Analytical Data
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Gene name
SH3GL1
- Application
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Alternative Names
EEN fusion partner of MLL (Endophilin-2) (Extra eleven-nineteen leukemia fusion gene protein) (EEN) (SH3 domain protein 2B) (SH3 domain-containing GRB2-like protein 1 CNSA1) (SH3D2B)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99961
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Expression Region
1-368aa
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Molecular Weight
45.0 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
SH3GL1, a member of the SH3 domain-containing family of proteins, plays a pivotal role in endocytosis and trafficking of membrane proteins, influencing signal transduction pathways. This protein is characterized by its ability to bend membranes, a function critical for the formation of clathrin-coated vesicles. The study of SH3GL1 has gained prominence due to its associations with various cellular processes, including actin dynamics, membrane recycling, and cell signaling. Dysregulation of SH3GL1 has been implicated in several diseases, such as cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. Furthermore, as a reconstituted protein, SH3GL1 allows researchers to dissect its functional mechanisms in vitro, providing insights into its biological significance and regulatory roles. Investigating SH3GL1's structure and interactions with other cellular components can unveil new aspects of cellular dynamics and contribute to our understanding of disease mechanisms. This research is crucial for developing novel strategies in therapeutics, as it opens avenues for targeted interventions that modulate SH3GL1's activity and restore normal cellular functions. Understanding the biophysical properties and regulatory networks of SH3GL1 through recombinant protein studies can also facilitate the identification of potential biomarkers for diseases associated with its dysfunction. Overall, the exploration of SH3GL1's biological roles and its implications in health and disease continues to be a vibrant field of investigation in molecular biology and biomedicine.
