Analytical Data
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Gene name
FSCN2
- Application
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Alternative Names
FSCN2；Fascin-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
O14926
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Expression Region
1-492aa
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AA Sequence
MPTNGLHQVL KIQFGLVNDT DRYLTAESFG FKVNASAPSL KRKQTWVLEP DPGQGTAVLL RSSHLGRYLS AEEDGRVACE AEQPGRDCRF LVLPQPDGRW VLRSEPHGRF FGGTEDQLSC FATAVSPAEL WTVHLAIHPQ AHLLSVSRRR YVHLCPREDE MAADGDKPWG VDALLTLIFR SRRYCLKSCD SRYLRSDGRL VWEPEPRACY TLEFKAGKLA FKDCDGHYLA PVGPAGTLKA GRNTRPGKDE LFDLEESHPQ VVLVAANHRY VSVRQGVNVS ANQDDELDHE TFLMQIDQET KKCTFYSSTG GYWTLVTHGG IHATATQVSA NTMFEMEWRG RRVALKASNG RYVCMKKNGQ LAAISDFVGK DEEFTLKLIN RPILVLRGLD GFVCHHRGSN QLDTNRSVYD VFHLSFSDGA YRIRGRDGGF WYTGSHGSVC SDGERAEDFV FEFRERGRLA IRARSGKYLR GGASGLLRAD ADAPAGTALW EY
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Molecular Weight
55 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
The FSCN2 (Fascin 2) protein is a member of the fascin family of actin-bundling proteins, which play critical roles in cell motility, architecture, and the formation of cellular structures such as filopodia and microvilli. The study of FSCN2 has gained attention due to its unique expression in various tissues, particularly in the brain and skeletal muscle, implicating its potential involvement in regulating neuronal development and muscle function. Recent research has indicated that FSCN2 may play a role in neurodegenerative diseases and muscle disorders, suggesting its importance as a therapeutic target. Investigating the recombinant form of FSCN2 is crucial for understanding its structure-function relationship, allowing researchers to dissect its molecular mechanisms in cellular processes. The ability to produce and purify FSCN2 as a recombinant protein facilitates detailed biochemical characterization and exploration of its interactions with actin and other cellular partners. This research may provide insights into the protein's role in health and disease, potentially leading to the development of novel strategies for modulating its function in various medical conditions.
