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- rabbit polyclonal IgG, 200 µg/ml
- raised against amino acids 451-720 mapping within the CREB Binding Domain of CBP of mouse origin.
- recommended for detection of CBP p265 and p300 of mouse, rat and human origin by WB, IP, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
- TransCruz reagent for Gel Supershift and ChIP applications, sc-1211 X, 200 µg/0.1 ml
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Informazioni ordiniCitazioni prodotti
Recommended Support Products:
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| Specie |
Nome del gene |
Codice del gene |
Locus cromosoma |
Isoform (mRNA) Accession # |
codice accesso proteina |
Numero d'ordine |
| Umano |
CREBBP |
1387 |
16p13.3 |
NM_004380 |
Q92793
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600140 |
| Mouse |
Crebbp |
12914 |
16 A1 |
|
P45481
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N/A |
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CBP Background Information Cyclic AMP-regulated gene expression frequently involves a DNA element designated the cAMP-regulated enhancer (CRE). Many transcription factors bind to this element, including the protein CREB, which is activated as a result of phosphorylation by protein kinase A. It has been shown that protein kinase A-mediated CREB phosphorylation results in its binding to a nuclear protein designated CBP (for CREB-binding protein). These findings suggest that CBP has many of the properties expected of a CREB co-activator. Another high molecular weight transcriptional adapter protein, designated p300, is characterized by three cysteine- and histidine-rich regions, of which the most carboxy terminal region specifically binds the adenovirus E1A protein. p300 molecules lacking an intact E1A binding site bypass E1A repression, even in the presence of high concentrations of E1A. Sequence analysis of CBP and p300 has revealed substantial homology, arguing that these proteins are members of a conserved family of co-activators.
| CBP (451) Citazioni prodotti |
Visualizza come altri ricercatori hanno utilizzato l'anticorpo CBP (451): sc-1211 e/o i coniugati per l'anticorpo CBP (451).
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CBP (451)
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CBP (451) : sc-1211. Western blot analysis of truncated rat recombinant CBP CREB binding domain fusion protein.
ChIP analysis of coactivator recruitment on Cyclin D2 promoter in C2C12 cells treated with LiCl and serum. Antibodies tested include β-catenin (H-102): sc-7199, β-catenin (C-18): sc-1496, β-catenin (E-5): sc-7963, Tip60 (N-17): sc-5725, TRRAP (T-17): sc-5405, TRRAP (Y-18): sc-12375, TRRAP (F-20): sc-12376, TRRAP (H-300): sc-11411, CBP (A-22): sc-369, CBP (C-20): sc-583, CBP (451): sc-1211, CPB (C-1): sc-7300, p300 (H-272): sc-8981, p300 (N-15): sc-584 and p300 (C-20): sc-585. Data kindly provided by M.G. Rosenfeld and reproduced with permission from Kioussi et al., Cell 2002, 111: 673-685.
ChIP analysis of cofactor occupancy dynamics on the ICAM1 promoter in 293 cells in response to IL-1β treatment. Antibodies tested include NFκB p50 (C-19): sc-1190, NFκB p50 (E-10): sc-8414, NFκB p50 (H-119): sc-7178, NFκB p65 (C-20): sc-372, NFκB p65 (A): sc-109, NFκB p65 (H-286): sc-7151, Bcl-3 (C-14): sc-185, Bcl-3 (H-146): sc-13038, PCAF (C-16): sc-6300, PCAF (H-369): sc-8999, CBP (A-22): sc-369, CBP (C-1): sc-7300, CBP (C-20): sc-583, CBP (451): sc-1211. Data kindly provided by M.G. Rosenfeld and reproduced with permission from Baek et al., Cell 2002, 110: 55-67.
ChIP analysis of cofactor occupancy dynamics on the IL-8 promoter in 293 cells in response to IL-1β treatment. Antibodies tested include NFκB p50 (C-19): sc-1190, NFκB p50 (E-10): sc-8414, NFκB p50 (H-119): sc-7178, NFκB p65 (C-20): sc-372, NFκB p65 (A): sc-109, NFκB p65 (H-286): sc-7151, CBP (A-22): sc-369, CBP (C-1): sc-7300, CBP (C-20): sc-583, CBP (451): sc-1211, p300 (C-20): sc- sc-585, p300 (N-15): sc-584, p300 (H-272): sc-8981. Data kindly provided by M.G. Rosenfeld and reproduced with permission from Baek et al., Cell 2002, 110: 55-67.
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