Anti-FKBP52/FKBP4 Antibody Picoband® Fluoro647 Conjugated

FK506-binding protein 4 is a protein that in humans is encoded by the FKBP4 gene. The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants FK506 and rapamycin. It has high structural and functional similarity to FK506-binding protein 1A (FKBP1A), but unlike FKBP1A, this protein does not have immunosuppressant activity when complexed with FK506. It interacts with interferon regulatory factor-4 and plays an important role in immunoregulatory gene expression in B and T lymphocytes. This encoded protein is known to associate with phytanoyl-CoA alpha-hydroxylase. It can also associate with two heat shock proteins (hsp90 and hsp70) and thus may play a role in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. This protein correlates strongly with adeno-associated virus type 2 vectors (AAV) resulting in a significant increase in AAV-mediated transgene expression in human cell lines. Thus this encoded protein is thought to have important implications for the optimal use of AAV vectors in human gene therapy. The human genome contains several non-transcribed pseudogenes similar to this gene.

Platelet-activating factor acetylhydrolase; PAF acetylhydrolase; 1-alkyl-2-acetylglycerophosphocholine esterase; 2-acetyl-1-alkylglycerophosphocholine esterase; Group-VIIA phospholipase A2; gVIIA-PLA2; LDL-associated phospholipase A2; LDL-PLA (2) ; PAF 2-acylhydrolase; PLA2G7; PAFAH

A synthetic peptide corresponding to a sequence at the C-terminus of human FKBP52/FKBP4, which shares 94.7% amino acid (aa) sequence identity with mouse and rat FKBP4.

Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids.

1. Chambraud, B., Radanyi, C., Camonis, J. H., Rajkowski, K., Schumacher, M., Baulieu, E.-E. Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-CoA alpha-hydroxylase is a new FKBP-associated protein. Proc. Nat. Acad. Sci. 96: 2104-2109, 1999. 2. Chen, H., Yong, W., Hinds, T. D., Jr., Yang, Z., Zhou, Y., Sanchez, E. R., Shou, W. Fkbp52 regulates androgen receptor transactivation activity and male urethra morphogenesis. J. Biol. Chem. 285: 27776-27784, 2010. 3. Cheung-Flynn, J., Prapapanich, V., Cox, M. B., Riggs, D. L., Suarez-Quian, C., Smith, D. F. Physiological role for the cochaperone FKBP52 in androgen receptor signaling. Molec. Endocr. 19: 1654-1666, 2005.