Analytical Data
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Gene name
SH3GL1
- Application
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Alternative Names
SH3GL1；CNSA1；SH3D2B；Endophilin-A2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MSVAGLKKQFYKASQLVSEKVGGAEGTKLDDDFKEMEKKVDVTSKAVTEVLARTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGECMIRHGKELGGESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCEKDLKEIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILDELAEKLKRRMREASSRPKREYKPKPREPFDLGEPEQSNGGFPCTTAPKIAASSSFRSSDKPIRTPSRSMPPLDQPSCKALYDFEPENDGELGFHEGDVITLTNQIDENWYEGMLDGQSGFFPLSYVEVLVPLPQ
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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, or SH3-domain-containing protein 3 GTPase-activating protein, has garnered significant attention in cellular biology due to its pivotal role in membrane trafficking and cytoskeletal dynamics. This protein is primarily involved in clathrin-mediated endocytosis, where it facilitates the budding and scission of vesicles from the plasma membrane, thereby influencing nutrient uptake and signal transduction. Research has increasingly linked SH3GL1 to various pathological conditions, including cancer and neurodegenerative diseases, suggesting that dysregulation of its activity may disrupt normal cellular functions. Furthermore, studies have highlighted the importance of its SH3 and BAR (Bin/Amphiphysin/Rvs) domains, which are essential for its interactions with other proteins and membrane curvature generation. Understanding the structure and function of SH3GL1 through recombinant protein studies could reveal new insights into its mechanistic roles and regulatory pathways. Such insights may ultimately lead to the development of targeted therapeutic strategies aimed at correcting the aberrant cellular processes associated with SH3GL1 dysfunction, providing a promising avenue for future biomedical research.
