Hsp90β Monoclonal Antibody (Clone K3701)_上海惠诚生物生物试剂,标准品,仪器设备,耗材,一站式服务

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Cat. Number

070273951065497

Chemical Name

Hsp90β Monoclonal Antibody (Clone K3701)

References

Synonyms

Heat Shock Protein 90β

Formula Weight

90.0

Formulation

Protein G affinity-purified mouse IgM, 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) Hsp90	+
Humanα Hsp90	-
Rat Hsp90	-

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).

Nemoto, T., Roi, R., Matsusaka, T., et al. Isoform-specific monoclonal antibodies against Hsp90. IUBMB Life 42(5) 881-889 (1997).

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).

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Size	Global Purchasing
25 µg
100 µg

Description

Antigen: human recombinant Hsp90β · Clone designation: K3701 · Host: mouse · Application(s): WB, EIA, and IHC · 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, 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.^3,4,5,6 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 heat shock protein, 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 signalling.^7,8 The number of proteins now known 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：Hsp90β Monoclonal Antibody (Clone H90-10)上一个：Hsp90β Polyclonal Antibody

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