Analytical Data
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Gene name
FKTN
- Application
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Alternative Names
FKTN；FCMD；Ribitol-5-phosphate transferase FKTN
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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
O75072
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Expression Region
1-461aa
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AA Sequence
MSRINKNVVLALLTLTSSAFLLFQLYYYKHYLSTKNGAGLSKSKGSRIGF DSTQWRAVKKFIMLTSNQNVPVFLIDPLILELINKNFEQVKNTSHGSTSQ CKFFCVPRDFTAFALQYHLWKNEEGWFRIAENMGFQCLKIESKDPRLDGI DSLSGTEIPLHYICKLATHAIHLVVFHERSGNYLWHGHLRLKEHIDRKFV PFRKLQFGRYPGAFDRPELQQVTVDGLEVLIPKDPMHFVEEVPHSRFIEC RYKEARAFFQQYLDDNTVEAVAFRKSAKELLQLAAKTLNKLGVPFWLSSG TCLGWYRQCNIIPYSKDVDLGIFIQDYKSDIILAFQDAGLPLKHKFGKVE DSLELSFQGKDDVKLDVFFFYEETDHMWNGGTQAKTGKKFKYLFPKFTLC WTEFVDMKVHVPCETLEYIEANYGKTWKIPVKTWDWKRSPPNVQPNGIWP ISEWDEVIQLY
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Molecular Weight
57 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
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Protein Description
FKTN (Fukutin) is a critical protein involved in the post-translational modifications of glycoproteins, especially in the context of the muscular dystrophy known as Fukuyama congenital muscular dystrophy (FCMD). This rare genetic disorder is caused by mutations in the FKTN gene, leading to a deficiency in Fukutin and resulting in severe muscle weakness and developmental delays in affected individuals. Research on FKTN focuses on its essential role in the glycosylation process, specifically the formation of the glycosylated dystroglycan complex, which is crucial for maintaining the structural integrity of muscle fibers. Mutations in FKTN disrupt this process, contributing to the pathophysiology of FCMD and other related disorders. Understanding the functional dynamics of FKTN and its interactions within the glycosylation pathway presents significant potential for therapeutic strategies, including gene therapy and molecular interventions aimed at restoring normal protein function. Consequently, ongoing studies are dedicated to elucidating the molecular mechanisms governing FKTN's activity, the impact of specific mutations, and the broader implications for neuromuscular diseases, emphasizing its significance in both fundamental science and potential clinical applications.
