Product Name:
FKBP52
Product Number:
ab-nn127
Target Full Name: Peptidyl-prolyl cis-trans isomerase FKBP4
Target Alias: FK506 binding protein 4; FKBP4; FKBP59; HBI; HSP56; p52; p59; PPIase; Rotamase; T cell FK506 binding protein
Product Type Specific: FK506 binding protein pan-specific antibody
Antibody Code: NN127
Antibody Target Type: Pan-specific
Protein UniProt: Q02790
Protein SigNET: FKBP52
Antibody Type: Monoclonal
Antibody Host Species: Mouse
Antibody Ig Isotype Clone: IgG
Antibody Immunogen Source: Synthetic peptide corresponding to the residues of human FKBP52
Production Method: Protein G purified
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Antibody Concentration: 1 mg/ml
Storage Buffer: Phosphate buffered saline, 50% glycerol, 0.09% sodium azide
Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.
Product Use: Western blotting | Immunohistochemistry | ICC/Immunofluorescence | Immunoprecipitation
Antibody Dilution Recommended: WB (1:2000), IHC (1:250), IP (5µg); optimal dilutions for assays should be determined by the user.
Antibody Potency: Medium potency. Detects a ~52 kDa protein in cell and tissue lysates by Western blotting. Heavy chain migrates close to FKBP52 on SDS-PAGE gels.
Antibody Species Reactivity: This antibody detects the target protein in the following species due to conservation of amino acid sequence: Human | Dog | Rat | Mouse | Hamster.
Antibody Positive Control: 0.5 µg/ml was sufficient for detection of FKBP52 in 20 µg total protein using WB by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.
Antibody Specificity: Very high
Related Product 1: FKBP51 expression antibody (Cat. No.: AB-NN249-1)
Scientific 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). They feature three main domains: an amino-terminal domain (NTD) for ATP binding, a middle domain (MD) for client protein binding, and a carboxy-terminal domain (CTD) for dimerization. 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. 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 signalling (7-8). The number of identified proteins known to interact with HSP90 is over 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 signalling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Its activity is regulated by numerous co-chaperones (such as p60/Hop, p50Cdc37, p23) that assist in the chaperoning process. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9). HSP90 is essential for cancer cell survival by stabilizing mutated or overexpressed proteins. This description may include information annotated by UniProt and/or Google AI.