Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) (AA 185-335) antibody

Details for Product No. ABIN361720, 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
Alternatives
anti-Mouse (Murine) Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 antibody for ELISA
Epitope
AA 185-335
50
33
24
22
16
13
12
7
6
5
4
4
3
3
3
3
3
3
2
2
1
1
1
1
1
1
1
1
Reactivity
Human, Mouse (Murine)
292
212
181
35
27
16
13
13
5
5
4
3
3
3
3
2
2
2
2
2
1
1
1
1
1
Host
Mouse
187
104
1
Clonality (Clone)
Monoclonal ()
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
Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
253
156
112
111
87
60
58
34
14
13
11
10
5
2
1
1
Options
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Immunogen Recombinant human HSP90beta, Specificity mapped to amino acids 185-335
Clone Hyb-K3701
Isotype IgM
Specificity Detects 90 kDa. This is a beta specific product, does not cross-react with alpha isoforms.
Purification Protein G Purified
Alternative Name HSP90 beta (HSP90AB1 Antibody Abstract)
Background HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85 % sequence amino acid 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 (3-6). 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 % 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. 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 (9). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Gene ID 3326
NCBI Accession NP_031381
UniProt P08238
Pathways Regulation of Cell Size
Application Notes
  • WB (1:1000)
  • IHC (1:3000)
  • optimal dilutions for assays should be determined by the user.
Comment

1 μg/ml was sufficient for detection of HSP90β in 20 μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.

Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) (AA 185-335) antibody (ABIN361720) Hsp90beta (K3701), cell lines.
Product cited in: Muralidharan, Ambade, Fulham, Deshpande, Catalano, Mandrekar: "Moderate alcohol induces stress proteins HSF1 and hsp70 and inhibits proinflammatory cytokines resulting in endotoxin tolerance." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 193, Issue 4, pp. 1975-87, 2014 (PubMed).

Bates, Salzman, May, Garcia, Hogan, McIntosh, Schlissel, Brown: "Extensive gene-specific translational reprogramming in a model of B cell differentiation and Abl-dependent transformation." in: PLoS ONE, Vol. 7, Issue 5, pp. e37108, 2012 (PubMed).

Background publications Kishimoto, Fukuma, Mizuno, Nemoto: "Identification of the pentapeptide constituting a dominant epitope common to all eukaryotic heat shock protein 90 molecular chaperones." in: Cell stress & chaperones, Vol. 10, Issue 4, pp. 296-311, 2005 (PubMed).

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).

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

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

Nemoto, Roi, Matsusaka, Iwanari, Yamashita, Kyakumoto, Sato: "Isoform-specific monoclonal antibodies against HSP90." in: Biochemistry and molecular biology international, Vol. 42, Issue 5, pp. 881-9, 1998 (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).

Nemoto, Sato, Iwanari, Yamashita, Takagi: "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." in: The Journal of biological chemistry, Vol. 272, Issue 42, pp. 26179-87, 1997 (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).

Lowe: "Colipase stabilizes the lid domain of pancreatic triglyceride lipase." in: The Journal of biological chemistry, Vol. 272, Issue 1, pp. 9-12, 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).

Minami, Kawasaki, Miyata, Suzuki, Yahara: "Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90." in: The Journal of biological chemistry, Vol. 266, Issue 16, pp. 10099-103, 1991 (PubMed).