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Mouse Svil (aa 1-2170 )
Svil Swiss - Prot #
Q8K4L3
Svil Protein names
Supervillin (Archvillin) (p205/p250)
Svil Gene names
Svil
Organism
Mus musculus (Mouse)
Svil Entry name
SVIL_MOUSE

Svil Codon-optimized cDNA Clone
Svil CDNA Cat#
RPY2711
Tag
cDNA Svil contains A 6x histidine tag
Condon optimized Svil cDNA Formulation
Liquid
Condon optimized Svil cDNA Storage
−20℃ to −70℃. Avoid repeated freeze-thaw cycles.
Condon optimized Svil cDNA Application (s)
Applications: 1. Codon-optimized cDNA sequence designed for

recombinant protein production in both E.coli and Mammalian cell. The

cDNA has been cloned into E.coli expression vector with 6x Histidine tag. 2.

May be used as RNAi assistance to restore the loss-of-function.

Recombinant Svil Protein
Recombinant Svil Protein Cat#
PY2711
Svil Protein Source
Recombinant protein
Recombinant Svil Protein Applications
Western Blot, may be used for other applications determined by user
Recombinant Svil Protein Purity
>90%, as determined by SDS-PAGE under reducing conditions
Recombinant Svil Protein Activity
N/A
Tag
Recombinant Svil contains A 6x histidine tag
Recombinant Svil protein Formulation
Liquid
Recombinant Svil protein Storage
−20℃ to −70℃. Avoid repeated freeze-thaw cycles.
Place Order for Recombinant SvilProtein or cDNA
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Svil’s Protein family
Villin/gelsolin family
Svil’s Subcellular locations
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm > cytoskeleton. Cell

projection > invadopodium. Cell projection > podosome.
Svil’s FUNCTION (According to UniProtKB/Swiss-Prot)
FUNCTION: Forms a high-affinity link between the actin cytoskeleton and the

membrane. Isoform 1 (archvillin) is among the first costameric proteins to

assemble during myogenesis and it contributes to myogenic membrane structure

and differentiation. Appears to be involved in myosin II assembly. May modulate

myosin II regulation through MLCK during cell spreading, an initial step in cell

migration. May play a role in invadopodial function. Isoform 2 may be involved in

modulation of focal adhesions. Supervillin-mediated down-regulation of focal

adehesions involves binding to TRIP6 (By similarity).
Svil Sequence databases
EMBL DDBJ GenBank
Svil 3D structure databases
ModBase
Svil’s Protein-protein interaction databases
STRING
Svil’s Proteomic databases
PRIDE
Svil’s Genome annotation databases
Ensembl GeneID KEGG UCSC
Svil’s Organism-specific databases
CTD MGI
Svil’s Phylogenomic databases
eggNOG GeneTree HOGENOM HOVERGEN InParanoid OrthoDB PhylomeDB OMA
Svil’s Gene expression databases
Bgee ArrayExpress Genevestigator
Svil’s Family and domain databases
InterPro PROSITE ProtoNet

FOR in vitro RESEARCH USE ONLY. NOT FOR USE IN HUMANS.