Anti-Grp75 Antibody
S52A-42__Mouse Anti-Mouse Grp75 Monoclonal IgG1 Dolutegravir (sodium)
Storage Buffer
PBS pH7.2, 50% glycerol, 0.09% sodium azide
Storage Temperature
-20ºC
Shipping Temperature
Blue Ice or 4ºC
Purification
Protein G Purified
Clonality
Monoclonal
Clone Number
S52A-42
Isotype
IgG1
Specificity
Detects ~75kDa.
Cite This Product
Mouse Anti-Mouse GRP75 Monoclonal, Clone S52A-42 (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SMC-133)
Certificate of Analysis
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.
References PubMed ID::http://www.ncbi.nlm.nih.gov/pubmed/19126683
Alternative Names
HSC74 Antibody, HSP74 Antibody, HSPA9 Antibody, HSPa9a Antibody, HSPA9B Antibody, Mortalin 2 Antibody, MOT2 Antibody, PBP74 Antibody
Research Areas
Cancer, Heat Shock, Alzheimer_s Disease, Cell Signaling, Neurodegeneration, Neuroscience, Parkinson_s Disease, Trafficking
Cellular Localization
Mitochondrion
Accession Number
NP_004125.3
Gene ID
3313
Swiss Prot
P38646
Scientific 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).
References
1. Kaul S.C., et al. (1993) Biochem Biophys Res Commun. 193: 348-355.
2. Wadhwa R., et al. (1993) J Biol Chem 268: 6615-6621.
3. Schneider H.C., et al. (1994) Nature 371: 768-774.
4. Manning-Krieg U.C., et al. (1991) EMBO J. 10: 3273-3280.
5. Wadhwa R., et al. (1998) J Biol Chem. 273: 29586-91.
6. Wadhwa R., et al. (2006) Int J Cancer 118: 2973-2980.
7. Kaul S.C., et al. (2003) Exp Cell Res. 286: 96-110.
8. Liberek K., et al. (1991) J Biol Chem. 266: 14491-14496.
9. Mizzen L.A., et al. (1991) Cell Regulation. 2: 165-179.
10. Leustek U.K., et al. (1989) PNAS USA. 86: 7805-7808.
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).
2. Wadhwa R., et al. (1993) J Biol Chem 268: 6615-6621.
3. Schneider H.C., et al. (1994) Nature 371: 768-774.
4. Manning-Krieg U.C., et al. (1991) EMBO J. 10: 3273-3280.
5. Wadhwa R., et al. (1998) J Biol Chem. 273: 29586-91.
6. Wadhwa R., et al. (2006) Int J Cancer 118: 2973-2980.
7. Kaul S.C., et al. (2003) Exp Cell Res. 286: 96-110.
8. Liberek K., et al. (1991) J Biol Chem. 266: 14491-14496.
9. Mizzen L.A., et al. (1991) Cell Regulation. 2: 165-179.
10. Leustek U.K., et al. (1989) PNAS USA. 86: 7805-7808.