HPA004835
Anti-ZYX antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-Zyxin antibody produced in rabbit, Anti-Zyxin-2 antibody produced in rabbit
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About This Item
Recommended Products
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
product line
Prestige Antibodies® Powered by Atlas Antibodies
form
buffered aqueous glycerol solution
species reactivity
human
technique(s)
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500
immunogen sequence
PAPKFSPVTPKFTPVASKFSPGAPGGSGSQPNQKLGHPEALSAGTGSPQPPSFTYAQQREKPRVQEKQHPVPPPAQNQNQVRSPGAPGPLTLKEVEELEQLTQQLMQDMEHPQRQNVAVNE
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
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.
Immunogen
Zyxin recombinant protein epitope signature tag (PrEST)
Application
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 sigma.com/prestige.
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:
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.
Linkage
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 Merck KGaA, Darmstadt, Germany
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 1
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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Ronald C van Gaal et al.
Journal of polymer science (2020), 59(12), 1253-1266 (2021-07-16)
Supramolecular motifs in elastomeric biomaterials facilitate the modular incorporation of additives with corresponding motifs. The influence of the elastomeric supramolecular base polymer on the presentation of additives has been sparsely examined, limiting the knowledge of transferability of effective functionalization between
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
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
S Gregory Call et al.
Biochemical and biophysical research communications, 415(3), 485-489 (2011-11-08)
Cell-cell junction remodeling is associated with dramatic actin reorganizations. Several actin regulatory systems have been implicated in actin remodeling events as cell-cell contacts are assembled and disassembled, including zyxin/LPP-VASP complexes. These complexes facilitate strong cell-cell adhesion by maintaining actin-membrane connections.
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