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anti-NF1P5 antibody product blog

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Posted on 2015-11-23 08:45:56 by mybiosource_staff
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Tags: Antibody; Monoclonal Antibody; HSP90 ; anti-NF1P5 antibody; NF1P5;
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The NF1P5 n/a (Catalog #MBS803038) is an Antibody produced from Mouse and is intended for research purposes only. The product is available for immediate purchase. The Hsp90 Antibody: APC reacts with Human, Rabbit, Rat, Mouse, Chicken, Achyla, Wheat Germ, Sf9 cell line and may cross-react with other species as described in the data sheet. MyBioSource\'s Hsp90 can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB), Immunohistochemistry (IHC).
1 ug/ml was sufficient for detection of hsp90 by Western Blot in 20 ug of HeLa lysate. Researchers should empirically determine the suitability of the NF1P5 n/a for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process.

The NF1P5 n/a product has the following accession number(s) (GI #22086553) (NCBI Accession #AAM90675.1) (Uniprot Accession #Q8LLI5). Researchers may be interested in using Bioinformatics databases such as those available at The National Center for Biotechnology Information (NCBI) website for more information about accession numbers and the proteins they represent. Even researchers unfamiliar with bioinformatics databases will find the NCBI databases to be quite user friendly and useful.

To buy or view more detailed product information and pricing, please click on the technical datasheet page below:


Please refer to the product datasheet for known applications of a given antibody. We\'ve tested the Hsp90 Antibody: APC with the following immunoassay(s):
Testing Data (IHC staining of inflammatory cells and epithelia mucosa in mouse colon tissues.)
Testing Data NF1P5.

Background Info: This antibody is reactive with both the constitutive and the inducible form of Hsp90. It does not bind to the native form and does not recognize Hsp90 from E.coli or yeast.

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 (1-4). 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 (5-6). 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 immuno-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 (7).

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