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Recombinant BRD3 (306-416) protein
Recombinant BRD3 (306-416) protein
- 中文名称：
- Recombinant BRD3 (306-416) protein
- 英文名称：
- Recombinant BRD3 (306-416) 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：
- AAA59645
- 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 >70% pure by SDS-PAGE.
- 产品形式：
- Recombinant BRD3 (306-416) protein was expressed in E Coli cells and is supplied in 25mM Tris pH7.4, 150mM NaCl, 5% 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 306-416 that contains the bromodomain sequences of BRD3 (accession number NM_007371.3) was expressed in E Coli and contains an N-terminal His-tag and C-terminal DYKDDDDK tag with an observed molecular weight of 19.2 kDa. It shows binding specificity for acetylated H4K8 and H4K12/K16/K20, as well as acetylated GATA1. Bromodomain-containing protein 3 (BRD3), also known as RING3L, belongs to the BET subclass of proteins 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). BRD3 binds and regulates GATA1 in an acetylation-dependent manner. GATA1 is a key regulator of gene expression for erythroid and megakaryocyte-specific genes, and mutations in GATA1 have been associated with congenital anemias and megakaryoblastic leukemias. Interestingly, tight interaction of BRD3 with GATA1 requires multiple acetylation modifications, and structural data showed that two adjacent acetylation sites in GATA1 interact with a single bromodomain. BRD3 protein expression is induced in activated lymphocytes. Additionally, it is highly expressed in undifferentiated ES cells and expression is observed to drop upon endothelial differentiation. Altered expression levels of BRD3 have been observed in certain cancers, such as nasopharyngeal carcinomas and bladder cancer. BRD3 also interacts with LANA-1, the Kaposi's sarcoma-associated herpesvirus (KSHV) latency-associated nuclear antigen 1, which is required for the replication of episomal viral genomes. Recombinant BRD3 (306-416) can be used in binding assays and inhibitor screening.
Background: Bromodomain-containing protein 3 (BRD3), also known as RING3L, belongs to the BET subclass of proteins 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). BRD3 binds and regulates GATA1 in an acetylation-dependent manner. GATA1 is a key regulator of gene expression for erythroid and megakaryocyte-specific genes, and mutations in GATA1 have been associated with congenital anemias and megakaryoblastic leukemias. Interestingly, tight interaction of BRD3 with GATA1 requires multiple acetylation modifications, and structural data showed that two adjacent acetylation sites in GATA1 interact with a single bromodomain. BRD3 protein expression is induced in activated lymphocytes. Additionally, it is highly expressed in undifferentiated ES cells and expression is observed to drop upon endothelial differentiation. Altered expression levels of BRD3 have been observed in certain cancers, such as nasopharyngeal carcinomas and bladder cancer. BRD3 also interacts with LANA-1, the Kaposi's sarcoma-associated herpesvirus (KSHV) latency-associated nuclear antigen 1, which is required for the replication of episomal viral genomes.
