Analytical Data
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Gene name
FSCN
- Application
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Alternative Names
FSCN;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
Q16658
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Expression Region
2-493aa
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AA Sequence
TANGTAEAV QIQFGLINCG NKYLTAEAFG FKVNASASSL KKKQIWTLEQ PPDEAGSAAV CLRSHLGRYL AADKDGNVTC EREVPGPDCR FLIVAHDDGR WSLQSEAHRR YFGGTEDRLS CFAQTVSPAE KWSVHIAMHP QVNIYSVTRK RYAHLSARPA DEIAVDRDVP WGVDSLITLA FQDQRYSVQT ADHRFLRHDG RLVARPEPAT GYTLEFRSGK VAFRDCEGRY LAPSGPSGTL KAGKATKVGK DELFALEQSC AQVVLQAANE RNVSTRQGMD LSANQDEETD QETFQLEIDR DTKKCAFRTH TGKYWTLTAT GGVQSTASSK NASCYFDIEW RDRRITLRAS NGKFVTSKKN GQLAASVETA GDSELFLMKL INRPIIVFRG EHGFIGCRKV TGTLDANRSS YDVFQLEFND GAYNIKDSTG KYWTVGSDSA VTSSGDTPVD FFFEFCDYNK VAIKVGGRYL KGDHAGVLKA SAETVDPASL WEY
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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
FSCN (Fascin) proteins are actin-binding proteins that play crucial roles in the regulation of cell morphology, motility, and adhesion. They are highly expressed in various cell types, particularly in dendritic cells, neuronal cells, and cancer cells, where they contribute to the organization of actin filaments and the formation of cellular protrusions such as filopodia and lamellipodia. The study of FSCN recombinant proteins has gained significant attention due to their implications in understanding fundamental cellular processes and their potential role in pathological conditions, including cancer metastasis and neurological disorders. Research indicates that aberrant expression or activity of FSCN proteins can lead to enhanced migratory capabilities of cancer cells, making them targets for therapeutic intervention. Furthermore, the creation of recombinant FSCN proteins allows for detailed functional studies, including investigations of their biochemical properties and interactions with other cellular components. These studies can unravel the molecular mechanisms by which FSCN regulates actin dynamics and cell movement, offering insights into cellular responses to environmental cues. Overall, the exploration of FSCN recombinant proteins is vital for dissecting their biological functions, elucidating their contribution to disease progression, and developing novel strategies for targeted therapies.
