Analytical Data
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Gene name
TWF2
- Application
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Alternative Names
TWF2；PTK9L；Twinfilin-2
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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
Q6IBS0
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Expression Region
1-349aa
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AA Sequence
AHQTGIHATEELKEFFAKARAGSVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQQPCYLLYRLDSQNAQGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCAAPAPLTSAERELQQIRINEVKTEISVESKHQTLQGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTEPTDVAQLPSRVPRDAARYHFFLYKHTHEGDPLESVVFIYSMPGYKCSIKERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDEVHPKQHAFKQAFAKPKGPGGKRGHKRLIRGPGENGDDS
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Molecular Weight
66.4 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
The TWF2 (Twinfilin-2) recombinant protein has garnered significant attention in the field of molecular biology due to its critical role in actin filament dynamics and cellular processes such as endocytosis, cell migration, and morphology. TWF2 is a member of the twinfilin family, characterized by the presence of two twinfilin-type actin-binding domains, which facilitate the regulation of actin monomers and filament turnover. Research has indicated that TWF2 is involved in various physiological processes, including neuronal differentiation and intracellular transport, implicating it in vital functions beyond mere structural support. Dysregulation of TWF2 has been associated with a range of pathological conditions, including cancer and neurodegenerative disorders, making it a potential biomarker and therapeutic target. The production of TWF2 as a recombinant protein enables researchers to investigate its structural properties and functional roles in greater detail, particularly its interactions with other cytoskeletal proteins and signaling pathways. Moreover, studying TWF2 in the context of recombinant systems allows for the exploration of its functional consequences in vitro and in vivo, enhancing our understanding of its contribution to cellular behavior and potential roles in disease mechanisms. As such, TWF2 continues to be a focal point in studies aimed at elucidating the complexities of actin dynamics and their implications in health and disease.
