Hsp90α/β Monoclonal Antibody (Clone K41220A)_上海惠诚生物生物试剂,标准品,仪器设备,耗材,一站式服务

服务热线：13917250134「同微信」

您的位置：首页>>Cayman>>Antibodies>>Hsp90α/β Monoclonal Antibody (Clone K41220A)

产品中心

/ Products Classification 点击展开+

Cat. Number

070281348749981

Chemical Name

Hsp90α/β Monoclonal Antibody (Clone K41220A)

References

Synonyms

Heat Shock Protein 90α/β

Formula Weight

90.0

Formulation

Protein G affinity-purified mouse IgG at a concentration of 1 mg/ml in PBS, pH 7.2, containing 0.09% sodium azide and 50% glycerol

Stability

1 year

Storage

-20°C

Shipping

Wet ice in continental US; may vary elsewhere

Specificity

Human (β-specific) Hsp90α./β	+
Rat Hsp90α./β	+
S. cerevisiae Hsp90α/β	+
S. pombe Hsp90α/β	+
Rice Hsp90α/β	-
P. caudatum Hsp90α/β	-

Show all 6 Hide all but first 3

Background Reading

Nemoto, T., Sato, N., Iwanari, H., et al. Domain structures and immunogenic regions of the 90-kDa heat shock protein (Hsp90). Probing with a library of anti-Hsp90 monoclonal antibodies and limited proteolysis. J Biol Chem 272(42) 26179-26187 (1997).

Kishimoto, J., Fukuma, Y., Mizuno, A., et al. Identification of the pentapeptide constituting a dominant epitope common to all eukaryotic heat shock protein 90 molecular chaperones. Cell Stress Chaperones 10(4) 296-311 (2005).

Minami, Y., Kawasaki, H., Miyata, Y., et al. Analysis of native forms and isoforms compositions of the mouse 90-kDa heat shock protein, Hsp90. J Biol Chem 266(16) 10099-10103 (1991).

Arlander, S.J.H., Eapen, A.K., Vroman, B.T., et al. Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. J Biol Chem 278(52) 52572-52577 (2003).

Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8(4 Suppl.) S55-S61 (2002).

Pratt, W.B., and Toft, D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18(3) 306-360 (1997).

Whitesell, L., Mimnaugh, E.G., De Costa, B., et al. Inhibition of heat shock protein Hsp90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 91 8324-8328 (1994).

Pratt, W.B. The Hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med 217 420-434 (1998).

Pratt, W.B., and Toft, D.O. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70-based chaperone machinery. Exp Biol Med 228 111-133 (2003).

Pearl, L.H., and Prodromou, C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem 59 157-172 (2001).

Show all 10 Hide all but first 3

Size	Global Purchasing
25 µg
100 µg

Description

Antigen: human recombinant Hsp90α/β · Clone designation: K41220A · Host: mouse · Application(s): WB and EIA · Hsp90 is an abundantly and ubiquitously expressed Hsp. It is understood to exist in two principal forms, α and β, which share 85% amino acid sequence homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment.¹ Despite the similarities, Hsp90α exists predominantly as a homodimer while Hsp90β 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.^3,4,5,6 Furthermore, Hsp90 is highly conserved between species, having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite its label of being a Hsp, Hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% 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.

1 Nemoto, T., Sato, N., Iwanari, H., et al. Domain structures and immunogenic regions of the 90-kDa heat shock protein (Hsp90). Probing with a library of anti-Hsp90 monoclonal antibodies and limited proteolysis. J Biol Chem 272(42) 26179-26187 (1997).

2 Minami, Y., Kawasaki, H., Miyata, Y., et al. Analysis of native forms and isoforms compositions of the mouse 90-kDa heat shock protein, Hsp90. J Biol Chem 266(16) 10099-10103 (1991).

3 Arlander, S.J.H., Eapen, A.K., Vroman, B.T., et al. Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress. J Biol Chem 278(52) 52572-52577 (2003).

4 Pearl, L.H., and Prodromou, C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem 59 157-172 (2001).

5 Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8(4 Suppl.) S55-S61 (2002).

6 Pratt, W.B., and Toft, D.O. Regulation of signaling protein function and trafficking by the Hsp90/Hsp70-based chaperone machinery. Exp Biol Med 228 111-133 (2003).

7 Pratt, W.B., and Toft, D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18(3) 306-360 (1997).

8 Pratt, W.B. The Hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med 217 420-434 (1998).

下一个：Hsp90α Monoclonal Antibody (Clone K41009)上一个：Hsp90β Monoclonal Antibody (Clone H90-10)

联系我们

电话：021-60498804
邮箱：info@e-biochem.com
地址：上海市徐汇区漕溪路258弄27号航星商务楼2-404

扫一扫，关注我们

惠诚品牌

产品中心: 分子生物; 分析化学; 生化试剂; 仪器耗材

企业动态

技术资料

在线咨询联系方式二维码

服务热线

021-60498804

扫一扫，关注我们