FKBP7 Proteins, Antibodies, cDNA Clones Research Reagents

All FKBP7 reagents are produced in house and quality controlled, including 3 FKBP7 Antibody, 15 FKBP7 Gene, 1 FKBP7 IP Kit, 2 FKBP7 Lysate, 2 FKBP7 Protein, 1 FKBP7 qPCR. All FKBP7 reagents are ready to use.

FKBP7 Protein (2)

    FKBP7 Antibody (3)

      FKBP7 cDNA Clone (15)

      BC009711

      クローニングベクター cDNA 製品

      In lentiviral vector

      XM_006234400.3

      クローニングベクター cDNA 製品

      In lentiviral vector

      FKBP7 qPCR Primer (1)

      FKBP7 Lysate (2)

        FKBP7 の背景知識

        PPIase is a member of the immunophilin protein family. It also belongs to the cyclophilin-type PPIase family, PPIL3 subfamily. PPIase contains 1 PPIase cyclophilin-type domain. Members of the immunophilin protein family play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. It has a very high substrate specificity for the four-residue peptide Ala-Ala-Pro-Phe only when the proline peptide bond is in the trans state. It interacts with several intracellular signal transduction proteins including type I TGF-beta receptor. It also interacts with multiple intracellular calcium release channels, and coordinates multi-protein complex formation of the tetrameric skeletal muscle ryanodine receptor. In mouse, deletion of this homologous gene causes congenital heart disorder known as noncompaction of left ventricular myocardium.

        FKBP7 の参考文献

        • 1. Shor B, et al. (2008) A new pharmacologic action of CCI-779 involves FKBP12-independent inhibition of mTOR kinase activity and profound repression of global protein synthesis. Cancer Res. 68(8):2934-43.
        • 2. Talmud PJ, et al. (2009) Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip. Am J Hum Genet. 85(5):628-42.
        • 3. Deleersnijder A, et al. (2011) Comparative analysis of different peptidyl-prolyl isomerases reveals FK506-binding protein 12 as the most potent enhancer of alpha-synuclein aggregation. J Biol Chem. 286(30):26687-701.

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