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S8695

Sigma-Aldrich

Anti-Supervillin antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Supervillin Isoform 1

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~250 kDa

species reactivity

human, mouse

technique(s)

indirect immunofluorescence: 10-20 μg/mL using human HeLa cells
western blot: 2.5-5 μg/mL using whole extracts of differentiated mouse C2 cells
western blot: 5-10 μg/mL using whole extracts of human HeLa cells

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SVIL(6840)
mouse ... Svil(225115)

General description

Supervillin is an F-actin-binding protein originally isolated from bovine neutrophils. It has two isoforms of reported 205/250 kDa. The longer isoform named archvillin is muscle specific. Supervillin is a tightly bound peripheral membrane protein that is concentrated at sites of epithelial cell-cell adhesion. The COOH-terminus of supervillin is homologous to villin/gelsolin. The NH2-terminus contains functional nuclear localization sequences and F-actin and myosin II binding domains. Supervillin is found in many cells of several species, but is most abundant in muscle, bone marrow, thyroid gland and salivary gland.

Immunogen

synthetic peptide corresponding to amino acid residues 900-918 of human supervillin with C-terminal added cysteine, conjugated to KLH. The corresponding sequence differs by two amino acids in mouse.

Application

Anti-Supervillin antibody produced in rabbit has been used in:
  • immunoblotting
  • chromatin immunoprecipitation (ChIP)
  • immunofluorescence

Biochem/physiol Actions

Supervillin participates in cell-cell adhesion, motility regulation and information transfer between cell compartments. It has been suggested that supervillin may mediate actin and myosin II filament organization at cholesterol-rich membrane domains. Supervillin has been identified as a transcriptional activator of the androgen receptor. Increased levels of supervillin are found in many carcinoma cell lines, including HeLa S3 cervical carcinoma, SW480 adenocarcinoma and A549 lung carcinoma cells.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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F-actin and myosin II binding domains in supervillin
Chen Y, et al.
Test, 278(46), 46094-46106 (2003)
Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton
Oh SW, et al.
Journal of Cell Science, 116(11), 2261-2275 (2003)
Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals
Wulfkuhle JD, et al.
Journal of Cell Science, 112(13), 2125-2136 (1999)
Supervillin associates with androgen receptor and modulates its transcriptional activity
Ting HJ, et al.
Proceedings of the National Academy of Sciences of the USA, 99(2), 661-666 (2002)
Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes
Nebl T, et al.
The Journal of Biological Chemistry, 277(45), 43399-43409 (2002)

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