You are viewing an incomplete version of our website. Please click to reload the website as full version.

HSP90AA2 antibody (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2)

Details for Product anti-HSP90AA2 Antibody No. ABIN361663, Supplier: Log in to see
Antigen
  • fb17b01
  • hsp90
  • hsp90a
  • hsp90a.1
  • hsp90alpha
  • wu:fb17b01
  • zgc:86652
  • HSP90ALPHA
  • HSPCA
  • HSPCAL3
  • heat shock protein 90, alpha (cytosolic), class A member 1, tandem duplicate 1
  • heat shock protein 90kDa alpha (cytosolic), class A member 2
  • hsp90aa1.1
  • HSP90AA2
Reactivity
Human, Mouse (Murine), Rat (Rattus)
144
125
110
14
7
6
6
6
6
5
3
2
2
2
2
2
Host
Mouse
72
69
2
2
Clonality (Clone)
Monoclonal ()
Conjugate
This HSP90AA2 antibody is un-conjugated
6
6
5
5
5
3
3
3
3
3
3
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
1
1
1
1
1
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
105
100
65
64
63
58
32
27
5
2
2
1
1
1
Options
Supplier
Log in to see
Supplier Product No.
Log in to see
Request

Get this product for free

It's quick and easy to submit your validation proposal. I want to validate this product

Learn more

Available images

Immunogen Human HSP90alpha
Clone 2G5-G3
Isotype IgG
Specificity Detects ~90 kDa. HSP90α-specific (>96 % α-specific by ELISA)
Sensitivity 0.5 µg/mL of SMC-147 was sufficient for detection of Hsp90alpha in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
Alternative Name HSP90 alpha (HSP90AA2 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 3320
NCBI Accession NP_001017963
UniProt P07900
Application Notes
  • WB (1:2000)
  • ICC/IF (1:100)
  • optimal dilutions for assays should be determined by the user.
Comment

0.5 μg/ml of SMC-147 was sufficient for detection of HSP90alpha in 20 μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

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
Western Blotting (WB) image for anti-HSP90AA2 antibody (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 2) (ABIN361663) Western Blotting Hsp90lpha RatTissue 10ug 1 in 1000 copy.
Product cited in: Ortega, Calvillo, Luna, Pérez-Severiano, Rubio-Osornio, Guevara, Limón: "17-AAG improves cognitive process and increases heat shock protein response in a model lesion with Aβ25-35." in: Neuropeptides, Vol. 48, Issue 4, pp. 221-32, 2014 (PubMed).

Hunter, OHagan, Kenyon, Dhanani, Prinsloo, Edkins: "Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells." in: PLoS ONE, Vol. 9, Issue 1, pp. e86842, 2014 (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).

Garg, Hassid: "Nitric oxide decreases cytosolic free calcium in Balb/c 3T3 fibroblasts by a cyclic GMP-independent mechanism." in: The Journal of biological chemistry, Vol. 266, Issue 1, pp. 9-12, 1991 (PubMed).