SRP2079
p300 human
recombinant, expressed in insect cells, ≥70% (SDS-PAGE)
Sinónimos:
KAT3B, RP1-85F18.1, RSTS2, p300
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About This Item
Código UNSPSC:
12352200
NACRES:
NA.26
Productos recomendados
origen biológico
human
recombinante
expressed in insect cells
Ensayo
≥70% (SDS-PAGE)
Formulario
frozen liquid
mol peso
~265 kDa
envase
pkg of 4 μg
concentración
500 μg/mL
color
clear colorless
Nº de acceso NCBI
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−70°C
Información sobre el gen
human ... EP300(2033)
Descripción general
E1A binding protein p300 (p300) has a central bromodomain and three cysteine- and histidine-rich regions. The carboxy-terminal region interacts with the adenovirus oncoprotein E1A. The gene encoding this protein is localized on human chromosome 22q13.[1] P300 is full length recombinant protein with flag tag at its N-terminus.
Aplicación
Acciones bioquímicas o fisiológicas
EP300 and CREBBP are highly related transcriptional coactivators mediating cAMP gene regulation. EP300 is known to acetylate many transcription factors, including p53, E2F, TFIIE, and TFIIF.
EP300 and CREBBP are highly related transcriptional coactivators mediating cAMP gene regulation. EP300 is known to acetylate many transcription factors, including p53, E2F, TFIIE, and TFIIF.
p300 activates transcription of E-cadherin, which helps to retain the cell in an epithelial state. p300 plays an essential role in integrating and mediating multiple signal-dependent transcription events. It acts as a histone acetyltransferase and controls transcription through chromatin remodeling. Mutation in the gene has been observed in various types of malignancies.[4]
p300 activates transcription of E-cadherin, which helps to retain the cell in an epithelial state. p300 plays an essential role in integrating and mediating multiple signal-dependent transcription events. It acts as a histone acetyltransferase and controls transcription through chromatin remodeling. Mutation in the gene has been observed in various types of malignancies.[4]
Human p300 and CBP (CREB binding protein) are highly related transcriptional coactivators. Both proteins have been identified through protein interaction assays. In addition to interacting with a variety of cellular factors and onco-proteins, loss of the wild type CBP alleles in isolated tumors suggests that CBP/p300 might serve as tumor suppressors. The ability of p300 to acetylate many transcription factors, including p53, E2F, TFIIE, and TFIIF etc. demonstrates a novel mechanism of targeted p300 regulation of gene expression.
Forma física
Clear and colorless frozen liquid solution
Nota de preparación
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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Certificados de análisis (COA)
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Acetylation-dependent regulation of MDM2 E3 ligase activity dictates its oncogenic function.
Nihira N T, et al.
Science Signaling, 10(466), eaai8026-eaai8026 (2017)
mTORC1 Phosphorylates Acetyltransferase p300 to Regulate Autophagy and Lipogenesis.
Wan W, et al.
Molecular Cell, 68(2), 323-335 (2017)
Pedro Latorre-Muro et al.
The Journal of biological chemistry, 296, 100205-100205 (2020-12-19)
Acetylation is known to regulate the activity of cytosolic phosphoenolpyruvate carboxykinase (PCK1), a key enzyme in gluconeogenesis, by promoting the reverse reaction of the enzyme (converting phosphoenolpyruvate to oxaloacetate). It is also known that the histone acetyltransferase p300 can induce
Tumour suppressor EP300, a modulator of paclitaxel resistance and stemness, is downregulated in metaplastic breast cancer.
Asaduzzaman M, et al.
Breast Cancer Research and Treatment, 163(3), 461-474 (2017)
R W Stein et al.
Journal of virology, 64(9), 4421-4427 (1990-09-01)
Adenovirus E1A transforming function requires two distinct regions of the protein. Transforming activity is closely linked with the presence of a region designated conserved domain 2 and the ability of this region to bind the product of the cellular retinoblastoma
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