Human PPIase / FKBP7 Protein (Fc Tag)

FKBP23,PPIase

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Catalog Number	P13250-H02H
Organism Species	Human
Host	Human Cells
Synonyms	FKBP23,PPIase
Molecular Weight	The recombinant human FKBP7/Fc is a disulfide-linked homodimer. The reduced monomer comprises 436 amino acids and has a predicted molecular mass of 49.4 kDa. The apparent molecular mass of the protein is approximately 55kDa in SDS-PAGE under reducing conditions.
predicted N	Gln 24
SDS-PAGE
Purity	> 90 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the human FKBP7 (Q9Y680-2) (Met1-Gln218) was expressed, fused with the Fc region of human IgG1 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.