Analytical Data
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Gene name
RET
- Application
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Alternative Names
Restrictocin
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Species
Aspergillus restrictus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P67876
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Expression Region
28-176aa
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Molecular Weight
23.9 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
RET (REarranged during Transfection) is a gene that encodes a receptor tyrosine kinase involved in the development of the nervous system and various endocrine organs. Its importance in both normal physiology and pathology has drawn significant research attention, particularly in the context of cancer. Aberrations in RET signaling, such as mutations and rearrangements, have been associated with several hereditary cancers, including medullary thyroid carcinoma and multiple endocrine neoplasia type 2 (MEN2). In recent years, the development of RET-targeted therapies, such as selective RET inhibitors, has shown promise in treating RET-driven malignancies, leading to a surge of interest in understanding its molecular mechanisms and interactions. The generation of recombinant RET proteins has enabled detailed studies of its structure, function, and the pathways it influences, furthering our knowledge of RET-related diseases. This focus not only paves the way for novel therapeutic strategies but also enhances our understanding of RET signaling in cellular processes and development. With the growing emphasis on precision medicine, ongoing research aims to refine RET-targeting approaches, optimize treatment regimens, and explore the potential for combining RET inhibitors with other therapeutic modalities to improve patient outcomes.
