Heat shock protein HSP 90-alpha (UniProt: P07900; also known as Heat shock 86 kDa, HSP 86, HSP86, Lipopolysaccharide-associated protein 2, LAP-2, LPS-associated protein 2, Renal carcinoma antigen NY-REN-38) is encoded by the HSP90AA1 (also known as HSP90A, HSPC1, HSPCA) gene (Gene ID: 3320) in human. HSP90 serves as a molecular chaperone that maintains the stability and functionality of numerous client proteins in an ATPase-dependent manner. It is known to interact dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle, and chaperone function. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. HSP90 and its co-chaperones are also shown to modulate transcription at least at three different levels (a) by altering the steady-state levels of certain transcription factors in response to various physiological cues (b) modulating the activity of certain epigenetic modifiers, such as histone deacetylases, and (c) by participation in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. In its resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer, which is defined as the open conformation. Upon ATP-binding, the N-terminal domain undergoes significant conformational changes and comes in contact to form an active closed conformation. Following the completion of its chaperoning activity, ATP molecule is hydrolyzed to ADP which then dissociates from HSP90 and directs the protein back to the resting state. This monoclonal antibody (clone 1G6-D7) is reported to inhibit both de novo tumor formation and expansion of already formed tumors in mice. (Ref.: Li, W., et al. (2012). Biochim. Biophys. Acta. 1823(3); 730 741; Zou, M., et al. (2017). Oncogene 36(15); 2160-2171).

~90 kDa observed; 84.66 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

A recombinant fragment corresponding to 115 amino acids from the F-5 region of human HSP90 alpha.

Anti-Hsp90 alpha, clone 1G6-D7, Cat. No. MABC1106, is a mouse monoclonal antibody that detects Hsp90 alpha, Hsp90 beta and has been tested for use in ELISA, Immunoprecipitation, Functional assay, Inhibition, and Western Blotting.

Immunoprecipitation Analysis: A representative lot immunoprecipitated Hsp90 alpha in Immunoprecipitation applications (Dong, H., et. al. (2016). Sci Rep. 6:20605).

ELISA Analysis: A representative lot detected Hsp90 alpha in ELISA applications (Zou, M., et. al. (2017). Oncogene. 36(15):2160-2171).

Affects Function Analysis: A representative lot blocked parental MDA-MB-231 cell invasion in a dose-dependent manner. (Zou, M., et. al. (2017). Oncogene. 36(15):2160-2171).

Western Blotting Analysis: A representative lot detected Hsp90 alpha in Western Blotting applications (Zou, M., et. al. (2017). Oncogene. 36(15):2160-2171).

Inhibits Activity/Function Analysis: A representative lot inhibited both de novo tumor formation and expansion of already formed tumors in mice. (Zou, M., et. al. (2017). Oncogene. 36(15):2160-2171).

Clone 1G6-D7 is a mouse monoclonal antibody that detects HSP90 alpha and HSP90 beta in human cells. it targets an epitope within 9 amino acids from the internal region.

Format: Purified

Evaluated by Western Blotting in MDA-MB-231 cell lysate.

Western Blotting Analysis: 1 µg/mL of this antibody detected Hsp90 alpha in MDA-MB-231 cell lysate.

Concentration: Please refer to lot specific datasheet.