Analytical Data
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Gene name
FRK
- Application
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Alternative Names
FRK;PTK5;RAK;Tyrosine-Protein kinase FRK
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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
P42685
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Expression Region
1-505aa
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AA Sequence
MSNICQRLWE YLEPYLPCLS TEADKSTVIE NPGALCSPQS QRHGHYFVAL FDYQARTAED LSFRAGDKLQ VLDTLHEGWW FARHLEKRRD GSSQQLQGYI PSNYVAEDRS LQAEPWFFGA IGRSDAEKQL LYSENKTGSF LIRESESQKG EFSLSVLDGA VVKHYRIKRL DEGGFFLTRR RIFSTLNEFV SHYTKTSDGL CVKLGKPCLK IQVPAPFDLS YKTVDQWEID RNSIQLLKRL GSGQFGEVWE GLWNNTTPVA VKTLKPGSMD PNDFLREAQI MKNLRHPKLI QLYAVCTLED PIYIITELMR HGSLQEYLQN DTGSKIHLTQ QVDMAAQVAS GMAYLESRNY IHRDLAARNV LVGEHNIYKV ADFGLARVFK VDNEDIYESR HEIKLPVKWT APEAIRSNKF SIKSDVWSFG ILLYEIITYG KMPYSGMTGA QVIQMLAQNY RLPQPSNCPQ QFYNIMLECW NAEPKERPTF ETLRWKLEDY FETDSSYSDA NNFIR
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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
FRK (Fyn-related kinase) is a member of the Src family of non-receptor tyrosine kinases, playing a critical role in various cellular processes, including cell proliferation, differentiation, and survival. Research into FRK has gained momentum due to its involvement in cancer biology, where it may influence tumor growth and metastasis. Elevated levels of FRK have been implicated in several cancer types, suggesting that it could be a potential biomarker for cancer progression and a target for therapeutic intervention. Additionally, understanding FRK's signaling pathways could shed light on its role in immune responses and neuronal signaling. The study of recombinant FRK proteins allows for detailed investigations into its biochemical properties, substrate interactions, and regulatory mechanisms. Through structural and functional analyses, researchers aim to elucidate how FRK contributes to various pathophysiological conditions and explore its potential role in drug development. As a result, FRK has emerged as a promising candidate for targeted therapies, and ongoing studies focus on developing inhibitors that could selectively modulate its activity in cancer treatment and other diseases.











