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Human PPIase / FKBP7 Protein (His Tag)

FKBP23,PPIase

Catalog Number P13250-H08H
Organism Species Human
Host Human Cells
Synonyms FKBP23,PPIase
Molecular Weight The recombinant human FKBP7 consists of 206 amino acids and predicts a molecular mass of 23.8 KDa. It migrates as an approximately 27and 30 KDa band in SDS-PAGE under reducing conditions.
predicted N Gln 24
SDS-PAGE
Purity (84.2+12.5) % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human FKBP7 (Q9Y680-2) (Met1-Gln218) was expressed with a polyhistidine tag at the C-terminus.
Bio-activity
Research Area Immunology |Signal Transduction |Protein Trafficking |ER Proteins
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background 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.
Reference
  • 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.