Analytical Data
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Gene name
RFT1
- Application
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Alternative Names
RFT1; Protein RFT1 homolog
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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
Q96AA3
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Expression Region
1-541 aa
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AA Sequence
MGSQEVLGHAARLASSGLLLQVLFRLITFVLNAFILRFLSKEIVGVVNVRLTLLYSTTLFLAREAFRRACLSGGTQRDWSQTLNLLWLTVPLGVFWSLFLGWIWLQLLEVPDPNVVPHYATGVVLFGLSAVVELLGEPFWVLAQAHMFVKLKVIAESLSVILKSVLTAFLVLWLPHWGLYIFSLAQLFYTTVLVLCYVIYFTKLLGSPESTKLQTLPVSRITDLLPNITRNGAFINWKEAKLTWSFFKQSFLKQILTEGERYVMTFLNVLNFGDQGVYDIVNNLGSLVARLIFQPIEESFYIFFAKVLERGKDATLQKQEDVAVAAAVLESLLKLALLAGLTITVFGFAYSQLALDIYGGTMLSSGSGPVLLRSYCLYVLLLAINGVTECFTFAAMSKEEVDRYNFVMLALSSSFLVLSYLLTRWCGSVGFILANCFNMGIRITQSLCFIHRYYRRSPHRPLAGLHLSPVLLGTFALSGGVTAVSEVFLCCEQGWPARLAHIAVGAFCLGATLGTAFLTETKLIHFLRTQLGVPRRTDKMT
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Molecular Weight
86.7 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
RFT1 (Reduced Fundic Tension 1) is a protein implicated in various biological processes, particularly in the context of protein glycosylation and endoplasmic reticulum (ER) function. Research has shown that RFT1 plays a critical role in the transport of nucleotide-sugar glycosylation precursors into the ER, which is essential for proper glycoprotein synthesis. Mutations or dysfunctions in RFT1 can lead to various diseases, including congenital disorders of glycosylation. Investigating RFT1 recombinantly allows scientists to better understand its structure-function relationship, the mechanisms by which it facilitates sugar transport, and its broader implications in cellular biology. Moreover, RFT1's role in the ER stress response highlights its potential involvement in metabolic disorders, making it a focal point for therapeutic targeting. Recent studies have employed techniques such as CRISPR gene editing and proteomics to dissect the enzymatic pathways influenced by RFT1, further uncovering its significance in maintaining cellular homeostasis. Through these endeavors, RFT1 emerges not only as a vital component of the glycosylation machinery but also as a promising target for novel treatments aimed at addressing glycosylation-related diseases.
