|Reactivity||Human, Mouse, Rat|
|Calculated MW||43529 Da|
|Application & Usage||Western blotting (0.5-4 µg/ml). However, the optimal concentrations should be determined individually. Blocking peptide is available separately. The antibody recognizes a ~40 kDa band in samples from human, mouse and rat origins. Reactivity to other species has not been tested.|
|Other Names||FKBPR38 , FKBP8 , FKBP 8 , FK506 binding protein 8 , FKBP 38|
|Formulation||100 µg (0.2mg/ml) protein A purified rabbit anti-FKBP38 polyclonal antibody in phosphate-buffered saline (PBS) containing 0.1% BSA, 20% glycerol, and 0.02% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||FKBP38 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis (By similarity). Required for normal embryonic development.|
|Cellular Location||Mitochondrion membrane; Single-pass membrane protein; Cytoplasmic side|
|Tissue Location||Detected throughout the embryonic body, in caudal neural tube, limbs and head. Detected in adult retina, brain, heart, kidney, liver, pancreas, lung, testis and urinary bladder (at protein level). Detected in adult brain, kidney, liver, testis and trigeminal nerve, and in embryo. Detected at lower levels in lung, spleen, heart and ovary. Widely expressed in forebrain. Detected in the Purkinje cell layer in the cerebellum and in hippocampus neurons.|
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FK506-binding protein 38 (FKBP38), a member of the immunophilin family, has been implicated to play an important role in apoptosis thro µgh its involvement in the mechanism that targets Bcl-2 and Bcl-xL to the outer mitochondrial membrane (OMM). Suppression of endogenous FKBP38 by RNAi or transfection of a mutant FKBK38 missing the transmembrane domain necessary for mitochondrial insertion, resulted in the translocation of Bcl-2 and Bcl-xL from the OMM to the cytosol. It has also been s µggested that FKBP38 may play a role in the cross-talk between the Bcl-2 and the Calcineurin/NF-AT apoptosis signaling pathways and in cell size regulation thro µgh interactions with tuberous sclerosis genes.
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