Analytical Data
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Gene name
SH3GLB2
- Application
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Alternative Names
SH3 domain-containing GRB2-like protein B2
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NR46
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Expression Region
1-395aa
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Molecular Weight
60 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
SH3GLB2, or SH3 domain-containing GRB2-like protein 2, is a member of the SH3GL family, which plays a critical role in cellular processes such as endocytosis, signal transduction, and cytoskeletal organization. Research into SH3GLB2 has gained attention due to its involvement in various cellular functions and its potential implications in cellular dynamics, particularly in the context of cancer and neurodegenerative diseases. The protein is known to contain a Src homology 3 (SH3) domain that facilitates interactions with other proteins, suggesting its function in mediating signal transduction pathways. Understanding the structure and function of SH3GLB2 through recombinant protein studies can illuminate its role in disease mechanisms and physiological processes. Moreover, the development of recombinant SH3GLB2 protein allows for in-depth functional assays and structural analyses, which are crucial for discovering its biological activities and identifying potential therapeutic targets. Given the rising interest in protein-protein interactions and their regulatory mechanisms in cellular signaling, the investigation of SH3GLB2 provides a promising avenue for understanding complex biological networks and developing novel treatment strategies.
