serpin Peptidase Inhibitor, Clade A

Serpin Peptidase Inhibitor, Clade A, Member 1 (SERPINA1) is a well-known member of this family. It is also known as alpha-1-antitrypsin (AAT) and is a major plasma serine protease inhibitor. SERPINA1 primarily inhibits elastase but also has moderate affinity for other proteases such as trypsin, chymotrypsin, and thrombin . The recombinant form of this protein, derived from mouse models, is used extensively in research to study its function and therapeutic potential.

Mechanism of Action

Serpins function through a unique mechanism known as the “suicide substrate” mechanism. They present a reactive center loop (RCL) that acts as a bait for the target protease. Upon cleavage of the RCL by the protease, the serpin undergoes a significant conformational change, trapping the protease in a covalent complex and thereby inhibiting its activity . This irreversible inhibition is crucial for regulating proteolytic activity in various biological processes.

Applications in Research and Medicine

Recombinant forms of serpin peptidase inhibitors, such as the mouse recombinant SERPINA1, are invaluable tools in biomedical research. They are used to study the molecular mechanisms of protease inhibition, the role of serpins in disease, and their potential as therapeutic agents. For instance, SERPINA1 is being investigated for its role in conditions like chronic obstructive pulmonary disease (COPD) and liver diseases, where its deficiency or dysfunction leads to pathological proteolytic activity .

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