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Heat Shock 70kDa Protein 9 (Mortalin) (HSPA9) (AA 551-766) antibody

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AA 551-766
Caenorhabditis elegans (C. elegans), Human, Mouse (Murine), Rat (Rattus)
Clonality (Clone)
Monoclonal ()
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
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Immunogen Fusion protein amino acids 551-766 of mouse SALM2.
Clone S52A-42
Specificity Detects ~75 kDa.
Sensitivity 1 µg/ml was sufficient for detection of Grp75 in 10 µg of heat shock HeLa lysate by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.
Purification Protein G Purified
Background Grp75, also known as mortalin, is a member of HSP70 family of chaperone proteins that is not heat inducible (1, 2). Grp75 is actually induced under conditions of low glucose and other nutritional and environmental stresses. Grp75 resides primarily in the mitochondrial matrix, where it collaborates with HSP60 in the re-folding of proteins translocated into this organelle (3, 4). Related forms may also be found in the cytosol or on the surface of the extracellular membrane. Other Grp75 functions include its ability to inactivate the tumor suppressor p53 (5). Studies have found that Grp75 is over-expressed in many tumor tissues and immortalized human cell lines, suggesting its role in the tumor formation (6). Grp75 is also implicated in cell aging, as its overexpression appears to prolong the life span of human fibroblasts (7). And finally, like its E.coli homolog DnaK (8), GRP75 possesses a cation-dependent ATPase activity considered central to its function as a chaperone (9, 10).
Cellular Localization: Mitochondrion
Gene ID 3313
NCBI Accession NP_004125
UniProt P38646
Application Notes Recommended Dilution: WB (1:1000), ICC/IF (1:200), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-Heat Shock 70kDa Protein 9 (Mortalin) (HSPA9) (AA 551-766) antibody (ABIN361739) Grp75(S52A 42) human cell lines mix.
Product cited in: Saar Ray, Moskovich, Iosefson et al.: "Mortalin/GRP75 binds to complement C9 and plays a role in resistance to complement-dependent cytotoxicity." in: The Journal of biological chemistry, Vol. 289, Issue 21, pp. 15014-22, 2014 (PubMed).

Rozenberg, Kocsis, Saar et al.: "Elevated levels of mitochondrial mortalin and cytosolic HSP70 in blood as risk factors in patients with colorectal cancer." in: International journal of cancer. Journal international du cancer, Vol. 133, Issue 2, pp. 514-8, 2013 (PubMed).

Background publications Wadhwa, Takano, Kaur et al.: "Upregulation of mortalin/mthsp70/Grp75 contributes to human carcinogenesis." in: International journal of cancer. Journal international du cancer, Vol. 118, Issue 12, pp. 2973-80, 2006 (PubMed).

Kaul, Yaguchi, Taira et al.: "Overexpressed mortalin (mot-2)/mthsp70/GRP75 and hTERT cooperate to extend the in vitro lifespan of human fibroblasts." in: Experimental cell research, Vol. 286, Issue 1, pp. 96-101, 2003 (PubMed).

Wadhwa, Takano, Robert et al.: "Inactivation of tumor suppressor p53 by mot-2, a hsp70 family member." in: The Journal of biological chemistry, Vol. 273, Issue 45, pp. 29586-91, 1998 (PubMed).

Kaul, Wadhwa, Komatsu et al.: "On the cytosolic and perinuclear mortalin: an insight by heat shock." in: Biochemical and biophysical research communications, Vol. 193, Issue 1, pp. 348-55, 1993 (PubMed).

Wadhwa, Kaul, Ikawa et al.: "Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype." in: The Journal of biological chemistry, Vol. 268, Issue 9, pp. 6615-21, 1993 (PubMed).

Schneider, Berthold, Bauer et al.: "Mitochondrial Hsp70/MIM44 complex facilitates protein import." in: Nature, Vol. 371, Issue 6500, pp. 768-74, 1994 (PubMed).

Leustek, Dalie, Amir-Shapira et al.: "A member of the Hsp70 family is localized in mitochondria and resembles Escherichia coli DnaK." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 86, Issue 20, pp. 7805-8, 1989 (PubMed).

Manning-Krieg, Scherer, Schatz: "Sequential action of mitochondrial chaperones in protein import into the matrix." in: The EMBO journal, Vol. 10, Issue 11, pp. 3273-80, 1991 (PubMed).

Liberek, Skowyra, Zylicz et al.: "The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein." in: The Journal of biological chemistry, Vol. 266, Issue 22, pp. 14491-6, 1991 (PubMed).

Mizzen, Kabiling, Welch: "The two mammalian mitochondrial stress proteins, grp 75 and hsp 58, transiently interact with newly synthesized mitochondrial proteins." in: Cell regulation, Vol. 2, Issue 2, pp. 165-79, 1991 (PubMed).