Analytical Data
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Gene name
BRAF
- Application
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Alternative Names
BRAF;BRAF1;RAFB1;Serine/threonine-Protein kinase B-raf
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P15056
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Expression Region
381-766aa
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AA Sequence
DLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSS SSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDV AVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQ WCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSN NIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDK NPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSK VRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASE PSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH
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Molecular Weight
69 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
BRAF (B-Raf proto-oncogene, serine/threonine kinase) is a critical component of the RAS-RAF-MEK-ERK signaling pathway, which regulates cell proliferation, differentiation, and survival. Mutations in the BRAF gene, particularly the V600E mutation, are frequently associated with various cancers, including melanoma, thyroid, and colorectal cancers, leading to aberrant activation of this pathway. This has prompted extensive research into BRAF as a therapeutic target; selective BRAF inhibitors, such as vemurafenib and dabrafenib, have been developed and are used in clinical settings for treating BRAF-mutant tumors. However, resistance to these therapies often develops, necessitating further investigation into BRAF’s structural characteristics and interactions with other proteins. Recombinant BRAF proteins, produced through genetic engineering techniques, facilitate the study of its function in cellular signaling as well as the exploration of novel inhibitors. Additionally, these recombinant proteins enable researchers to examine the effects of specific mutations on BRAF activity and drug resistance mechanisms, thereby enhancing our understanding of tumor biology and paving the way for the development of more effective treatments. Understanding BRAF’s role in cancer also extends to potential combination therapies that target multiple points in the signaling pathway, aiming to circumvent resistance and improve patient outcomes. This comprehensive approach underscores the importance of BRAF research in the field of oncology and personalized medicine.











