Recombinant Human FKBP12 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2094

Recombinant Human FKBP12 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2094
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Product Overview

Tag His
Host Species Human
Accession NP_463460
Background FK56 binding protein 12 (FKBP12), also known as FKBP1, along with cyclophilin, are two major members of the immunophilin protein family who serve as receptors for the immunosuppressant drugs cyclosporin A and FK56. As a conserved molecules in many eukaryotes, FKBP12 has been characterized as a peptidyl-prolyl isomerase that catalyzes the transition between cis- and trans-proline residues, and is involved in several biochemical processes including protein folding, receptor signaling, protein trafficking and transcription. FKBP12 has attracted immense attention and its role in mediating the immunosuppressive functions. FKBP12 serves a dual role as a peptidyl-prolyl cis-trans isomerase and as a modulator of several cell signaling pathways. In one such a role, FKBP12 interacts with and regulates the functional state of the ryanodine Ca2+ channel receptor by altering protein conformation and coordinating multi-protein complex formation. Another physiological role of FKBP12 is an interactor and a regulator of the type I serine/threonine kinase receptors of TGF-beta superfamily. Current data, derived from detailed biochemical studies as well as from functional studies in various systems, suggest that FKBP12 functions as a "guardian" for the type I receptors to prevent them from leaky signaling under sub-optimal ligand concentrations, thereby providing a molecular "gradient reader" for TGF-beta family morphogens. This aspect of FKBP12 function may be critical for cellular responsiveness to morphogenetic gradients of the TGF-beta family members during early development, serving to assure the translation of different ligand concentrations into different signaling readouts. In addition, FKBP12 may be involved in neuronal or astrocytic cytoskeletal organization and in the abnormal metabolism of tau protein in Alzheimer's disease (AD) damaged neurons.
Description A DNA sequence encoding the human FKBP12 (NP_463460) (Met 1-Glu 108) was expressed with a C-terminal His tag.
Source E.coli
Predicted N Terminal Met 1
AA Sequence Met 1-Glu 108
Molecular Weight The recombinant human FKBP12 consists of 114 a.a. and predicts a molecular mass of 12.9 kDa as estimated by SDS-PAGE.
Purity >96% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, 10% glycerol, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular Location Cytoplasm, cytosol. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
Protein Families FKBP-type PPIase family, FKBP1 subfamily
Database References

