Analytical Data
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Gene name
Raf-1
- Application
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Alternative Names
RAF1; CRAF; V-raf-1 Murine Leukemia Viral Oncogene Homolog 1; Proto-oncogene c-RAF
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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
P04049
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Expression Region
Trp342~Ser619
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Molecular Weight
35kDa
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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
Raf-1, also known as c-Raf, is a crucial serine/threonine kinase that plays a pivotal role in the mitogen-activated protein kinase (MAPK) signaling pathway, which is essential for various cellular processes such as proliferation, differentiation, and survival. The dysregulation of Raf-1 activity has been implicated in numerous cancers, making it a promising target for therapeutic intervention. Research into Raf-1 recombinant proteins aims to elucidate the molecular mechanisms underlying its activation and function in signaling cascades. By generating and studying Raf-1 recombinant proteins, scientists can perform detailed biochemical assays, structural analyses, and functional studies. This research not only enhances our understanding of Raf-1's role in normal physiology but also aids in identifying potential inhibitors that could serve as effective anti-cancer agents. The findings from these studies can contribute to the development of targeted therapies, which may revolutionize treatment strategies for patients with Raf-1-related malignancies. Overall, the exploration of Raf-1 recombinant proteins is a vital component of modern cancer research, with significant implications for improving drug design and therapeutic efficacy.
