€548.00 €465.80
Bromodomain-containing protein 4 (BRD4) is a member of the bromodomain and extra-terminal domain (BET) family.{33144} It is a ubiquitously expressed nuclear protein with roles in a variety of cellular processes, including regulation of gene transcription, cell cycle progression, and viral genome segregation.{33144,49639} BRD4 is comprised of two N-terminal bromodomains (BD1 and BD2) that can bind to acetylated lysine residues in histones, serving to couple histone acetylation marks to the transcriptional regulation of target promoters, an extra-terminal (ET) domain that facilitates protein-protein interactions, and a C-terminal motif, and can be expressed as either a long or short isoform generated via alternative splicing.{33144,49639,49640} In addition to binding acetylated lysine residues on histones, BRD4 can bind to a variety of non-histone proteins and protein complexes, including positive transcription elongation factor b (P-TEFb) and the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) envelope (E) protein, a transmembrane protein involved in CoV virion assembly and pathogenesis of the related virus, SARS-CoV.{33144,55024,53462,49521} In mice, knock-down of Brd4 is embryonic lethal.{49639} Chromosomal translocations leading to the fusion of BRD4 with the nuclear protein in testis (NUT) gene and resulting in expression of BRD4-NUT fusion proteins are associated with NUT midline carcinoma (NMC).{33144,49640} Inhibition of BRD4-NUT binding to chromatin by the BET bromodomain inhibitor (+)-JQ1 (Item No. 11187) induces tumor regression and prolongs survival in NMC mouse xenograft models.{19004} Cayman’s BRD4 bromodomain 1 (human, recombinant; His-tagged) protein can be used for ELISA, Western blot (WB), and binding assay applications.
Territorial Availability: Available through Bertin Technologies only in France
| Size | 100 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | 0 |
| Formulation | 50 mM Tris, pH 8.0, with 500 mM NaCl, 5% glycerol, and 1 mM DTT |
| Purity | ≥90% |
| Custom code | 3504.00 |
| UNSPSC code | 12352204 |
Cayman Chemical’s mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.
Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.
Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.
Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.
Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009
Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.
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