71 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using NBC1-18380 in the following applications:
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
20 mM Tris-HCl buffer (pH 8.0), 0.5 MM DTT, 10% glycerol
Preservative
No Preservative
Concentration
1 mg/ml
Purity
>95%, by SDS-PAGE
Alternate Names for Recombinant Human GRP75/HSPA9B/Mortalin His Protein
75 kDa glucose-regulated protein
CSA
GRP75
GRP-75
GRP75mthsp75
Heat shock 70 kDa protein 9
heat shock 70kD protein 9B
heat shock 70kDa protein 9 (mortalin)
heat shock 70kDa protein 9B (mortalin-2)
HSPA9
HSPA9B
HSPA9BMGC4500
Mortalin
mortalin, perinuclear
Mortalin-2
MOT
MOT2
mot-2
MTHSP75
p66-mortalin
PBP74
PBP74CSA
Peptide-binding protein 74
stress-70 protein, mitochondrial
Background
HSPA9 belongs to the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members. HSPA9 was localized to chromosome 5, band q31, a region that is frequently 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. Also it inhibits nuclear translocation, transcriptional activation, and control of centrosome-duplication functions of p53. Recombinant human HSPA9 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.
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