Votre recherche pour: Geldanamycin

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Anti-HSP90B Rabbit Polyclonal Antibody

Fournisseur: ENZO LIFE SCIENCES

Description: The 90 kDa molecular chaperone family includes 90 kDa heat shock protein Hsp90 and 94 kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells express inducible Hsp90 alpha and constitutive Hsp90 beta isoforms that are encoded by separate genes. The amino acid sequences of human and yeast Hsp90 alpha are 85% and 90% homologous to those of Hsp90 beta, respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular protein in most cells. Hsp90 functions as part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, Hsp90 provides a necessary component of such fundamental cellular processes as hormone signaling and cell cycle control by serving as a chaperone for many key signaling molecules including steroid receptors, cell cycle kinases involved in signal transduction, and p53. As many of these client proteins are known oncogenes, Hsp90 inhibitors such as 17-AAG, a geldanamycin analog, have been of benefit in the treatment of many cancers.

Anti-HSP90B1 Rat Monoclonal Antibody [clone: 9G10]

Fournisseur: ENZO LIFE SCIENCES

Description: Glucose-regulated protein 94 (Grp94, gp96), an abundant resident endoplasmic reticulum (ER) lumenal stress protein, belongs to the Hsp90 family of molecular chaperones along with cytosolic Hsp90. Grp94 and such other resident soluble proteins of the ER as the Ca 2+ binding protein subfamily (CaBP, CaBPI, CaBP2 and calreticulin) possess the C-terminal tetrapeptide Lys-Asp-Glu-Leu (KDEL), a sorting signal considered responsible for the retention of these proteins in the pre-Golgi compartments. Stress conditions such as glucose starvation and heat shock which promote protein misfolding or unfolding increase Grp94 expression. In addition to a homeostatic role in protein folding and assembly, Grp94 can function in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. Grp94 and Hsp90 share high sequence identity and apparently identical adenosine nucleotide dependent modes of regulation, although previous data suggests that Hsp90 and Grp94 may differ in their nucleotide binding properties. The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket which also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol. However, the molecular basis for adenosine nucleotide-dependent regulation of Grp94 remains unclear. Data supports a ligand dependent regulation of Grp94 function, and suggests a model whereby Grp94 function is regulated through a ligand -dependent conversion of Grp94 from an inactive to an active conformation.