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Item number | Size | Datasheet | Manual | SDS | Delivery time | Quantity | Price |
---|---|---|---|---|---|---|---|
009-001-S27S | 20 µg | - | - |
6 - 10 business days* |
482.00€
|
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You can also order by e-mail: info@biomol.com
Larger quantity required? Request bulk
You can also order by e-mail: info@biomol.com
Larger quantity required? Request bulk
Recombinant human KAT3B (EP300) (532-1153, contains the catalytic domain) was expressed by... more
Product information "KAT3B (EP300) protein-GST fusion"
Recombinant human KAT3B (EP300) (532-1153, contains the catalytic domain) was expressed by baculovirus in Sf9 insect cells using an N-Terminal Glutathione-S-Transferase fusion protein. The purity was determined to be >80% by densitometry. Protein function: Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac). Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity. Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription, exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter. Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:10733570, PubMed:11430825, PubMed:11701890, PubMed:12402037, PubMed:12586840, PubMed:12929931, PubMed:14645221, PubMed:15186775, PubMed:15890677, PubMed:16617102, PubMed:16762839, PubMed:18722353, PubMed:18995842, PubMed:23415232, PubMed:23911289, PubMed:23934153, PubMed:8945521). Acetylates XBP1 isoform 2, acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178). Acetylates PCNA, acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). Acetylates MEF2D. [The UniProt Consortium]
Keywords: | P300, EP300, p300 HAT, E1A-associated protein p300, Histone acetyltransferase p300 |
Supplier: | Rockland Immunochemicals |
Supplier-Nr: | 009-001-S27S |
Properties
Application: | WB |
Conjugate: | No |
Host: | Human |
Database Information
KEGG ID : | K04498 | Matching products |
UniProt ID : | Q09472 | Matching products |
Gene ID : | GeneID 2033 | Matching products |
Handling & Safety
Storage: | -80°C |
Shipping: | -20°C (International: -20°C) |
Caution
Our products are for laboratory research use only: Not for administration to humans!
Our products are for laboratory research use only: Not for administration to humans!
Information about the product reference will follow.
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