Analytical Data
-
Gene name
BAZ1A
- Application
-
Alternative Names
cbp146; CHRAC subunit ACF1; DKFZp586E0518; FLJ14383; Gtl5; hACF1
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9NRL2
-
Expression Region
1457-1556aa
-
AA Sequence
LVSKIQVPDYYDIIKKPIALNIIREKVNKCEYKLASEFIDDIELMFSNCFEYNPRNTSEAKAGTRLQAFFHIQAQKLGLHVTPSNVDQVSTPPAAKKSRI
-
Molecular Weight
36.74 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
BAZ1A is a member of the bromodomain and extraterminal (BET) family of proteins, which are known to play critical roles in chromatin dynamics and transcriptional regulation. It functions as a histone acetylation reader, influencing various cellular processes, including gene expression, DNA repair, and cell cycle progression. The study of BAZ1A has gained momentum due to its involvement in several diseases, particularly cancer, where alterations in chromatin regulation can contribute to tumorigenesis. Its unique structural features, including the presence of multiple bromodomains, enable BAZ1A to interact with specific acetylated lysines on histones, thereby facilitating the recruitment of transcriptional machinery. Recent research highlights the potential of targeting BAZ1A in therapeutic strategies for cancers characterized by aberrant chromatin modifications. Understanding the intricate molecular mechanisms governing BAZ1A's functions could pave the way for novel interventions, making it a significant focus within the fields of epigenetics and oncology. As the field progresses, the exploration of BAZ1A's role in various biological contexts continues to reveal its importance in both normal physiology and disease states.
