HSP90 Antibody | StressMarq Biosciences SMC-137D product information

product summary

company name :

StressMarq Biosciences

product type :

antibody

product name :

HSP90 Antibody

catalog :

SMC-137D

quantity :

100 µg

price :

314.00 USD

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

D7A

reactivity :

human, mouse, rat, bovine

application :

western blot, ELISA, immunohistochemistry, immunoprecipitation

more info or order :

StressMarq Biosciences product webpage

citations: 2

Published Application/Species/Sample/Dilution	Reference
western blot; rat	Akkad H, Corpeno R, Larsson L. Masseter muscle myofibrillar protein synthesis and degradation in an experimental critical illness myopathy model. PLoS ONE. 2014;9:e92622 pubmed publisher
	Ojima K, Ichimura E, Suzuki T, Oe M, Muroya S, Nishimura T. HSP90 modulates the myosin replacement rate in myofibrils. Am J Physiol Cell Physiol. 2018;315:C104-C114 pubmed publisher

product information

Catalog No :

SMC-137D

Product Name :

HSP90 Antibody

Description :

Mouse Anti-Chicken HSP90 Monoclonal IgG1

Target :

HSP90

Conjugate :

Unconjugated

2021 List Price :

314.00 USD

Currency :

USD

Research Area(s) :

Cancer Heat Shock Cell Signaling Protein Trafficking Chaperone Proteins Cancer Tumor Biomarkers

Alternative Name(s) :

HSP86 Antibody, HSP89A Antibody, HSP90A Antibody, HSP90AA1 Antibody, HSPC1 Antibody, HSPCA Antibody, HsoCAL3 Antibody

Size :

100 µg

Category :

Antibodies

Product Type :

Monoclonal

Clone Number :

D7A

Immunogen :

Full length protein HSP90 purified from chicken brain

Immunogen Species :

Chicken

Accession Number :

NP_001103255.1

Swiss-Prot :

P11501

Applications :

WB IHC IP ELISA AM

Host Species :

Mouse

Isotype :

IgG1

Species Reactivity Abbreviation :

Hu Ms Rt Bv Pg Rb Ck

Species Reactivity Full Name :

Human Mouse Rat Bovine Pig Rabbit Chicken

Antibody Dilution :

WB (1:500), IP (5µg) ; optimal dilutions for assays should be determined by the user.

Purification :

Protein G Purified

Storage Buffer :

PBS pH7.2, 50% glycerol, 0.09% sodium azide

Concentration :

1 mg/ml

Specificity :

Recognizes 90kDa. Can isolate complexes of HSP90, Src kinase and cec37.

Storage Temperature :

-20ºC

Shipping Temperature :

Blue Ice or 4ºC

Cite this Product :

StressMarq Biosciences Cat# SMC-137D, RRID: AB_2121062

Certificate of Analysis :

2 µg/ml was sufficient for detection of HSP90α in 20 µg of heat shocked HeLa cell lysate as well as in 100 ng of human HSP90α protein by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.

Cellular Localization :

Cytoplasm Melanosome

Scientific Background :

HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (4-7). 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 (8-9). The number of proteins now known 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(6). 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 immune-adsorption 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 (10). For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.

References :

1. Schuh S. et al. (1985) J Biol Chem. 260 (26): 14292-14296. 2. Lipsich L.A., Cutt J.R. and Brugge J.S. (1982) Mol. Cell Biol. 2(7): 875-880. 3. Brugge J.S., Yonemoto W., and Darrow D. (1983) Mol. Cell. Biol. 3(1): 9-19. 4. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577. 5. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186. 6. Neckers L, et al. (2002) Trends Mol Med 8:S55-S61. 7. Pratt W, Toft D. (2003) Exp Biol Med 228:111-133. 8. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360. 9. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434. 10. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324– 8328.

Field of Use :

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.

Image Filenames :

SMC-137_Hsp90_Antibody_D7alpha_IHC_Mouse_inflamed-colon_40x_1.png SMC-137_Hsp90_Antibody_D7Alpha_WB_Rat_cell-lysates_1.png
SMC-137_Hsp90_Antibody_D7alpha_IHC_Huma
n_colon-carcinoma_40x_1.png

more info or order :

StressMarq Biosciences product webpage