Recombinant Mouse FKBP12 protein is a Mouse Full Length protein, in the 1 to 108 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
M G S S H H H H H H S S G L V P R G S H M G S H M G V Q V E T I S P G D G R T F P K R G Q T C V V H Y T G M L E D G K K F D S S R D R N K P F K F T L G K Q E V I R G W E E G V A Q M S V G Q R A K L I I S S D Y A Y G A T G H P G I I P P H A T L V F D V E L L K L E
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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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 (By similarity).
Fkbp1, Fkbp1a, Peptidyl-prolyl cis-trans isomerase FKBP1A, PPIase FKBP1A, 12 kDa FK506-binding protein, Calstabin-1, FK506-binding protein 1A, Immunophilin FKBP12, Rotamase, 12 kDa FKBP, FKBP-12, FKBP-1A
Recombinant Mouse FKBP12 protein is a Mouse Full Length protein, in the 1 to 108 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
pH: 7.4
Constituents: 79% PBS, 20% Glycerol (glycerin, glycerine), 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab201895 was purified using conventional chromatography techniques.
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 (By similarity).
Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
FKBP12 also known as FKBP-12 or FKBP12 protein is a small protein with a molecular weight of approximately 12 kDa. It belongs to the family of immunophilins and acts as a peptidyl-prolyl cis-trans isomerase (PPIase) facilitating the folding of proteins by catalyzing the isomerization of proline residues in polypeptides. The FKBP12 protein is expressed in various tissues throughout the body including the brain heart and skeletal muscles. It plays a mechanical role in binding certain macrolide antibiotics such as FK506 (tacrolimus) influencing their biological effects by altering protein conformation.
FKBP12 is significant in cellular mechanisms beyond protein folding. It interacts with and forms complexes with other proteins such as ryanodine receptors and transforming growth factor-beta (TGF-β) receptors impacting calcium signaling and cell growth. FKBP12's interaction with FK506 has been extensively studied because it forms a complex that inhibits calcineurin ultimately leading to immunosuppressive effects. This property of FKBP12 makes it important for modulating the immune response and has importance in transplant medicine.
FKBP12 is actively involved in calcium signaling and TGF-β signaling pathways. FKBP12 influences these pathways by binding to ryanodine receptors affecting calcium release from intracellular stores and also modulating the function of TGF-β receptors impacting cellular growth and proliferation processes. It is associated with proteins such as calcineurin and Smad proteins in these pathways maintaining cellular homeostasis and regulating immune and inflammatory responses.
FKBP12 plays a role in immunological and proliferative diseases. It is implicated in autoimmune disorders due to its interaction with FK506 leading to the suppression of unwanted immune responses. FKBP12 is also linked to cardiac hypertrophy as its modulation of calcium release through ryanodine receptors can affect heart muscle function. The protein interacts with calcineurin in these contexts contributing to pathological processes in these diseases. Researchers target FKBP12 with ELISA and other assays to investigate its involvement in these disorders and assess therapeutic interventions.
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15% SDS-PAGE analysis of ab201895 (3μg).
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