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Recombinant Human Brd4 protein is a Human Fragment protein, in the 49 to 170 aa range, expressed in Escherichia coli, with >=98% purity and suitable for SDS-PAGE.

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Images

SDS-PAGE - Recombinant Human Brd4 protein (AB176936), expandable thumbnail

Key facts

Purity
>=98% SDS-PAGE
Expression system
Escherichia coli
Tags
His tag N-Terminus
Applications
SDS-PAGE
Biologically active
No

Amino acid sequence

E T S N P N K P K R Q T N Q L Q Y L L R V V L K T L W K H Q F A W P F Q Q P V D A V K L N L P D Y Y K I I K T P M D M G T I K K R L E N N Y Y W N A Q E C I Q D F N T M F T N C Y I Y N K P G D D I V L M A E A L E K L F L Q K I N E L P T E E T E

Reactivity data

Application
SDS-PAGE
Reactivity
Reacts
Dilution info
-
Notes

-

Associated Products

Select an associated product type

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Target data

Function

Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation (PubMed:20871596, PubMed:23086925, PubMed:23317504, PubMed:29176719, PubMed:29379197). Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:22334664, PubMed:23317504, PubMed:23589332). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (By similarity). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:23086925). According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B (PubMed:19103749). Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (PubMed:23317504). Isoform B. Acts as a chromatin insulator in the DNA damage response pathway. Inhibits DNA damage response signaling by recruiting the condensin-2 complex to acetylated histones, leading to chromatin structure remodeling, insulating the region from DNA damage response by limiting spreading of histone H2AX/H2A.x phosphorylation.

Alternative names

Recommended products

Recombinant Human Brd4 protein is a Human Fragment protein, in the 49 to 170 aa range, expressed in Escherichia coli, with >=98% purity and suitable for SDS-PAGE.

Key facts

Purity
>=98% SDS-PAGE
Expression system
Escherichia coli
Applications
SDS-PAGE
Accession
O60885-1
Animal free
No
Species
Human
Concentration
Loading...
Storage buffer

pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.61% Tris

Sequence info

Amino acid sequence

E T S N P N K P K R Q T N Q L Q Y L L R V V L K T L W K H Q F A W P F Q Q P V D A V K L N L P D Y Y K I I K T P M D M G T I K K R L E N N Y Y W N A Q E C I Q D F N T M F T N C Y I Y N K P G D D I V L M A E A L E K L F L Q K I N E L P T E E T E
Accession
O60885
Protein length
Fragment
Predicted molecular weight
14.6 kDa
Amino acids
49 to 170
Nature
Recombinant
Tags
His tag N-Terminus

Specifications

Form
Liquid

General info

Function

Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation (PubMed:20871596, PubMed:23086925, PubMed:23317504, PubMed:29176719, PubMed:29379197). Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:22334664, PubMed:23317504, PubMed:23589332). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (By similarity). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:23086925). According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B (PubMed:19103749). Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (PubMed:23317504).

Sequence similarities

Belongs to the BET family.

Post-translational modifications

Phosphorylation by CK2 disrupt the intramolecular binding between the bromo domain 2 and the NPS region and promotes binding between the NPS and the BID regions, leading to activate the protein and promote binding to acetylated histones. In absence of phosphorylation, BRD4 does not localize to p53/TP53 target gene promoters, phosphorylation promoting recruitment to p53/TP53 target promoters.

Subcellular localisation
Nucleus

Storage

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C

Notes

This product is manufactured by BioVision, an Abcam company and was previously called 7643 Bromodomain-containing Protein 4 (BrD4, domain 49-170aa), human recombinant. 7643-20 is the same size as the 20 μg size of ab176936.

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.
Activity summary

The Brd4 protein also known as Bromodomain containing protein 4 plays an important role as a transcriptional regulator. It recognizes acetylated lysine residues on histone tails through its bromodomains. This binding impacts chromatin structure and transcriptional activation. The Brd4 protein has a molecular weight of around 150 kDa and is often used as a marker in studies using Brd4 western blot techniques. It mainly expresses in the nucleus of most cell types and is an important focus for developing Brd4 anticuerpos useful for detecting protein size discrepancies in research.

Biological function summary

Brd4 plays a significant role in regulating gene expression during cell cycle progression. It interacts with the Mediator complex enabling communication between transcriptional activators and RNA polymerase II. This protein is integral for maintaining chromatin in an active state ensuring accessibility for transcription machinery. Moreover Brd4 size and functionality relate to the elongation of transcription by RNA polymerase II ensuring the seamless expression of genes essential for cellular functions.

Pathways

Brd4 integrates into transcriptional and epigenetic regulation pathways. It acts in the positive regulation of the MYC pathway directly linking Brd4 with proto-oncogene c-Myc. Also Brd4 engages in the JAK/STAT signaling pathway where its activity affects cell growth and immune response. These interactions establish Brd4 as a central regulator within these pathways facilitating communication and coordination among molecular players.

Associated diseases and disorders

Brd4 link heavily to cancer and inflammatory diseases. Aberrant Brd4 activity often associates with various cancers including leukemia where its regulation impacts oncogenic drivers. Clinically targeting Brd4 presents a therapeutic avenue as its inhibition affects cyclin-dependent kinase 9 (CDK9) an important regulator of the cell cycle. Similarly Brd4 alterations implicate in inflammatory disorders impacting nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kB) signaling revealing pathways for intervening in pathogenic processes.

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1 product image

  • SDS-PAGE - Recombinant Human Brd4 protein (ab176936), expandable thumbnail

    SDS-PAGE - Recombinant Human Brd4 protein (ab176936)

    15% SDS-PAGE analysis of ab176936.

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Product protocols

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