FKBP8 antibody

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Description
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.
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Product specifications
| Category | Primary Antibodies |
| Immunogen Target | FK506 binding protein 8, 38kDa (FKBP8) |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Recommended Dilution | WB: 1:500-1:2000 |
| Clonality | polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Observed MW | 53 kDa |
| Purity | ≥95% as determined by SDS-PAGE |
| Purification | Immunogen affinity purified |
| Size 1 | 100µg |
| Form | liquid |
| Tested Applications | ELISA, WB |
| Storage | PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.) |
| UniProt ID | Q14318 |
| Gene ID | 23770 |
| Alias | Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8),38 kDa FK506-binding protein (38 kDa FKBP, FKBP-38, hFKBP38),FK506-binding protein 8 (FKBP-8),FKBPR38,Rotamase,FKBP8,FKBP38 |
| Background | Antibody anti-FKBP8 |
| Status | RUO |
| Note | Mol. Weight 53 kDa |
Descripción
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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.
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