Analytical Data
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Gene name
BRAF
- Application
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Alternative Names
B-raf 1; BRAF1; RAFB1; V-Raf Murine Sarcoma Viral Oncogene Homolog B1
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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 95% as determined by SDS-PAGE.
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Uniprot
P15056
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Expression Region
Ile457~Leu717
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Molecular Weight
33kDa
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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
BRAF is a serine/threonine kinase that plays a critical role in the RAS-RAF-MEK-ERK signaling pathway, which is essential for cell division, differentiation, and survival. Mutations in the BRAF gene, particularly the V600E mutation, are frequently associated with various human cancers, most notably melanoma, while also being implicated in colorectal and thyroid cancers. The discovery of these mutations has spurred extensive research into BRAF as a therapeutic target. Recombinant BRAF proteins are vital for studying the structure-function relationships of BRAF and for developing targeted therapies. By producing BRAF in a controlled environment, researchers can examine its activity, interactions, and the effects of mutations on its function. This has led to the development of BRAF inhibitors such as vemurafenib, which have significantly improved treatment outcomes in patients with BRAF-mutant melanomas. Additionally, the exploration of BRAF in combination therapies aims to overcome resistance and improve the efficacy of existing treatments. As the understanding of BRAF's role in cancer continues to evolve, the ongoing study of recombinant BRAF proteins remains a crucial element in advancing cancer research and personalized medicine approaches.
