SERPINB5 Human, His

Serpin Peptidase Inhibitor, Clade B Member 5 Human Recombinant, His tag
Cat. No.
BT24399
Source
Escherichia Coli.
Synonyms
PI5, maspin, SERPINB5, serpin peptidase inhibitor clade B (ovalbumin) member 5, Serpin B5, Protease inhibitor 5.
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.
Shipped with Ice Packs
In Stock

Description

SERPINB5 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 395 amino acids (1-375 a.a.) and having a molecular mass of 44.2 kDa.
The SERPINB5 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
SERPINB5 (Maspin) is a tumor suppressor protein belonging to the serine proteinase inhibitor family. It plays a crucial role in embryonic development due to its critical functions in cell adhesion. Maspin is found in normal breast and prostate epithelial cells but is often downregulated in corresponding carcinomas. It hinders the growth, invasion, and metastasis of mammary tumors and reduces the invasive capacity of pancreatic ductal adenocarcinoma cells. As a breast tumor suppressor gene, SERPINB5 serves as a significant marker for disease progression in breast neoplasms. Additionally, high maspin expression is associated with squamous cell carcinoma in non-small-cell lung cancer. Maspin expression has also been directly linked to the aggressiveness of ovarian carcinoma. Notably, maspin does not exhibit serine protease inhibitory activity because it lacks the typical stressed-to-relaxed conformational transition seen in active serpins.
Description
Recombinant human SERPINB5, with a 20-amino acid His tag at the N-terminus, is produced in E. coli. This single, non-glycosylated polypeptide chain consists of 395 amino acids (residues 1-375) and has a molecular weight of 44.2 kDa. Purification of SERPINB5 is achieved using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The SERPINB5 solution is provided at a concentration of 1 mg/ml and is formulated in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the product should be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To ensure stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. It is important to avoid repeated cycles of freezing and thawing.
Purity
The purity of SERPINB5 is greater than 95.0%, as determined by SDS-PAGE analysis.
Synonyms
PI5, maspin, SERPINB5, serpin peptidase inhibitor clade B (ovalbumin) member 5, Serpin B5, Protease inhibitor 5.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MDALQLANSA FAVDLFKQLC EKEPLGNVLF SPICLSTSLS LAQVGAKGDT ANEIGQVLHF ENVKDVPFGF QTVTSDVNKL SSFYSLKLIK RLYVDKSLNL STEFISSTKR PYAKELETVD FKDKLEETKG QINNSIKDLT DGHFENILAD NSVNDQTKILVVNAAYFVGK WMKKFPESET KECPFRVNKT DTKPVQMMNM EATFCMGNID SINCKIMELP FQNKHLSMFI LLPKDVEDES TGLEKIEKQLNSESLSQWTN PSTMANAKVK LSIPKFKVEK MIDPKACLEN LGLKHIFSED TSDFSGMSET KGVALSNVIH KVCLEITEDG GDSIEVPGAR ILQHKDELNA DHPFIYIIRH NKTRNIIFFG KFCSP.

Product Science Overview

Introduction

Serpin Peptidase Inhibitor, Clade B Member 5, also known as SERPINB5 or Maspin, is a member of the serine protease inhibitor (serpin) family. This family of proteins is known for its role in inhibiting serine proteases, which are enzymes that cleave peptide bonds in proteins. The recombinant form of SERPINB5, tagged with a His (histidine) tag, is used in various research applications to study its function and interactions.

Gene and Protein Structure

The SERPINB5 gene is located on chromosome 18 and encodes a protein that is approximately 42 kDa in size. The protein consists of a single polypeptide chain and does not undergo the typical serpin conformational change from the stressed (S) to the relaxed ® state, which is characteristic of active serpins . This unique feature means that SERPINB5 does not exhibit serine protease inhibitory activity .

Biological Function

SERPINB5 is primarily known for its role as a tumor suppressor. It has been shown to inhibit the growth, invasion, and metastatic properties of mammary tumors . Despite lacking serine protease inhibitory activity, SERPINB5 plays a crucial role in regulating cell adhesion, motility, and apoptosis. It is involved in several biological processes, including extracellular matrix organization, prostate gland morphogenesis, and regulation of epithelial cell proliferation .

Clinical Significance

SERPINB5 has been identified as a biomarker for various cancers, including hepatocellular carcinoma and bone squamous cell carcinoma . Its expression levels are often correlated with the progression and prognosis of these cancers. Additionally, SERPINB5 is being studied for its potential therapeutic applications in cancer treatment due to its tumor-suppressing properties .

Recombinant SERPINB5 with His Tag

The recombinant form of SERPINB5, tagged with a His tag, is produced using recombinant DNA technology. The His tag facilitates the purification and detection of the protein in research studies. This recombinant protein is used in various assays to investigate the molecular mechanisms underlying its tumor-suppressing functions and to identify potential therapeutic targets.

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