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Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody

Details for Product No. ABIN361849, Supplier: Log in to see
Antigen
  • hsp90b
  • HSP90-BETA
  • HSP90B
  • HSPC2
  • Hspcb
  • 90kDa
  • AL022974
  • C81438
  • Hsp84
  • Hsp84-1
  • Hsp90
  • hsp90beta
  • wu:fa29f01
  • wu:fa91e11
  • wu:fd59e11
  • wu:gcd22h07
  • HSPCB
  • D6S182
  • HSP84
  • HSP90
  • Heat Shock Protein 90, endoplasmic reticulum
  • heat shock protein 90B
  • heat shock protein hsp90 beta
  • heat shock protein 90 alpha (cytosolic), class B member 1
  • heat shock protein 90, alpha (cytosolic), class B member 1
  • heat shock protein 90kDa alpha (cytosolic), class B member 1
  • HSP90B
  • hsp90b
  • Hsp90ab1
  • hsp90ab1
  • HSP90AB1
Reactivity
Human, Mouse (Murine), Rat (Rattus)
291
220
187
35
27
16
14
13
6
4
4
4
3
2
2
2
2
2
2
2
1
1
1
1
1
Host
Rabbit
186
104
1
Clonality
Polyclonal
Conjugate
Un-conjugated
8
8
6
5
4
4
4
3
3
3
3
3
3
3
3
3
3
3
3
3
3
3
3
3
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
252
163
114
112
87
58
55
33
14
14
10
10
5
2
1
1
Options
Supplier
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Immunogen Full length protein HSP90
Specificity Detects ~90kda. Does not cross-react with HSP90α.
Purification Peptide Affinity Purified
Alternative Name HSP90 beta (HSP90AB1 Antibody Abstract)
Background HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its 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 (5-6). 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. In 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 (7). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Gene ID 3326
NCBI Accession NP_031381
UniProt P08238
Application Notes
  • WB (1:1000)
  • IHC (1:100)
  • ICC/IF (1:120)
  • optimal dilutions for assays should be determined by the user.
Comment

A 1:1000 dilution of SPC-177 was sufficient for detection of HSP90 in 20 μg of HeLa cell lysate by ECL immunoblot analysis.

Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Storage -20 °C
Supplier Images
Western Blotting (WB) image for anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody (ABIN361849) Cell line mix, Western Blotting 1 in 2000 Hsp90beta.
Product cited in: Donlin, Andresen, Just, Rudensky, Pappas, Kruger, Jacobs, Unger, Zieseniss, Dobenecker, Voelkel, Chait, Gregorio, Rottbauer, Tarakhovsky, Linke: "Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organization." in: Genes & development, Vol. 26, Issue 2, pp. 114-9, 2012 (PubMed).

Wagatsuma, Shiozuka, Kotake, Takayuki, Yusuke, Mabuchi, Matsuda, Yamada: "Pharmacological inhibition of HSP90 activity negatively modulates myogenic differentiation and cell survival in C2C12 cells." in: Molecular and cellular biochemistry, Vol. 358, Issue 1-2, pp. 265-80, 2011 (PubMed).

Background publications Arlander, Eapen, Vroman, McDonald, Toft, Karnitz: "Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress." in: The Journal of biological chemistry, Vol. 278, Issue 52, pp. 52572-7, 2003 (PubMed).

Pratt, Toft: "Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery." in: Experimental biology and medicine (Maywood, N.J.), Vol. 228, Issue 2, pp. 111-33, 2003 (PubMed).

Pearl, Prodromou: "Structure, function, and mechanism of the Hsp90 molecular chaperone." in: Advances in protein chemistry, Vol. 59, pp. 157-86, 2002 (PubMed).

Neckers: "Hsp90 inhibitors as novel cancer chemotherapeutic agents." in: Trends in molecular medicine, Vol. 8, Issue 4 Suppl, pp. S55-61, 2002 (PubMed).

Pratt: "The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors." in: Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.), Vol. 217, Issue 4, pp. 420-34, 1998 (PubMed).

Pratt, Toft: "Steroid receptor interactions with heat shock protein and immunophilin chaperones." in: Endocrine reviews, Vol. 18, Issue 3, pp. 306-60, 1997 (PubMed).

Whitesell, Mimnaugh, De Costa, Myers, Neckers: "Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, Issue 18, pp. 8324-8, 1994 (PubMed).