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中文名稱(chēng)

熱休克蛋白90 A抗體

英文名字
Hsp90 alpha Antibody: APC/Cy7
供應(yīng)商
StressMarq
產(chǎn)品貨號(hào)
SMC-554D-APCCY7
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背景資料
HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms A and B, which share 85% sequence amino acid homology. The two isoforms of HSP90, are expressed in the cytosolic compartment (1). Despite the similarities, HSP90A exists predominantly as a homodimer while HSP90B exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively.nHSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite it's label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (7-8). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase (5). When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation.nIn most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9). For more information visit our HSP90 Scientific Resource Guide at HSP90.ca.
應(yīng)用類(lèi)型
WB | ELISA
免疫原
純化的 HSP90
來(lái)源宿主
小鼠
反應(yīng)性
人
保存建議
廠家推薦藍(lán)冰運(yùn)輸。收到產(chǎn)品后建議保存于-20oC。
其他
StressMarq Biosciences Inc. 在2007年成立于加拿大維多利亞，是一家生物科技公司，專(zhuān)門(mén)從事試劑與試劑盒研究，服務(wù)范圍遍及1937多個(gè)國(guó)家。 StressMarq公司的核心技術(shù)領(lǐng)域?yàn)榧?xì)胞應(yīng)激（尤其是熱休克蛋白（HSP）領(lǐng)域，領(lǐng)先全球），離子通道，載體研究，同時(shí)在神經(jīng)科學(xué)領(lǐng)域推出特有的具有生物活性的Tau蛋白與A-突觸核蛋白。產(chǎn)品領(lǐng)域涉及到：細(xì)胞凋亡、細(xì)胞信號(hào)、通路和轉(zhuǎn)運(yùn)、細(xì)胞器標(biāo)志物、熱休克、神經(jīng)生物學(xué)、神經(jīng)科學(xué)、氧化應(yīng)激、磷酸化運(yùn)輸?shù)取３颂峁┯糜谶M(jìn)一步研究的相關(guān)工具外，Str
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