Analytical Data
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Gene name
KRAS
- Application
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Alternative Names
K-Ras 2Ki-Rasc-K-rasc-Ki-ras
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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
P01116
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Expression Region
2-168aa
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Molecular Weight
23.1 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
Related Products
Protein Description
KRAS is a prominent member of the RAS gene family, which encodes proteins that act as molecular switches in various cellular processes, including growth, differentiation, and survival. Mutations in the KRAS gene are commonly associated with several types of cancers, particularly pancreatic, colorectal, and lung cancers, making it a critical target for cancer research. The most frequent mutations occur at codons 12, 13, and 61, leading to constitutive activation of KRAS and driving tumorigenesis through aberrant signaling pathways such as the MAPK and PI3K pathways. Due to its central role in oncogenic signaling, KRAS has been a challenging target for drug development, historically considered "undruggable." However, advances in biotechnology and pharmacology have led to the emergence of novel therapeutic strategies aimed at inhibiting mutant KRAS or its downstream effectors. The study of recombinant KRAS proteins, which involves the production of these proteins in vitro using expression systems, has become a pivotal approach to understand the molecular mechanisms of KRAS activation and its interactions with potential inhibitors. Such research not only aids in elucidating the functional impact of specific mutations but also supports the identification and validation of promising drug candidates. Ongoing investigations into KRAS-targeted therapies continue to hold significant promise for improving treatment outcomes in KRAS-mutant cancers, emphasizing the importance of continued research in this area.











