|Other Names||Peptidyl-prolyl cis-trans isomerase FKBP1B, PPIase FKBP1B, 126 kDa FK506-binding protein, 126 kDa FKBP, FKBP-126, FK506-binding protein 1B, FKBP-1B, Immunophilin FKBP126, Rotamase, h-FKBP-12, FKBP1B, FKBP126, FKBP1L, FKBP9, OTK4|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7868a was selected from the N-term region of human FKBP1B. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||FKBP12.6, FKBP1L, FKBP9, OTK4|
|Function||Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.|
|Cellular Location||Cytoplasm. Sarcoplasmic reticulum|
|Tissue Location||Detected in heart muscle (at protein level). Isoform 1 and isoform 2 are ubiquitous with highest levels in brain and thymus.|
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Provided below are standard protocols that you may find useful for product applications.
FKBP1B is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. The protein is highly similar to the FK506-binding protein 1A. Its physiological role is thought to be in excitation-contraction coupling in cardiac muscle. There are two alternatively spliced transcript variants of this gene encoding different isoforms.
Arakawa H., Nagase H.Biochem. Biophys. Res. Commun. 200:836-843(1994) Lam E., Martin M.M., Timerman A.P.Biol. Chem. 270:26511-26522(1995)Deivanayagam C.C., Carson M.Acta Crystallogr. D 56:266-271(2000)
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