Phospho-HSP90α (Thr5/7) Antibody

• 产品编号：CST-3488S      品牌：CST       原厂货号：3488S
• 产品分类：抗体 > 一抗 > 磷酸化抗体
• 应用分类：

描述：

Phospho-HSP90α (Thr5/7) Antibody识别内源性的Thr5/7磷酸化的HSP90α蛋白。该多克隆抗体用与人类HSP90α中Thr5/7位点附近的氨基酸序列对应的人工合成磷酸化的肽段免疫动物而制成。该抗体使用蛋白A和蛋白亲和层析纯化而得。HSP70和HSP90是正常情况下组成性表达的分子伴侣，能够保持蛋白合成稳态，并且在环境压力下被诱导（1）。HSP70和HSP90能够与未折叠蛋白相互作用，防止其不可逆的堆积，并且在ATP和共伴侣依赖的形式下催化其重新折叠（1）。HSP70的底物广泛，包括新合成和变性的蛋白，HSP90倾向于有更局限的底物，大部分是信号分子。HSP70和HSP90经常在多分子伴侣系统中协同发挥功能，它们至少需要一些共伴侣：HSP40、Hop和p23（2,3）。共伴侣调节分子伴侣的内在ATP酶活性或者招募分子伴侣到特定的底物或亚细胞区域中去（1,4）。当泛素连接酶CHIP与HSP70/HSP90复合物结合作为协同因子，未折叠的底物将被蛋白酶降解（4）。HSP70/HSP90的生物学功能应该不仅是其分子伴侣活性。它们也是核激素以及其它信号分子的成熟和激活所至关重要的（1,3）。它们在囊泡形成和蛋白转运中也扮演作用（2）。Phospho-HSP90α (Thr5/7) Antibody直接针对HSP90α在Thr5/7位点磷酸化的蛋白，该位点由由CST公司使用PhosphoScan发现，其是CST的基于质谱的磷酸化位点发现平台。以往研究也发现HSP90α在Thr5/7的磷酸化是由人双链DNA活化的蛋白激酶导致的（5）。请参见PhosphoSitePlus®，CST修饰位点知识库，www.phosphosite.org。

1. Nollen, E.A. and Morimoto, R.I. (2002) J. Cell Sci. 115, 2809-2816.
2. Young, J.C. et al. (2003) Trends Biochem. Sci. 28, 541-547.
3. Pratt, W.B. and Toft, D.O. (2003) Exp. Biol. Med. 228, 111-133.
4. Hohfeld, J. et al. (2001) EMBO Rep. 2, 885-890.
5. Lees-Miller, S.P. and Anderson, C.W. (1989) J Biol Chem 264, 17275-80.

原厂资料：

Specificity / Sensitivity

Phospho-HSP90α (Thr5/7) Antibody detects endogenous levels of HSP90α only when phosphorylated at Thr5/7.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr5/7 of human HSP90α. Antibodies are purified by protein A and peptide affinity chromatography.

Background

HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP and co-chaperone dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

Phospho-HSP90α (Thr5/7) Antibody is directed against the HSP90α threonine phosphorylation site at Thr5/7 that was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's MS/MS platform for phosphorylation site discovery. Phosphorylation of HSP90α at Thr5/7 was previously observed by the human double-stranded DNA-activated protein kinase (5). Please visit PhosphoSitePlus®, CST's modification site knowledgebase, at www.phosphosite.org for more information.

1. Nollen, E.A. and Morimoto, R.I. (2002) J. Cell Sci. 115, 2809-2816.
2. Young, J.C. et al. (2003) Trends Biochem. Sci. 28, 541-547.
3. Pratt, W.B. and Toft, D.O. (2003) Exp. Biol. Med. 228, 111-133.
4. Hohfeld, J. et al. (2001) EMBO Rep. 2, 885-890.
5. Lees-Miller, S.P. and Anderson, C.W. (1989) J Biol Chem 264, 17275-80.

注意事项：

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.