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

Details for Product No. ABIN263944
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Antigen
Synonyms 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
Reactivity
Dog (Canine), Chicken, Human, Rabbit, Rat (Rattus)
(207), (125), (112), (20), (18), (18), (16), (12), (8), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1)
Host
Mouse
(153), (64), (1)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(3), (3), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Immunohistochemistry (Frozen Sections) (IHC (fro)), Enzyme Immunoassay (EIA), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (Frozen Paraffin-embedded Sections) (IHC (frpe)), Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
(202), (95), (83), (67), (44), (38), (34), (18), (14), (14), (11), (10), (1), (1), (1), (1)
Pubmed 8 references available
Quantity 50 μg
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Catalog No. ABIN263944
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Immunogen Recombinant human hsp90 beta.
Clone H90-10
Isotype IgG2a
Specificity Detects 90 kDa proteins corresponding to the Molecular Mass of HSP90beta.
Characteristics Synonyms: HSP90B, HSPC2, HSPCB, Heat shock protein HSP 90-beta, Heat shock 84 kDa, HSP84
Purification Affinity Chromatography on Protein G
Alternative Name HSP90AB1 / HSP90 beta
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 it's 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).Synonyms: HSP84, HSP90B, HSPC2, HSPCB, Heat shock 84 kDa, Heat shock protein HSP 90-beta
Molecular Weight 83 kDa
Gene ID 3326
UniProt P08238
Application Notes Western blot (Ref.10,11): 1 μg/mL was sufficient for detection of HSP90beta in 20 μg ofHeLalysate. Immunoprecipitation (Ref.10,11). ELISA. Immunohistochemistry.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Concentration 1.0 mg/mL
Buffer PBS pH 7.2 containing 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
Storage Comment Store the antibody at -20 °C.
Shelf life: one year from despatch.
Expiry Date 12 months
Supplier Images
anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody
anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody (2) anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody (Image 2)
anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody (3) anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody (Image 3)
anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody (4) anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody (Image 4)
Background publications Minami, Kawasaki, Miyata et al.: "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).

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

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

Barent, Nair, Carr et al.: "Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes." in: Molecular endocrinology (Baltimore, Md.), Vol. 12, Issue 3, pp. 342-54, 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).

Loo, Jensen, Cui et al.: "Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome." in: The EMBO journal, Vol. 17, Issue 23, pp. 6879-87, 1999 (PubMed).

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

Arlander, Eapen, Vroman et al.: "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).

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