HSCB Human

HscB Iron-Sulfur Cluster Co-Chaperone Human Recombinant
Cat. No.
BT15305
Source
E.coli.
Synonyms
HscB iron-sulfur cluster co-chaperone homolog (E. coli), DnaJ homolog (Hsp40) subfamily C member 20, iron-sulfur cluster co-chaperone protein HscB mitochondrial, J-type co-chaperone HSC20, DNAJC20, HSC20, dJ366L4.2, JAC1.
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

HSCB Human Recombinant produced in E. coli is a single polypeptide chain containing 231 amino acids (30-235) and having a molecular mass of 26.7 kDa.
HSCB is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
The HscB Iron-Sulfur Cluster Co-Chaperone (HSCB), a member of the hscB family, plays a crucial role in iron-sulfur cluster assembly within mitochondria. This protein, containing a single J domain, exhibits widespread expression in various tissues including the lungs, brain, stomach, spleen, ovaries, testes, liver, muscles, and heart. Located in both the mitochondria and cytoplasm, HSCB functions as a co-chaperone, interacting with ISCU and HSPA9 to facilitate the assembly of iron-sulfur clusters.
Description
This recombinant HSCB protein, expressed in E. coli, is a single polypeptide chain consisting of 231 amino acids (residues 30-235). With a molecular weight of 26.7 kDa, it includes a 25 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
The product is a sterile, colorless solution that has been filtered for purity.
Formulation
The HSCB solution is provided at a concentration of 1mg/ml and is formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 150mM NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to store the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the HSCB protein is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms
HscB iron-sulfur cluster co-chaperone homolog (E. coli), DnaJ homolog (Hsp40) subfamily C member 20, iron-sulfur cluster co-chaperone protein HscB mitochondrial, J-type co-chaperone HSC20, DNAJC20, HSC20, dJ366L4.2, JAC1.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAASQA GSNYPRCWNC GGPWGPGRED RFFCPQCRAL QAPDPTRDYF SLMDCNRSFR VDTAKLQHRY QQLQRLVHPD FFSQRSQTEK DFSEKHSTLV NDAYKTLLAP LSRGLYLLKL HGIEIPERTD YEMDRQFLIE IMEINEKLAE AESEAAMKEI ESIVKAKQKE FTDNVSSAFE QDDFEEAKEI LTKMRYFSNI EEKIKLKKIP L

Product Science Overview

Introduction

The HscB Iron-Sulfur Cluster Co-Chaperone, also known as Human Recombinant HscB, is a highly conserved mitochondrial protein that plays a crucial role in the assembly and maintenance of iron-sulfur (Fe-S) clusters. These clusters are essential cofactors involved in various biochemical processes, including electron transport, enzyme catalysis, and regulation of gene expression. HscB is a member of the heat shock cognate B (HscB) family of proteins and functions as a co-chaperone in the iron-sulfur cluster assembly machinery.

Function and Mechanism

HscB primarily interacts with the scaffold protein IscU and the chaperone protein HSPA9 (also known as mortalin or GRP75). The interaction between HscB and IscU is critical for the successful assembly of Fe-S clusters. HscB facilitates the transfer of nascent Fe-S clusters from IscU to target apoproteins by stimulating the ATPase activity of HSPA9 . This process ensures the proper incorporation of Fe-S clusters into recipient proteins, which is vital for their functional activity.

Structural Insights

The solution structure of HscB has been extensively studied using nuclear magnetic resonance (NMR) spectroscopy. These studies have revealed that HscB consists of a J-domain, a linker region, and a C-domain. The J-domain is responsible for binding to HSPA9, while the C-domain interacts with IscU . The conserved patch of residues in the C-domain is the principal binding site for IscU, and mutations in this region can significantly affect the binding affinity and functional activity of HscB .

Biological Significance

HscB is essential for mitochondrial iron-sulfur cluster biogenesis, a process that is evolutionarily conserved across species. In humans, defects in the HscB gene can lead to various mitochondrial disorders, including congenital sideroblastic anemia (CSA). CSA is characterized by the presence of ringed sideroblasts in the bone marrow, resulting from impaired heme biosynthesis and mitochondrial iron metabolism . Mutations in HscB can disrupt the assembly of Fe-S clusters, leading to defective mitochondrial function and cellular iron homeostasis .

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