Analytical Data
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Gene name
SH3BGR
- Application
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Alternative Names
SH3BGR; SH3 domain-binding glutamic acid-rich protein; SH3BGR protein; 21-glutamic acid-rich protein; 21-GARP
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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
P55822
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Expression Region
1-239 aa
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AA Sequence
MPLLLLGETE PLKLERDCRS PVDPWAAASP DLALACLCHC QDLSSGAFPD RGVLGGVLFP TVEMVIKVFV ATSSGSIAIR KKQQEVVGFL EANKIDFKEL DIAGDEDNRR WMRENVPGEK KPQNGIPLPP QIFNEEQYCG DFDSFFSAKE ENIIYSFLGL APPPDSKGSE KAEEGGETEA QKEGSEDVGN LPEAQEKNEE EGETATEETE EIAMEGAEGE AEEEEETAEG EEPGEDEDS
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Molecular Weight
26.0 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
Related Products
Protein Description
SH3BGR (SH3 domain-binding glutamic acid-rich protein) is a protein that has garnered significant interest in recent years due to its potential roles in cellular signaling and various biological processes. Research indicates that SH3BGR interacts with numerous SH3 domain-containing proteins, which are implicated in critical cellular functions such as cytoskeletal dynamics, signal transduction, and the regulation of gene expression. Understanding the function and mechanisms of SH3BGR is vital, as alterations in its expression or activity have been linked to various pathologies, including cancer and neurodegenerative diseases. The study of SH3BGR is further driven by its involvement in cellular responses to stress and inflammation, highlighting its potential as a therapeutic target. Investigations utilizing recombinant SH3BGR protein have provided insights into its structural properties and functional interactions, facilitating the elucidation of its biological roles. As research progresses, the comprehensive understanding of SH3BGR’s involvement in health and disease is anticipated to have significant implications for developing novel therapeutic strategies.
