Heat Shock Protein 90 (HSP90) antibody

Details for Product No. ABIN361823
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Antigen
Synonyms
git10, swo1, HSP90, htpG, SCBAC25F8.08, 23.m06066, 17.m07646, HSP90-1, 143198_at, 83, 83K HSP, DMHSP82, E(sev)3A, E(sina)2, HSP82, HSP83, ORF1, Su(Raf)3A, anon-EST:Liang-2.53, anon-WO0068693, anon-WO0 ... show more
git10, swo1, HSP90, htpG, SCBAC25F8.08, 23.m06066, 17.m07646, HSP90-1, 143198_at, 83, 83K HSP, DMHSP82, E(sev)3A, E(sina)2, HSP82, HSP83, ORF1, Su(Raf)3A, anon-EST:Liang-2.53, anon-WO0068693, anon-WO0140519.209, clone 2.53, en(lz)3C/4C, hsp84, l(3)j5C2, ms(3)08445, stc, DmelCG1242, CG1242, 86kDa, 89kDa, AL024080, AL024147, Hsp86-1, Hsp89, Hsp90, Hspca, hsp4, Hsp86, EL52, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCA, HSPCAL1, HSPCAL4, HSPN, LAP2, hsp86, hsp89, hsp90, hsp90a, hspc1, hspca, hspn, lap2, D6S182, HSP84, HSP90B, HSPC2, HSPCB show less
Reactivity
Human, Rat (Rattus), Mouse (Murine)
(139), (54), (52), (30), (23), (12), (7), (5), (5), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Host
Rabbit
(110), (49), (6), (1)
Clonality
Polyclonal
Conjugate
Un-conjugated
(5), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1)
Application
Western Blotting (WB), ELISA, Immunoprecipitation (IP), Immunohistochemistry (IHC), Immunofluorescence (IF)
(144), (87), (81), (70), (37), (31), (25), (9), (4), (2), (2)
Pubmed 4 references available
Quantity 100 µL
Options
Shipping to United States (Change)
Availability Will be delivered in 3 to 4 Business Days
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Catalog No. ABIN361823
315.70 $
Plus shipping costs $45.00

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Immunogen Full length protein Hsp90
Isotype IgG
Specificity Detects approx. 90 kDa proteins corresponding to the molecular mass of Hsp90α/β.
Alternative Name Hsp90
Background Synonyms:
Hsp84, Hsp86, Hsp90A, Hsp90AA1, Hsp90AB1, Hsp90B, HspC1, HspC2, HspCAL1, HspCAL4, Hsp90N
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. Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. 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.. 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.
Gene ID 3326
NCBI Accession NP_031381
UniProt P08238
Research Area Cancer, Heat Shock Proteins
Application Notes Recommended Dilution: 1:20000-40000 (ECL) (WB)
Restrictions For Research Use only
Format Liquid
Storage -20 °C
Background publications Pratt, Toft: "Steroid receptor interactions with heat shock protein and immunophilin chaperones." in: Endocrine reviews, Vol. 18, Issue 3, pp. 306-60, 1997 (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).

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).

Validation Images
Did you look for something else?
back to top