Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1) antibody

Antigen: Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1)

Synonyms: htpG

Clonality: Monoclonal (H9010)

Host: Mouse

Reactivity: Human, Rabbit, Chicken

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunoprecipitation (IP), ELISA, Immunohistochemistry (IHC)

Catalog no.: ABIN361717

Additional Information

Alternative name: Hsp90

Gene ID: 3326

UniProt: P08238

Immunogen: Recombinant human Hsp90beta

Isotype: IgG2a

Clone: H9010

Description: Synonyms: Hsp84, Hsp90, Hsp90 beta, Hsp90B, HspC2, HSPCB

Characteristics: Accession Number: NP_031381.2

Specificity: Detects 90kDa proteins corresponding to the molecular mass of Hsp90beta.
Reactivity: Human (beta-specific), Rabbit (Beta Specific), Chicken (Alpha/Beta)

Sensitivity: 1 µg/mL of SMC-107 was sufficient for detection of Hsp90beta in 20µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Application Details

Application Notes: 1µg/ml was sufficient for detection of hsp90beta by Western Blot in 20µg of HeLa lysate.

Concentration: 1mg/mL

Purification: Protein G Purified

Buffer: PBS pH7.2, 50% glycerol

Storage: Store at -20° C. Shipping Conditions: Blue Ice or 4° C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Heat Shock Proteins, Cancer

Restrictions: For Research Use only

Images

Hsp90 (H9010) Western Blotting, heat shock Hela.

Hsp90 (H9010), cell lines.

Rabbit reticulocyte lysate

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).

Whitesell, Mimnaugh, De Costa et al.: "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).

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).

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

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).