Analytical Data
-
Gene name
SRFBP1
- Application
-
Alternative Names
STRAP; p49; BUD22; Rlb1; SRF-dependent transcription regulation-associated protein
-
Species
Mouse
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9CZ91
-
Expression Region
Met1~Glu278
-
Molecular Weight
39kDa
-
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
SRFBP1 (Serine/Arginine-Rich Splicing Factor 1) is a crucial splicing factor involved in the regulation of pre-mRNA splicing, influencing gene expression and protein diversity. Recent studies have highlighted its significant role in various biological processes, including cell differentiation, proliferation, and apoptosis. Dysregulation of SRFBP1 has been associated with several diseases, particularly cancers, where it may contribute to aberrant splicing patterns and oncogenic pathways. Consequently, understanding the structure and function of SRFBP1 through recombinant protein studies becomes essential for elucidating its mechanisms in splice site recognition and interaction with other splicing components. The characterization of SRFBP1 as a recombinant protein allows for the analysis of its biochemical properties, interaction with RNA, and potential regulatory roles in cellular contexts. Such research can provide insights into therapeutic targets, as restoring normal splicing functions might mitigate the effects of its dysregulation in disease states. This growing interest in SRFBP1 highlights its potential as a key player in the development of novel strategies for disease intervention, emphasizing the necessity for further investigation into its functional dynamics and therapeutic implications.
