Analytical Data
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Gene name
SORBS2
- Application
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Alternative Names
Sorbin and SH3 domain-containing protein 2(Arg-binding protein 2)(ArgBP2)(Arg/Abl-interacting protein 2)(Sorbin)
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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
O94875
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Expression Region
863-1100aa
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Molecular Weight
33.1 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
SORBS2, a member of the SORBS family of adaptor proteins, plays a significant role in various cellular processes, including cytoskeletal dynamics and cell adhesion. It is characterized by its SH3 (Src homology 3) domain, which facilitates interactions with other proteins involved in signaling pathways. Research has indicated that SORBS2 is implicated in the regulation of insulin signaling and may play a role in metabolic disorders, such as obesity and diabetes. Its potential involvement in cancer progression has also garnered attention, as altered expression of SORBS2 has been linked to tumorigenesis. Consequently, studying SORBS2 recombinant proteins offers valuable insights into its structure, function, and interactions, which are essential for understanding its biological significance. By investigating the properties of SORBS2, including its binding affinities and effects on cellular behavior, researchers aim to elucidate its role in disease mechanisms. The development of SORBS2 recombinant proteins facilitates detailed studies of its interactions and functions, potentially paving the way for novel therapeutic strategies targeting related pathways in metabolic and neoplastic diseases. Given the intricate roles of SORBS2 in cellular signaling, ongoing research is crucial for uncovering its complete biological profile and therapeutic potential.