Gene Functions References

  1. These findings of this study suggested that FKBP12 is linked to the accumulation of alpha-SYN and phosphorylated tau protein in alpha-synucleinopathies. FKBP12 may play important roles in the pathogenesis of alpha-synucleinopathies. PMID: 29246765
  2. FKBP12 binding is required for full Met activation and everolimus can inhibit Met PMID: 27223077
  3. Specifically tested on two model systems, the power of iSPOT is demonstrated to accurately predict the structures of a large protein-protein complex (TGFbeta-FKBP12) and a multidomain nuclear receptor homodimer (HNF-4alpha), based on the structures of individual components of the complexes. PMID: 27496803
  4. These results identify a novel function for FKBP12 in downregulating MDM2, which directly enhances sensitivity of cancer cells to chemotherapy and nutlin-3 treatment. PMID: 27617579
  5. Data show that FKBP12 (FK506 binding protein 1A)conformational transition Is coupled to histidine tautomerization. PMID: 27936610
  6. Electrostatic effects on the folding stability of FKBP12 PMID: 27381026
  7. Findings indicate that mutant huntingtin (mHTT) aggregates can be transformed into benign species by isomerase FKBP12. PMID: 26450664
  8. RyRs have been identified as important targets of FKBP12 and FKBP12.6, members of the immunophilin family PMID: 26009182
  9. How phosphorylation of RyR affects channel activity and whether proteins such as the FK-506 binding proteins (FKBP12 and FKBP12.6) are involved in heart failure PMID: 26009186
  10. Ultra-fast Shape Recognition with Atom Types--the discovery of novel bioactive small molecular scaffolds for FKBP12 and 11betaHSD1. PMID: 25659145
  11. Selectivity within the FKBP family, in particular selective inhibition of FKBP12 or FKBP51, is possible. FKBP51 is a pharmacologically tractable target for stress-related disorders. PMID: 25615537
  12. peptidyl prolyl cis-trans isomerase activity of FKBP12 probably plays a role in inhibition of receptor phosphorylation. PMID: 24607931
  13. FKBP12 inhibits RyR1 and FKBP12 E31Q/D32N/W59F mutant activates RyR1 in vitro. PMID: 24559985
  14. FKBP12 regulates the localization and processing of amyloid precursor protein in human cell lines. PMID: 24499793
  15. Enhanced plasticity in the active site of FKBP12.6 is likely to contribute to marked attenuation in the spatial extent of the residues that exhibit doubling of their amide resonances compared with those of the homologous FKBP12. PMID: 24598733
  16. the structural basis of the slow resonance doubling transition of FKBP12 and the more rapid conformational linebroadening transition in the 80's loop to gain insight into how these effects are propagated through the protein structure PMID: 24405377
  17. the association of FKBP12 with OPRM1 attenuates the phosphorylation of the receptor and triggers the recruitment and activation of PKCepsilon. PMID: 24113748
  18. The K44V mutation selectively reduces the line-broadening in the 40's loop, verifying that at least three distinct conformational transitions underlie the line-broadening processes of FKBP12. PMID: 23688288
  19. N-terminal and central domain elements are closely apposed near the FKBP12 binding site within the RyR1 three-dimensional structure. PMID: 23585572
  20. These data corroborate other studies suggesting that mutations in FKBP12 and FKBP12.6 genes are not commonly related to cardiac diseases. PMID: 22236651
  21. The study provides biochemical evidence of the interaction between FKBP12 and RYR1, RYR3 and IP3R. PMID: 22100703
  22. Results suggest that FKBP12 forms an endogenous inhibitor of EGFR phosphorylation directly involved in control of cellular EGFR activity (as in carcinoma). PMID: 22103444
  23. FKBP12 is the most important PPIase modulating alpha-SYN aggregation and validate the protein as an interesting drug target for Parkinson disease PMID: 21652707
  24. It is likely that in FKBP12-ligand complexes, tryptophan 59 provides added binding energy at the active site at the expense of protein stability, a characteristic common to other proteins. PMID: 12600203
  25. folding and kinetics of human FKBP12 PMID: 12850152
  26. the central binding site for the 12 kDa FK506-binding protein of type-3 ryanodine receptor, encompassing the critical valine proline motif, plays a crucial role in the modulation of the Ca2+ release properties PMID: 14970260
  27. experimental data on the stability of FKBP12 are reported for the effects of three environmental variables: pH, salt, and macromolecular crowding PMID: 15992823
  28. The spinal horn neurons stained with anti-FKBP 12 antibody was significantly decreased in the motor neuron disease cases compared to that in controls. PMID: 16036432
  29. FKBP12 accelerated the aggregation of alpha-synuclein in vitro. PMID: 16410343
  30. These findings indicate a new inhibitory function of FKBP12 as an adaptor molecule for the Smad7-Smurf1 complex to regulate the duration of the activin signal through activin type I receptors. PMID: 16720724
  31. characterization of the stability, binding and enzymatic properties of three FK506 binding proteins (FKBP-12) differing only by the length and sequence of their N-terminus PMID: 16908189
  32. Data show that insertion of a chaperone domain from E. coli SlyD converts human FKBP12 into a powerful catalyst of protein folding. PMID: 17397867
  33. FKBP12.0-RyR2 interaction can regulate the gain of excitation-contraction coupling in cardiomyocytes PMID: 17872463
  34. FKBP12 is predominantly present during early neointima formation, while mature neointimal atheromas show a relatively low expression without confinement to luminal areas. PMID: 17962721
  35. fndings suggest that the peptidyl-prolyl isomerase activity requires only the hydrophobic cavity that captures the Pro-containing peptide PMID: 18029417
  36. We investigated in detail the effect of FKBP12 on early aggregation and on fibril formation of wild-type, A53T and A30P alpha-SYN. FKBP12 has a much smaller effect on the fibril formation of these two clinical mutants of alpha-SYN. PMID: 18346205
  37. CCI-779 inhibits mTOR signaling through an FKBP12-independent mechanism that leads to profound translational repression in cancer cells. PMID: 18413763
  38. our results suggest that FKBP12 may be involved in neuronal or astrocytic cytoskeletal organization and in the abnormal metabolism of tau protein in Alzheimer's disease damaged neurons PMID: 19414059


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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