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Villin1 Recombinant Rabbit Monoclonal Antibody (IRS243RB)

Price: Regular price $278.00

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Catalog# IRS243RB

Rabbit Monoclonal to Villin1

Tested for

  • mIHC

Reacts with

  • Mouse

Recombinant production enables lot-to-lot consistency and is animal-cruelty-free

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Specifications

Product Type

Recombinant Rabbit monoclonal primary

Product Name

Villin1 Recombinant Rabbit Monoclonal Antibody (IRS243RB)

Immunogen

Synthetic peptide within human villin1 aa 176-225 / 827.

Host

Rabbit

Positive Control

Mouse small intestine tissue.

Conjugation

Unconjugated

Clonality

Monoclonal

APPLICATION DILUTION

  • mIHC

  • 1:100

PROPERTIES

Form

Liquid

Storage Condition

Shipped at 4C. Store at +4C short term (1-2 weeks). It is recommended to aliquot into single-use upon delivery. Store at -20C long term.

Storage Buffer

1*PBS (pH7.4), 0.1% BSA, 40% Glycerol, 0.2% Proclean 950.

Purification

Protein A affinity purified.

Molecular Weight

Predicted band size: 93 kDa

Isotype

IgG

TARGET

UNIPROT #

Q62468

PROTEIN NAME

Villin1

SYNONYMS

D2S1471 antibody;OTTHUMP00000164145 antibody;VIL antibody;VIL1 antibody;VILI_HUMAN antibody;Villin 1 antibody;Villin-1 antibody;Villin1 antibody

SUBCELLULAR LOCATION

Cytoskeleton.

FUNCTION

Caldesmon, Filamin 1, Nebulin and Villin are differentially expressed and regulated Actin binding proteins. Both muscular (CDh) and non-muscular (CDl) forms of Caldesmon have been identified and each has been shown to bind to Actin as well as to calmodulin and myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CDl is widely expressed in non-muscle tissues and cells. Filamin 1, which is ubiquitously expressed and exists as a homodimer, functions to crosslink Actin to filaments. Nebulin is a large filamentous protein specific to muscle tissue that may function as a ruler for filament length. Several isoforms of Nebulin are produced by alternative exon usage. Villin is Ca2+-regulated and is the major structural component of the brush border of absorptive cells.

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