SERPINH1 Human

Heat Shock 47kDa Human Recombinant
Cat. No.
BT19231
Source
Escherichia Coli.
Synonyms
HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% 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

Recombinant Human HSP47 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (18-418 a.a.) and having a molecular mass of 48.9 kDa. HSP47 human recombinant is fused to a 38 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.

Product Specs

Introduction
SERPINH1, a member of the serpin superfamily, acts as a serine proteinase inhibitor. Its expression is induced by heat shock. This protein resides in the endoplasmic reticulum lumen where it functions as a molecular chaperone for collagen. Its role involves facilitating the folding and assembly of procollagen, retaining unfolded molecules within the ER, and guiding correctly folded molecules from the ER to the Golgi apparatus. Autoantibodies targeting HSP47 have been identified in individuals with rheumatoid arthritis. Notably, SERPINH1 exhibits specific binding to collagen, underscoring its chaperone function in collagen biosynthesis.
Description
Recombinant Human HSP47, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 439 amino acids (residues 18-418). With a molecular weight of 48.9 kDa, this recombinant protein is fused to a 38 amino acid His Tag at its N-terminus and purified using standard chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The SERPINH1 protein solution is provided at a concentration of 1mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0) and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the protein should be kept at 4°C. For extended storage, it is recommended to freeze the protein at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. To maintain protein integrity, repeated freeze-thaw cycles should be avoided.
Purity
The purity of the protein is determined to be greater than 90.0% using SDS-PAGE analysis.
Synonyms
HSP47, HSP-47, Colligin-1, CBP1, Collagen Binding Protein-1, Serpin Peptidase Inhibitor Clade-H memebr 1, Serpin H1, Collagen-binding protein, Colligin, 47 kDa heat shock protein, Rheumatoid arthritis-related antigen RA-A47, Arsenic-transactivated protein 3, AsTP3, Cell proliferation-inducing gene 14 protein, SERPINH1, CBP2, gp46, PIG14, PPROM, RA-A47, SERPINH2.
Source
Escherichia Coli.
Amino Acid Sequence

MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAA EVKKPAAAAA PGTAEKLSPK AATLAERSAG LAFSLYQAMA KDQAVENILV SPVVVASSLG LVSLGGKATT ASQAKAVLSA EQLRDEEVHA GLGELLRSLS NSTARNVTWK LGSRLYGPSS VSFADDFVRS SKQHYNCEHS KINFRDKRSA LQSINEWAAQ TTDGKLPEVT KDVERTDGAL LVNAMFFKPH WDEKFHHKMV DNRGFMVTRS YTVGVMMMHR TGLYNYYDDE KEKLQIVEMP LAHKLSSLII LMPHHVEPLE RLEKLLTKEQ LKIWMGKMQK KAVAISLPKG VVEVTHDLQK HLAGLGLTEA IDKNKADLSR MSGKKDLYLA SVFHATAFEL DTDGNPFDQD IYGREELRSP KLFYADHPFI FLVRDTQSGS LLFIGRLVRP KGDKMRDEL.

Product Science Overview

Introduction

Heat Shock Protein 47 (HSP47), also known as Serpin-H1, is a 47 kDa collagen-binding stress protein localized in the endoplasmic reticulum (ER) of collagen-secreting cells . It is a member of the heat shock protein (HSP) family, which are highly conserved proteins that play crucial roles in protein folding and protection against stress-induced damage.

Discovery and Function

Heat shock proteins were first discovered by Ferruccio Ritossa in 1962 when he observed chromosome “puffing” in Drosophila cells exposed to elevated temperatures . HSP47 specifically functions as a molecular chaperone essential for collagen biosynthesis . It binds to procollagen in the ER, ensuring proper folding and preventing premature aggregation .

Role in Collagen Biosynthesis

HSP47 is critical for the stability and secretion of collagen, a major structural protein in the extracellular matrix. It binds to the triple-helical region of procollagen, facilitating its proper folding and transport from the ER to the Golgi apparatus . This process is vital for maintaining the structural integrity of tissues such as skin, bones, and connective tissues.

Clinical Significance

HSP47 has been identified as a potential therapeutic target in various fibrotic conditions, where excessive collagen production leads to tissue scarring and organ dysfunction . Upregulation of HSP47 has been observed in collagen-producing cells in several fibrotic diseases, making it a promising candidate for drug development .

Recombinant HSP47

Recombinant human HSP47 is produced using Chinese Hamster Ovary (CHO) cells and is often tagged with a His-tag for purification purposes . This recombinant protein is used in research to study its role in collagen biosynthesis and its potential as a therapeutic target. It is also utilized in assays to enhance neurite outgrowth in neuronal cells .

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