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Recombinant BRD4 (44-168) protein
Recombinant BRD4 (44-168) protein
- 中文名称:
- Recombinant BRD4 (44-168) protein
- 英文名称:
- Recombinant BRD4 (44-168) protein
- 品牌:
- AAA Biotech
- 品牌介绍:
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具,核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号:
- AAA59648
- 规格:
- 0.1 mg|1 mg|2x1 mg|3x1 mg|4x1 mg
- 保存建议:
- Recombinant proteins in solution are temperature sensitive and must be stored at -80 degree C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage.
Shipping Temp: Dry Ice
- 货期:
- 6-8周
- 纯度:
- The recombinant protein is >90% pure by SDS-PAGE.
- 产品形式:
- Recombinant BRD4 (44-168) protein was expressed in E Coli and is supplied in 25mM Tris-HCl pH8.0, 300mM NaCl and 10% glycerol.
- 免责声明:
- *本产品仅供科研实验使用,不得用于临床诊断。*
- 说明书:
Short Description: The peptide corresponding to amino acids 44-168 that contains the bromodomain sequences of BRD4 (accession number NM_058243.2) was expressed in E Coli and contains an N-terminal His-tag and C-terminal DYKDDDDK tag with an observed molecular weight of 30 kDa. It shows binding specificity for acetylated H3K9, H3K9/K14, H4K5, H4K8, H4K12, H4K5/K8, H4K5/K12, H4K8/K12, H4K12/K16, H4K12/K16/K20 and H4K5/K8/K12/K16, as well as acetylated RelA-K310. Bromodomain-containing protein 4 (BRD4) belongs to the BET subclass of proteins, which are characterized by two N-terminal bromodomains and one ET (Extra Terminal) domain. BRDs associate with chromatin through their bromodomains that recognize acetylated histone lysine residues. Bromodomains function as 'readers' of these epigenetic histone marks and regulate chromatin structure and gene expression by linking associated proteins to the acetylated nucleosomal targets. The ET domain functions as a protein binding motif and exerts atypical serine-kinase activity. The BET family consists of at least four members in mouse and human, BRD2 (also referred to as FSRG1, RING3), BRD3 (FSRG2, ORFX), BRD4 (FSRG4, MCAP/HUNK1), and BRDT (FSRG3, BRD6). BRD proteins are related to the female sterile homeotic protein gene in Drosophila, a gene required maternally for proper expression of other homeotic genes, such as Ubx, which is involved in pattern formation. BRD4 has been identified recently as a therapeutic target in many cancers, including acute myeloid leukemia, multiple myeloma, Burkitt's lymphoma, NUT midline carcinoma, colon cancer, and breast cancer. BRD4 regulates the transcription of oncogenes, HIV, and human papilloma virus (HPV). It has been shown to bind and phosphorylate RNA pol II, which implicates its involvement in the regulation of eukaryotic transcription. Recombinant BRD4 (44-168) can be used in binding assays and inhibitor screening.
Background: Bromodomain-containing protein 4 (BRD4) belongs to the BET subclass of proteins, which are characterized by two N-terminal bromodomains and one ET (Extra Terminal) domain. BRDs associate with chromatin through their bromodomains that recognize acetylated histone lysine residues. Bromodomains function as 'readers' of these epigenetic histone marks and regulate chromatin structure and gene expression by linking associated proteins to the acetylated nucleosomal targets. The ET domain functions as a protein binding motif and exerts atypical serine-kinase activity. The BET family consists of at least four members in mouse and human, BRD2 (also referred to as FSRG1, RING3), BRD3 (FSRG2, ORFX), BRD4 (FSRG4, MCAP/HUNK1), and BRDT (FSRG3, BRD6). BRD proteins are related to the female sterile homeotic protein gene in Drosophila, a gene required maternally for proper expression of other homeotic genes, such as Ubx, which is involved in pattern formation. BRD4 has been identified recently as a therapeutic target in many cancers, including acute myeloid leukemia, multiple myeloma, Burkitt's lymphoma, NUT midline carcinoma, colon cancer, and breast cancer. BRD4 regulates the transcription of oncogenes, HIV, and human papilloma virus (HPV). It has been shown to bind and phosphorylate RNA pol II, which implicates its involvement in the regulation of eukaryotic transcription.