The 90kDa molecular chaperone family includes 90kDa heat shock protein Hsp90 and 94kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells contain isoforms Hsp90α and Hsp90β, encoded by separate genes. The amino acid sequences of human and yeast Hsp90α are 85% and 90% homologous to those of Hsp90β, 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 proteins 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 signalling and cell cycle control. In this context, researchers identified key regulatory proteins as substrates of Hsp90, including steroid receptors, cell cycle kinases involved in signal transduction, and p53. Hsp90 may act as a capacitor for morphological evolution by buffering widespread variation, potentially affecting morphogenic pathways. When temperature and other stress factors compromise Drosophilia Hsp90 buffering, cryptic variant expression occurs, and selection can lead to the continued expression of these traits, even after Hsp90 function is restored.
序列
重组人热休克蛋白70蛋白产品,又称Human Heat Shock Protein 70, Heat Shock Protein 70.其对应NCBI基因号为3303,对应Accession号为P08107.
来源宿主
提供的【HSP70】重组人热休克蛋白70产品的来源为大肠杆菌重组表达.
溶解建议
重组人热休克蛋白70产品请按照说明书建议进行溶解操作:Reconstitute in H₂O (solubility > 40 mg/ml), aliquot and store at -80 °C.