HSPA9 Human

Heat Shock 70kDa Protein 9 Human Recombinant
Cat. No.
BT18286
Source
Escherichia Coli.
Synonyms
Mortalin, GRP75, MOT2, GSPA9B, PBP74, MOT-2, MTHSP75, Stress-70 protein mitochondrial, 75 kDa glucose-regulated protein, GRP 75, Heat shock 70 kDa protein 9, Peptide-binding protein 74, MOT, HSPA9, HSPA9B, CSA, MGC4500.
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

Recombinant Human HSPA9 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 654 amino acids (47-679) and having a molecular mass of 71 kDa.
HSP9A is expressed with a 20 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
HSPA9, a member of the heat shock protein 70 family, encompasses both heat-inducible and constitutively expressed proteins known as heat-shock cognate proteins. This gene encodes a heat-shock cognate protein that participates in regulating cell proliferation and functions as a chaperone. Notably, HSPA9 is localized to chromosome 5, band q31, a region frequently deleted in myeloid leukemias and myelodysplasia (MDS). This suggests its potential role as a tumor suppressor gene, aligning with the biological function observed in its murine counterpart. HSPA9 demonstrates its regulatory role by suppressing p53's nuclear translocation, transcriptional activation, and control over centrosome duplication.
Description
Recombinant Human HSPA9, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 654 amino acids (47-679). With a molecular weight of 71 kDa, it features a 20 amino acid His tag fused at the N-terminus. The protein is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterilized by filtration.
Formulation
The HSPA9 protein solution is formulated in 20mM Tris-HCl buffer at pH 8, with 10% glycerol and 0.5mM DTT.
Stability
For short-term storage (2-4 weeks), the protein can be stored at 4°C. For extended periods, storage at -20°C in a frozen state is recommended. To ensure long-term stability, adding a carrier protein like 0.1% HSA or BSA is advisable. Repeated freezing and thawing should be avoided.
Purity
The purity of the protein is determined to be greater than 95.0% using SDS-PAGE analysis.
Synonyms
Mortalin, GRP75, MOT2, GSPA9B, PBP74, MOT-2, MTHSP75, Stress-70 protein mitochondrial, 75 kDa glucose-regulated protein, GRP 75, Heat shock 70 kDa protein 9, Peptide-binding protein 74, MOT, HSPA9, HSPA9B, CSA, MGC4500.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASEAIKGAV VGIDLGTTNS CVAVMEGKQA KVLENAEGAR TTPSVVAFTA DGERLVGMPA KRQAVTNPNN TFYATKRLIG RRYDDPEVQK DIKNVPFKIV RASNGDAWVE AHGKLYSPSQ IGAFVLMKMK ETAENYLGHT AKNAVITVPA YFNDSQRQAT KDAGQISGLN VLRVINEPTA AALAYGLDKS EDKVIAVYDL GGGTFDISIL EIQKGVFEVK STNGDTFLGG EDFDQALLRH IVKEFKRETG VDLTKDNMAL QRVREAAEKA KCELSSSVQT DINLPYLTMD SSGPKHLNMK LTRAQFEGIV TDLIRRTIAP CQKAMQDAEV SKSDIGEVIL VGGMTRMPKV QQTVQDLFGR APSKAVNPDE AVAIGAAIQG GVLAGDVTDV LLLDVTPLSL GIETLGGVFT KLINRNTTIP TKKSQVFSTA ADGQTQVEIK VCQGEREMAG DNKLLGQFTL IGIPPAPRGV PQIEVTFDID ANGIVHVSAK DKGTGREQQI VIQSSGGLSK DDIENMVKNA EKYAEEDRRK KERVEAVNMA EGIIHDTETK MEEFKDQLPA DECNKLKEEI SKMRELLARK DSETGENIRQ AASSLQQASL KLFEMAYKKM ASEREGSGSS GTGEQKEDQK EEKQ.

Product Science Overview

Gene and Protein Structure

HSPA9 is encoded by the HSPA9 gene, which is located on chromosome 5, band q31.1 . This region is frequently deleted in myeloid leukemias and myelodysplasia (MDS), suggesting that HSPA9 may function as a tumor suppressor gene . The protein itself has a molecular weight of approximately 71 kDa and consists of 654 amino acids .

Function and Mechanism

HSPA9 functions primarily as a molecular chaperone. It assists in the proper folding of newly synthesized polypeptides, refolding of denatured proteins, and stabilization of native proteins . Additionally, HSPA9 is involved in the inhibition of nuclear translocation, transcriptional activation, and control of centrosome-duplication functions of the p53 protein .

Clinical Significance

Due to its role in protein folding and stress response, HSPA9 is implicated in various diseases, including cancer and autoimmune disorders . Its overexpression has been observed in inflamed tissues, and it has been shown to have immunosuppressive activity by downregulating nuclear factor-kappa B (NF-κB) activation . This makes HSPA9 a potential target for therapeutic interventions in conditions such as rheumatoid arthritis and other autoimmune diseases .

Recombinant HSPA9

Recombinant HSPA9 is produced using Escherichia coli (E. coli) expression systems and is purified using conventional chromatography techniques . The recombinant protein is often tagged with a His-tag at the N-terminus to facilitate purification and detection . It is typically formulated in a buffer containing Tris-HCl, DTT, and glycerol to maintain stability and activity .

Applications

Recombinant HSPA9 is widely used in research to study its function and role in various cellular processes. It is also used in drug discovery and development, particularly in the context of cancer and autoimmune diseases .

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