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Anti-ZYX antibody produced in rabbit

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Anti-Zyxin antibody produced in rabbit, Anti-Zyxin-2 antibody produced in rabbit
Human Protein Atlas Number:

biological source


Quality Level



antibody form

affinity isolated antibody

antibody product type

primary antibodies



product line

Prestige Antibodies® Powered by Atlas Antibodies


buffered aqueous glycerol solution

species reactivity



antibody small pack of 25 μL


immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500

immunogen sequence


UniProt accession no.

shipped in

wet ice

storage temp.


Gene Information

human ... ZYX(7791)

General description

ZYX (zyxin) is a proline-rich protein with a molecular mass of 61kDa. It is composed of three LIM domains followed by a zinc finger domain. It is widely expressed in human tissues specifically at the focal contacts in adherent erythroleukemia cells.


Zyxin recombinant protein epitope signature tag (PrEST)


Anti-ZYX antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project ( Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit

Biochem/physiol Actions

ZYX (zyxin) participates in actin remodeling in association with other proteins. It is localized at the cell-cell junctions and facilitates strong cell adhesion by interacting with α-actinin. It exerts response during external mechanical force and internal actin-myosin force. Depending on the activation of Rho-kinase and myosin II, ZYX accumulates at the force-bearing sites. It has been reported that the LIM domain drives the recruitment of zyxin during cell migration.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.


Corresponding Antigen APREST86861.

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Sigma-Aldrich Co. LLC


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.

Storage Class Code

10 - Combustible liquids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

Certificate of Origin

Katherine M Harrington et al.
The Journal of biological chemistry, 291(41), 21388-21406 (2016-08-05)
Accumulating evidence supports a role for prolactin (PRL) in the development and progression of human breast cancer. Although PRL is an established chemoattractant for breast cancer cells, the precise molecular mechanisms of how PRL regulates breast cancer cell motility and
Miki Fukumoto et al.
Cancer science, 108(5), 941-951 (2017-03-02)
Phosphoinositides play pivotal roles in the regulation of cancer cell phenotypes. Among them, phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2 ) localizes to the invadopodia, and positively regulates tumor cell invasion. In this study, we examined the effect of PI(3,4)P2 on focal adhesion dynamics
J Zumbrunn et al.
European journal of biochemistry, 241(2), 657-663 (1996-10-15)
We have cloned the gene for a novel LIM-domain protein from human fibroblasts whose expression is substantially decreased in simian-virus-40-(SV40)-transformed cells. This protein has a calculated molecular mass of 61 kDa and comprises a proline-rich domain followed by three LIM
T Macalma et al.
The Journal of biological chemistry, 271(49), 31470-31478 (1996-12-06)
Zyxin is a component of adhesion plaques that has been suggested to perform regulatory functions at these specialized regions of the plasma membrane. Here we describe the isolation and characterization of cDNAs encoding human and mouse zyxin. Both the human
Arisa Uemura et al.
Biophysical journal, 101(5), 1069-1075 (2011-09-06)
Cellular responses to mechanical perturbation are vital to cell physiology. In particular, migrating cells have been shown to sense substrate stiffness and alter cell morphology and speed. Zyxin is a focal adhesion protein that responds to external mechanical forces; however

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