Analytical Data
-
Gene name
SH3BGRL
- Application
-
Alternative Names
SH3BGRL;Adapter SH3BGRL
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O75368
-
Expression Region
1-114aa
-
AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMVIRVY IASSSGSTAI KKKQQDVLGF LEANKIGFEE KDIAANEENR KWMRENVPEN SRPATGYPLP PQIFNESQYR GDYDAFFEAR ENNAVYAFLG LTAPPGSKEA EVQAKQQA
-
Molecular Weight
15 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
SH3BGRL (SH3 Domain Binding Glutamic Acid-Rich Locus) is a protein that plays a critical role in various cellular processes, including cell signaling, proliferation, and differentiation. Its interactions with SH3 domains of other proteins suggest it may act as a scaffold or regulatory molecule in signal transduction pathways. Research into SH3BGRL has gained momentum due to its potential implications in human health, particularly in cancer biology and neurodegenerative diseases. Abnormal expression of SH3BGRL has been linked to tumorigenesis, making it a candidate for targeted therapies or biomarkers in specific cancers. Moreover, its involvement in neuronal signaling highlights its relevance in understanding neurological disorders. Investigating the structural and functional properties of SH3BGRL through recombinant protein techniques provides insights into its role in cellular functions and interactions with other signaling molecules. This research not only facilitates a better understanding of the fundamental biology of SH3BGRL but also paves the way for therapeutic advancements in diseases where SH3BGRL's dysregulation has been identified. Thus, the recombinant expression and characterization of SH3BGRL is crucial for unraveling its biological significance and potential exploitation in biomedical applications.
