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48-602MAG
Buffer Detection Kit for Magnetic Beads
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14-418
Sigma-Aldrichp300, HAT Domain
Recombinant GST-fusion protein corresponding to amino acids 1066-1707 of human p300.
More>>Recombinant GST-fusion protein corresponding to amino acids 1066-1707 of human p300. Less<<
p300, HAT Domain: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Recombinant GST-fusion protein corresponding to amino acids 1066-1707 of human p300.
Key Applications
Histone Acetyltransferase Assay (HAT)
Biological Information
Source
Expressed in E. coli.
Specific Activity
For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.<br /> Unit definition: 1 Unit is defined as the transfer of 1nmol of [<sup>3</sup>H]-acetate/minute to acid-extracted histones.
EP300 encodes the adenovirus E1A-associated cellular p300 transcriptional co-activator protein. p300 is related by sequence to CBP (CREB-binding protein [CREB: cyclic-AMP responsive element binding protein]), and like CBP can stimulate transcription through activation of CREB. This EP300 activity is specifically inhibited by the adenovirus oncoprotein E1A. EP300 has also been identified as a co-activator of HIF1A (hypoxia-inducible factor 1 alpha), and thus plays a role in the stimulation of hypoxia-induced genes such as VEGF.
FUNCTION: SwissProt: Q09472 # 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. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB 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. SIZE: 2414 amino acids; 264144 Da SUBUNIT: Interacts with phosphorylated CREB1 (By similarity). Interacts with DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, SPIB, SRY, TCF7L2, TP53, SRCAP and TRERF1. The TAZ- type 1 domain interacts with HIF1A. Probably part of a complex with HIF1A and CREBBP. Part of a complex containing CARM1 and NCOA2/GRIP1. Interacts with ING4 and this interaction may be indirect. Interacts with the C-terminal region of CITED4. Interacts with HTLV-1 Tax and p30II. Interacts with and acetylates HIV-1 Tat. SUBCELLULAR LOCATION: Nucleus. PTM: Phosphorylated. & Methylated at Arg-580 and Arg-604 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2142 by CARM1, which impairs interaction with NCOA2/GRIP1. & Citrullinated at Arg-2142 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1. DISEASE: SwissProt: Q09472 # Defects in EP300 may play a role in epithelial cancer. & Chromosomal aberrations involving EP300 may be a cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13) with MYST3. & Defects in EP300 are a cause of Rubinstein-Taybi syndrome (RSTS) [MIM:180849]. RSTS is an autosomal dominant disorder characterized by craniofacial abnormalities, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. SIMILARITY: SwissProt: Q09472 ## Contains 1 bromo domain. & Contains 1 KIX domain. & Contains 2 TAZ-type zinc fingers. & Contains 1 ZZ-type zinc finger.
Molecular Weight
100 kDa
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Routinely evaluated by HAT Assay.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
-20°C for up to 6 months from the date of receipt.
Acetylation of snail modulates the cytokinome of cancer cells to enhance the recruitment of macrophages. Hsu, DS; Wang, HJ; Tai, SK; Chou, CH; Hsieh, CH; Chiu, PH; Chen, NJ; Yang, MH Cancer cell
26
534-48
2014
Snail is primarily known as a transcriptional repressor that induces epithelial-mesenchymal transition by suppressing adherent proteins. Emerging evidence suggests that Snail can act as an activator; however, the mechanism and biological significance are unclear. Here, we found that CREB-binding protein (CBP) is the critical factor in Snail-mediated target gene transactivation. CBP interacts with Snail and acetylates Snail at lysine 146 and lysine 187, which prevents the repressor complex formation. We further identified several Snail-activated targets, including TNF-α, which is also the upstream signal for Snail acetylation, and CCL2 and CCL5, which promote the recruitment of tumor-associated macrophages. Here, we present our results on the mechanism by which Snail induces target gene transactivation to remodel the tumor microenvironment.
HBP1 is a sequence-specific DNA-binding transcription factor with many important biological roles. It activates or represses the expression of some specific genes during cell growth and differentiation. Previous studies have exhibited that HBP1 binds to p16(INK4A) promoter and activates p16(INK4A) expression. We found that trichostatin A (TSA), an inhibitor of HDAC (histone deacetylase), induces p16(INK4A) expression in an HBP1-dependent manner. This result was drawn from a transactivation experiment by measuring relative luciferase activities of p16(INK4A) promoter with HBP1-binding site in comparison with that of the wild-type p16(INK4A) promoter by transient cotransfection with HBP1 into HEK293T cells and 2BS cells. HBP1 acetylation after TSA treatment was confirmed by immunoprecipitation assay. Our data showed that HBP1 interacted with histone acetyltransferase p300 and CREB-binding protein (CBP) and also recruited p300/CBP to p16(INK4A) promoter. HBP1 was acetylated by p300/CBP in two regions: repression domain (K297/305/307) and P domain (K171/419). Acetylation of Repression domain was not required for HBP1 transactivation on p16(INK4A). However, luciferase assay and western blotting results indicate that acetylation of P domain, especially K419 acetylation is essential for HBP1 transactivation on p16(INK4A). As assayed by SA-beta-gal staining, the acetylation of HBP1 at K419 enhanced HBP1-induced premature senescence in 2BS cells. In addition, HDAC4 repressed HBP1-induced premature senescence through permanently deacetylating HBP1. We conclude that our data suggest that HBP1 acetylation at K419 plays an important role in HBP1-induced p16(INK4A) expression.
Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates Schiltz, R L, et al J Biol Chem, 274:1189-92 (1999)
1998