|Other Names||Heat shock protein 75 kDa, mitochondrial, HSP 75, TNFR-associated protein 1, Tumor necrosis factor type 1 receptor-associated protein, TRAP-1, TRAP1, HSP75|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP14128b was selected from the C-term region of TRAP1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA.|
|Cellular Location||Mitochondrion. Mitochondrion inner membrane Mitochondrion matrix|
|Tissue Location||Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung, placenta and bladder. Expression is higly reduced in bladder cancer and renal cell carcinoma specimens compared to healthy tissues, but it is increased in other type of tumors.|
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HSP90 proteins are highly conserved molecular chaperonesthat have key roles in signal transduction, protein folding,protein degradation, and morphologic evolution. HSP90 proteinsnormally associate with other cochaperones and play important rolesin folding newly synthesized proteins or stabilizing and refoldingdenatured proteins after stress. TRAP1 is a mitochondrial HSP90protein. Other HSP90 proteins are found in cytosol (see HSP90AA1;MIM 140571) and endoplasmic reticulum (HSP90B1; MIM 191175) (Chenet al., 2005 [PubMed 16269234]).
Liu, D., et al. Cancer Lett. 296(2):194-205(2010)Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Nguyen, M.C., et al. Cancer Immunol. Immunother. 59(9):1313-1323(2010)Landriscina, M., et al. Cancer Res. 70(16):6577-6586(2010)Leav, I., et al. Am. J. Pathol. 176(1):393-401(2010)
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