Analytical Data
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Gene name
BRD3
- Application
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Alternative Names
BRD3;KIAA0043;RING3L;Bromodomain-containing Protein 3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15059
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Expression Region
1-416aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSTATTV APAGIPATPG PVNPPPPEVS NPSKPGRKTN QLQYMQNVVV KTLWKHQFAW PFYQPVDAIK LNLPDYHKII KNPMDMGTIK KRLENNYYWS ASECMQDFNT MFTNCYIYNK PTDDIVLMAQ ALEKIFLQKV AQMPQEEVEL LPPAPKGKGR KPAAGAQSAG TQQVAAVSSV SPATPFQSVP PTVSQTPVIA ATPVPTITAN VTSVPVPPAA APPPPATPIV PVVPPTPPVV KKKGVKRKAD TTTPTTSAIT ASRSESPPPL SDPKQAKVVA RRESGGRPIK PPKKDLEDGE VPQHAGKKGK LSEHLRYCDS ILREMLSKKH AAYAWPFYKP VDAEALELHD YHDIIKHPMD LSTVKRKMDG REYPDAQGFA ADVRLMFSNC YKYNPPDHEV VAMARKLQDV FEMRFAKMP
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Molecular Weight
48 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
BRD3, or Bromodomain-containing protein 3, is a member of the BET (Bromodomain and Extra-Terminal) protein family, which plays a pivotal role in epigenetic regulation by recognizing acetylated lysine residues on histones and non-histone proteins. Research on BRD3 has gained momentum due to its significant involvement in various cellular processes, including transcriptional regulation, cell cycle control, and differentiation. Notably, BRD3 has been implicated in several malignancies, making it a potential therapeutic target in cancer treatment. Its aberrant expression is associated with poor prognosis and has been linked to oncogenic signaling pathways. Furthermore, BRD3 acts as a co-activator for numerous transcription factors, thereby influencing gene expression profiles essential for tumor progression. The development of small-molecule inhibitors targeting BRD3 and other members of the BET family is currently under investigation, showing promising results in preclinical studies. These inhibitors aim to disrupt the interaction between BRD3 and acetylated proteins, thereby hindering cancer cell proliferation and survival. Understanding the structural and functional properties of BRD3 is vital to uncover its precise roles in pathology and develop effective therapeutic strategies. Overall, the ongoing research on BRD3 not only sheds light on its fundamental biological functions but also holds therapeutic promise in combating various diseases, particularly cancer.











