Analytical Data
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Gene name
SHP-2
- Application
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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
Q06124-2
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Expression Region
T2-R593
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Molecular Weight
65-66 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
SHP-2 (Src Homology 2-containing Protein Tyrosine Phosphatase 2) is a crucial cytoplasmic protein tyrosine phosphatase that plays a significant role in various cellular processes, including cell growth, differentiation, and survival. It is involved in the negative regulation of signaling pathways triggered by receptor tyrosine kinases, thereby influencing numerous biological responses. Dysregulation of SHP-2 has been implicated in several diseases, particularly cancer, where it contributes to oncogenic signaling and tumor progression. Recent studies have highlighted the importance of SHP-2 as a therapeutic target, especially in cancers with mutations that activate growth factor signaling pathways. As a result, the development of SHP-2 recombinant proteins has garnered significant attention in the scientific community. Researchers are focused on understanding its molecular structure, functional mechanisms, and interactions with other proteins, aiming to elucidate how SHP-2 regulates key signaling pathways. Using recombinant DNA technology, scientists can produce SHP-2 protein for functional assays, allowing for detailed studies of its enzymatic activity and role in tumor biology. Insights gained from SHP-2 research could pave the way for novel cancer therapies and improve our understanding of the fundamental processes governing cellular signaling and disease etiology.
