catalog number :
MBS143785
products type :
Recombinant Protein
products full name :
Recombinant Human Heat Shock 70kDa protein 9
products short name :
Heat Shock 70kDa protein 9
products name syn :
HSPA9 Human; Heat Shock 70kDa Protein 9 Human Recombinant; 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
other names :
stress-70 protein, mitochondrial; Stress-70 protein, mitochondrial; stress-70 protein, mitochondrial; 75 kDa glucose-regulated protein; catecholamine-regulated protein 40; epididymis secretory sperm binding protein Li 124m; heat shock 70kD protein 9B; mortalin, perinuclear; mortalin-2; p66-mortalin; peptide-binding protein 74; heat shock 70kDa protein 9 (mortalin); 75 kDa glucose-regulated protein; GRP-75; Heat shock 70 kDa protein 9; Mortalin; MOT; Peptide-binding protein 74; PBP74
products gene name :
HSPA9
other gene names :
HSPA9; HSPA9; CSA; MOT; MOT2; CRP40; GRP75; PBP74; GRP-75; HSPA9B; MTHSP75; HEL-S-124m; GRP75; HSPA9B; mt-HSP70; GRP-75; MOT; PBP74
uniprot entry name :
GRP75_HUMAN
purity :
Greater than 95.0% as determined by SDS-PAGE.
form :
The HSPA9 protein solution contains 20mM Tris-HCl, pH-8, 10% glycerol and 0.5mM DTT. Sterile filtered colorless solution.
storage stability :
Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
products categories :
HEAT SHOCK PROTEINS; Recombinant Proteins; Heat Shock Protein
products description :
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. Introduction: HSPA9 is part of the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members that are also called heat-shock cognate proteins. HSPA9 encodes a heat-shock cognate protein that is involved in the control of cell proliferation and acts as a chaperone. HSPA9 was restricted to chromosome 5, band q31, a region that is often deleted in myeloid leukemias and myelodysplasia (MDS), making it a candidate tumor suppressor gene, which is consistent with the biological function of its murine homologue. HSPA9 supresses nuclear translocation, transcriptional activation, and control of centrosome-duplication functions of p53.
ncbi acc num :
NP_004125.3
ncbi gb acc num :
NM_004134.6
ncbi mol weight :
73,680 Da
ncbi pathways :
Metabolism Of Proteins Pathway (106230); Mitochondrial Protein Import Pathway (576261); Parkin-Ubiquitin Proteasomal System Pathway (700638); RNA Degradation Pathway (117291); RNA Degradation Pathway (116127); Tuberculosis Pathway (213780); Tuberculosis Pathway (213743)
ncbi summary :
This gene encodes a member of the heat shock protein 70 gene family. The encoded protein is primarily localized to the mitochondria but is also found in the endoplasmic reticulum, plasma membrane and cytoplasmic vesicles. This protein is a heat-shock cognate protein. This protein plays a role in cell proliferation, stress response and maintenance of the mitochondria. A pseudogene of this gene is found on chromosome 2.[provided by RefSeq, May 2010]
uniprot summary :
HSPA9B: Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone. Interacts with FXN. Interacts with HSCB. Component of the MINOS/MitOS complex, that includes IMMT, HSPA9 and CHCHD3 and associates with mitochondrial outer membrane proteins SAMM50, MTX1 and MTX2. Belongs to the heat shock protein 70 family. Protein type: Nucleolus; Heat shock protein; Chaperone. Chromosomal Location of Human Ortholog: 5q31.1. Cellular Component: focal adhesion; mitochondrion; cytoplasm; nucleolus. Molecular Function: protein binding; ubiquitin protein ligase binding; unfolded protein binding; ATP binding. Biological Process: cellular protein metabolic process; protein folding; protein export from nucleus; protein targeting to mitochondrion; negative regulation of apoptosis