|Application ||WB, IHC-P, IF, E|
|Other Accession||P97534, Q8HYX6, Q9Z2I2, P68107|
|Predicted||Bovine, Rabbit, Rat|
|Calculated MW||11783 Da|
|Antigen Region||16-46 aa|
|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||This FKBP1B antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 16-46 amino acids from the N-terminal region of human FKBP1B.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||FKBP1B Antibody (N-term) is for research use only and 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.
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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