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A3986

Sigma-Aldrich

Anti-Palladin antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-PALLD

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About This Item

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 ~140/90 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): 5-10 μg using lysates of HeLa cells
indirect immunofluorescence: 2-5 μg/mL using human HeLa cells
western blot: 0.5-1.0 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 ... PALLD(23022)

General description

Palladin exists in humans as 7 different isoforms and is a component of actin-containing microfilaments.
Palladin is a microfilament-associated phosphoprotein that is known to colocalize with alpha-actinin at cell-cell junctions, stress fibres, embryonic Z-lines, and focal adhesions. Palladin abnormalities have been linked to familial pancreatic cancer.
Rabbit anti-Palladin antibody binds to human palladin. Detection of the palladin band by immunoblotting is specifically inhibited by the immunizing peptide.
Palladin is a phosphoprotein, which is widely expressed in vertebrate cells and tissues. It is expressed as three major isoforms of 90, 140, and 200 kDa. Palladin consists of a proline-rich region in the NH2-terminal half of the protein and three tandem Ig C2 domains in the COOH-terminal.

Application

Rabbit anti-palladin antibody can be used for immunoprecipitation (5-10μg), indirect immunofluorescence (2-5μg/mL) and western blot (0.5-1.0μg/mL) using HeLa cells.

Biochem/physiol Actions

Palladin controls cell shape, adhesion, and contraction. It interacts with the actin-associated proteins α-actinin, VASP, ezrin, and profilin, suggesting that it is required for normal actin cytoskeleton organization. The Ig3 domain of palladin binds to F-actin. Its expression is required for normal mammalian embryogenesis since its inactivation leads to embryonic lethality.

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

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin
Rachlin AS and Otey CA
Journal of Cell Science, 119(6), 995-1004 (2006)
Palladin is an actin cross-linking protein that uses immunoglobulin-like domains to bind filamentous actin
Dixon RDS, et al.
Test, 283(10), 6222-6231 (2008)
Joshua S McLane et al.
Cancer microenvironment : official journal of the International Cancer Microenvironment Society, 9(2-3), 127-139 (2016-09-23)
Several changes have been described in the stroma surrounding a tumor, including changes in cellular composition, altered extracellular matrix composition and organization, and increases in stiffness. Tumor cells are influenced by the composition, organization, and mechanical properties of the microenvironment
Kay L Pogue-Geile et al.
PLoS medicine, 3(12), e516-e516 (2006-12-30)
Pancreatic cancer is a deadly disease. Discovery of the mutated genes that cause the inherited form(s) of the disease may shed light on the mechanism(s) of oncogenesis. Previously we isolated a susceptibility locus for familial pancreatic cancer to chromosome location
Characterization of human palladin, a microfilament-associated protein
Mykka?nen OM, et al.
Molecular Biology of the Cell, 12(10), 3060-3073 (2001)

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