Recombinant Proteins

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BRD1 Human

Bromodomain Containing 1 Human Recombinant

This product consists of a recombinant human BRD1 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain with a molecular weight of 17.8 kDa, comprising 156 amino acids (residues 556-688). The protein has a 23 amino acid His-tag attached to its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27232
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

BRD2 Human

Bromodomain Containing 2 Human Recombinant

Recombinant human BRD2 protein was expressed in E. coli as a single, non-glycosylated polypeptide chain consisting of 478 amino acids (residues 1-455) with a molecular weight of 52.8 kDa. The protein includes a 23 amino acid His-tag at the N-terminus. Purification was achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27298
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

BRD3 Human

Bromodomain Containing 3 Human Recombinant

Recombinant human BRD3, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 439 amino acids (with amino acids 1-416 being of particular interest). It possesses a molecular weight of 48.1 kDa. The protein is equipped with a 23 amino acid His-tag at its N-terminus to facilitate purification through specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27353
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.
Definition and Classification

Bromodomains are approximately 110 amino acid protein domains that recognize acetylated lysine residues, such as those on the N-terminal tails of histones . These domains are structurally conserved and are found in a variety of proteins involved in chromatin remodeling, transcriptional regulation, and other cellular processes . Bromodomain-containing proteins (BCPs) can be classified into several families, including the Bromodomain and Extra-Terminal (BET) family, which includes BRD2, BRD3, BRD4, and BRDT .

Biological Properties

Key Biological Properties: Bromodomains act as “readers” of acetylated lysine residues, translating these epigenetic marks into functional outcomes . They are involved in the regulation of gene expression, chromatin remodeling, and DNA damage repair .

Expression Patterns and Tissue Distribution: Bromodomain-containing proteins are ubiquitously expressed in eukaryotic cells, with specific expression patterns depending on the protein and tissue type . For example, BRD4 is widely expressed in various tissues, while BRDT is specifically expressed in the testis .

Biological Functions

Primary Biological Functions: Bromodomain-containing proteins play crucial roles in regulating gene expression by binding to acetylated histones and recruiting other transcriptional machinery . They are involved in processes such as cell cycle control, cell proliferation, and differentiation .

Role in Immune Responses and Pathogen Recognition: Some bromodomain-containing proteins, such as BRD4, have been implicated in the regulation of immune responses and inflammation . They can influence the expression of genes involved in pathogen recognition and immune signaling pathways .

Modes of Action

Mechanisms with Other Molecules and Cells: Bromodomains interact with acetylated lysine residues on histones and non-histone proteins, facilitating the recruitment of various protein complexes involved in transcriptional regulation . These interactions are crucial for the formation of chromatin remodeling complexes and the regulation of gene expression .

Binding Partners and Downstream Signaling Cascades: Bromodomain-containing proteins often function as scaffolding proteins, bringing together multiple protein partners to form functional complexes . These complexes can initiate downstream signaling cascades that regulate various cellular processes, including transcription, DNA repair, and cell cycle progression .

Regulatory Mechanisms

Transcriptional Regulation: Bromodomain-containing proteins regulate gene expression by binding to acetylated histones and recruiting transcriptional machinery . They can also interact with other transcription factors and co-activators to modulate gene expression .

Post-Translational Modifications: Bromodomain-containing proteins themselves can be regulated by post-translational modifications, such as phosphorylation, ubiquitination, and acetylation . These modifications can influence their stability, localization, and interactions with other proteins .

Applications

Biomedical Research: Bromodomain-containing proteins are important targets in biomedical research due to their roles in gene regulation and disease . They are studied for their involvement in cancer, inflammation, cardiovascular diseases, and viral infections .

Diagnostic Tools and Therapeutic Strategies: Bromodomain inhibitors have been developed as potential therapeutic agents for various diseases . These inhibitors can block the interaction between bromodomains and acetylated lysines, thereby modulating gene expression and cellular functions . Some bromodomain inhibitors are currently in clinical trials for cancer and other diseases .

Role in the Life Cycle

Development to Aging and Disease: Bromodomain-containing proteins play essential roles throughout the life cycle, from development to aging . They are involved in the regulation of gene expression during embryonic development, cell differentiation, and tissue homeostasis . Dysregulation of bromodomain-containing proteins has been linked to various diseases, including cancer, neurodevelopmental disorders, and inflammatory conditions .

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