Analytical Data
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Gene name
FKRP
- Application
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Alternative Names
Fkrp; FKRP_HUMAN; FLJ12576; Fukutin related protein; Fukutin-related protein; LGMD2I; MDC1C; MGC2991
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H9S5
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Expression Region
396-494aa
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AA Sequence
KAVEGDFFRVQYSESNHLHVDLWPFYPRNGVMTKDTWLDHRQDVEFPEHFLQPLVPLPFAGFVAQAPNNYRRFLELKFGPGVIENPQYPNPALLSLTGS
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Molecular Weight
36.63 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
FKRP (Fukutin-related protein) is a glycosyltransferase implicated in the post-translational modification of dystroglycan, a protein critical for muscle integrity and function. Mutations in the FKRP gene are linked to a spectrum of muscle dystrophies, including limb-girdle muscular dystrophy 2I (LGMD2I) and congenital muscular dystrophy (CMD). The severity of these disorders often correlates with specific FKRP mutations, highlighting the need for a deeper understanding of FKRP's molecular function and its role in protein glycosylation pathways. Research into FKRP recombinant proteins has gained momentum to elucidate the structure-function relationships of the protein and to develop potential therapeutic strategies. By producing and characterizing FKRP in a controlled environment, scientists can study its enzymatic activity, substrate specificity, and interaction with other cellular components. Furthermore, recombinant FKRP offers a platform for high-throughput screening of small molecules that may enhance its function or compensate for the loss of activity due to mutations. Overall, the study of FKRP and its recombinant forms is crucial for advancing our knowledge of muscular dystrophies and developing targeted therapies that could mitigate the effects of FKRP-related disorders.
