Analytical Data
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Gene name
BRD1
- Application
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Alternative Names
BRD1；BRL；BRPF2；Bromodomain-containing Protein 1
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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
O95696
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Expression Region
556-688aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSEQVAMEL RLTPLTVLLR SVLDQLQDKD PARIFAQPVS LKEVPDYLDH IKHPMDFATM RKRLEAQGYK NLHEFEEDFD LIIDNCMKYN ARDTVFYRAA VRLRDQGGVV LRQARREVDS IGLEEASGMH LPERPA
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Molecular Weight
18 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
Related Products
Protein Description
BRD1 (Bromodomain-containing protein 1) is a member of the bromodomain and extraterminal (BET) family of proteins, which play a crucial role in the regulation of gene expression, chromatin remodeling, and cell cycle progression. Research into BRD1 has gained momentum due to its involvement in several biological processes, including transcriptional regulation and potential links to various diseases, such as cancer and neurodegenerative disorders. The protein's unique structure, characterized by its bromodomain, enables it to interact with acetylated lysines on histones, thereby facilitating the recruitment of transcriptional machinery to specific genomic locations. Given its role in modulating gene expression, BRD1 is considered a potential therapeutic target in diseases where these pathways are dysregulated. Recent studies have focused on the characterization of BRD1's interactions and its functional implications in cellular contexts, aiming to elucidate its specific contributions to disease mechanisms. Additionally, the development of small molecules that can selectively inhibit BRD1 has emerged as a promising avenue for therapeutic intervention. Understanding the precise mechanisms of BRD1's action and its effects on the epigenetic landscape could pave the way for innovative treatments that leverage its role in transcriptional regulation. As such, BRD1 remains a significant focus in the field of epigenetics and molecular biology, with ongoing research aimed at unraveling its complex functions and therapeutic potential.
