Analytical Data
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Gene name
FG
- Application
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Alternative Names
FG；KICSTOR complex Protein ITFG2
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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
Q969R8
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Expression Region
1-447aa
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AA Sequence
MRSVSYVQRVALEFSGSLFPHAICLGDVDNDTLNELVVGDTSGKVSVYKNDDSRPWLTCSCQGMLTCVGVGDVCNKGKNLLVAVSAEGWFHLFDLTPAKVLDASGHHETLIGEEQRPVFKQHIPANTKVMLISDIDGDGCRELVVGYTDRVVRAFRWEELGEGPEHLTGQLVSLKKWMLEGQVDSLSVTLGPLGLPELMVSQPGCAYAILLCTWKKDTGSPPASEGPTDGSRETPAARDVVLHQTSGRIHNKNVSTHLIGNIKQGHGTESSGSGLFALCTLDGTLKLMEEMEEADKLLWSVQVDHQLFALEKLDVTGNGHEEVVACAWDGQTYIIDHNRTVVRFQVDENIRAFCAGLYACKEGRNSPCLVYVTFNQKIYVYWEVQLERMESTNLVKLLETKPEYHSLLQELGVDPDDLPVTRALLHQTLYHPDQPPQCAPSSLQDPT
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Molecular Weight
49.3 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
FG (FUS-Glycine) recombinant proteins are at the forefront of research due to their implications in understanding protein aggregation and neurodegenerative diseases. These proteins are characterized by the presence of low-complexity domains, particularly those rich in phenylalanine and glycine, which play significant roles in the formation of nuclear bodies and stress granules within cells. The study of FG proteins is crucial for unraveling the mechanisms of phase separation, a biological phenomenon where proteins and RNA form membraneless organelles, influencing various cellular processes. Dysregulation of FG proteins has been linked to conditions such as amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), underscoring their importance in neurobiology. Furthermore, as recombinant proteins, FG variants can be engineered to study their functions, interactions, and the effects of post-translational modifications, offering insights into therapeutic targets. Advances in molecular biology techniques have thus enabled researchers to dissect the role of FG proteins in cellular homeostasis and disease pathology, making them a pivotal focus in the quest for novel treatments and a deeper understanding of cellular dynamics. As research progresses, the potential for FG proteins to serve as biomarkers or therapeutic agents remains a promising avenue for future investigations.
