Western Blot: HSP90 beta Antibody (H9010) [NB110-61640] - Western blot analysis of Human Lysates showing detection of Hsp90 protein using Mouse Anti-Hsp90 Monoclonal Antibody, Clone H9010 (NB110-61640). Primary ...read more
Western Blot: HSP90 beta Antibody (H9010) [NB110-61640] - Human cell lysates from various cell lines showing detection of Hsp90 protein using Mouse Anti-Hsp90 Monoclonal Antibody, Clone H9010. 15 ug protein each lane. ...read more
Western Blot: HSP90 beta Antibody (H9010) [NB110-61640] - Western Blot analysis of Human Cervical cancer cell line (HeLa) lysate showing detection of Hsp90 protein using Mouse Anti-Hsp90 Monoclonal Antibody, Clone H9010 ...read more
1 ug/ml of HSP90 antibody was sufficient for detection of HSP90beta in 20 ug of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using goat anti-mouse IgG:HRP as the secondary antibody.
Read 5 Reviews rated 4.8 using NB110-61640 in the following applications:
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
PBS (pH 7.2), 50% Glycerol
0.09% Sodium Azide
Protein G purified
Alternate Names for HSP90 beta Antibody (H9010)
Heat shock 84 kDa
heat shock 90kD protein 1, beta
heat shock 90kDa protein 1, beta
heat shock protein 90kDa alpha (cytosolic), class B member 1
heat shock protein beta
heat shock protein HSP 90-beta
HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of Hsp90, are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta; 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% ofcytosolic 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).
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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