Analytical Data
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Gene name
SHB
- Application
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Alternative Names
SHB；SH2 domain-containing adapter Protein B
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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
Q15464-1
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Expression Region
395-509aa
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AA Sequence
LGERVDPAVPLEKQIWYHGAISRGDAENLLRLCKECSYLVRNSQTSKHDYSLSLRSNQGFMHMKLAKTKEKYVLGQNSPPFDSVPEVIHYYTTRKLPIKGAEHLSLLYPVAVRTL
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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
The study of SHB (SH2 domain-containing protein B) recombinant proteins has gained significant traction in recent years due to their crucial role in cell signaling and immune response regulation. SHB is a multifunctional adapter protein that interacts with various signaling molecules, playing a pivotal role in the modulation of cellular activities such as proliferation, differentiation, and apoptosis. Understanding the structure and function of SHB is essential for elucidating the molecular mechanisms underlying various diseases, including cancer and autoimmune disorders. Researchers have increasingly focused on producing recombinant SHB proteins to enable detailed biochemical analyses, structural studies, and the development of potential therapeutic applications. The ability to express and purify SHB in large quantities allows for the exploration of its interactions with other proteins and its role in various signaling pathways. Additionally, the generation of SHB knockdown or overexpression models in cell systems has provided insights into its functional significance in both normal and pathological contexts. As a result, SHB recombinant protein research has the potential to lead to novel biomarkers and innovative treatment strategies, further emphasizing the importance of this protein in cellular biology and medicine.
