Analytical Data
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Gene name
FIGN
- Application
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Alternative Names
FIGN；Fidgetin
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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
Q5HY92
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Expression Region
479-759aa
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AA Sequence
QGPPVDWNDIAGLDLVKAVIKEEVLWPVLRSDAFSGLTALPRSILLFGPRGTGKTLLGRCIASQLGATFFKIAGSGLVAKWLGEAEKIIHASFLVARCRQPSVIFVSDIDMLLSSQVNEEHSPVSRMRTEFLMQLDTVLTSAEDQIVVICATSKPEEIDESLRRYFMKRLLIPLPDSTARHQIIVQLLSQHNYCLNDKEFALLVQRTEGFSGLDVAHLCQEAVVGPLHAMPATDLSAIMPSQLRPVTYQDFENAFCKIQPSISQKELDMYVEWNKMFGCSQ
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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
FIGN (Fidgetin-like 1) is a member of the AAA+ ATPase family, which plays a crucial role in cellular activities such as cytoskeletal dynamics, organelle transport, and cellular signaling. The study of FIGN and its recombinant protein has garnered increasing interest due to its potential implications in various physiological and pathological processes, including developmental disorders and cancer. FIGN is known for its fidgetin-like activity in regulating the stability and organization of microtubules and actin filaments, key components of the cytoskeleton. Understanding the functional mechanisms of FIGN at the molecular level is vital, as its dysregulation has been associated with several diseases. Research on recombinant FIGN proteins has enabled scientists to investigate their biochemical properties, interactions with other cellular components, and effects on cellular processes. By employing techniques such as protein expression systems, purification methods, and functional assays, researchers aim to unravel the specific roles of FIGN in cellular architecture and dynamics. This has the potential to shed light on its therapeutic value, particularly in conditions where cytoskeletal abnormalities are prevalent. Furthermore, the ability to produce and manipulate recombinant FIGN allows for the exploration of its structure-function relationships, paving the way for innovative strategies in disease treatment and prevention. Overall, the exploration of FIGN recombinant proteins represents a promising avenue for advancing our understanding of cellular mechanisms and developing targeted therapies for diseases linked to cytoskeletal dysfunction.
