ANTI-P-PAXILLIN-TYR118 CLONE 1E19 ZOOMAB RABBIT MONOCLONAL (C15-1670-236)

General description

We are committed to bringing you greener alternative products, which adhere to one or more of The 12 Principles of Green Chemistry.This antibody is Preservative-free, produced without the harm or sacrifice of animals and exceptionally stable to allow for ambient shipping and storage if needed and thus aligns with "Waste Prevention", "Designing Safer Chemicals" and "Design for Energy Efficiency". Click here for more information.

ZooMAb^® antibodies represent an entirely new generation of recombinant monoclonal antibodies.Each ZooMAb^® antibody is manufactured using our proprietary recombinant expression system, purified to homogeneity, and precisely dispensed to produce robust and highly reproducible lot-to-lot consistency. Only top-performing clones are released for use by researchers. Each antibody is validated for high specificity and affinity across multiple applications, including its most commonly used application. ZooMAb^® antibodies are reliably available and ready to ship when you need them.

Specificity

Clone 1E19 is a ZooMAb^® Rabbit recombinant monoclonal antibody that specifically detects Paxillin phosphorylated on tyrosine 118.

Immunogen

KLH-conjugated linear peptide corresponding to 12 amino acids surrounding phosphotyrosine 118 in human Paxillin.

Application

Quality Control Testing

Evaluated by Western Blotting in lysates from C2C12 cells treated with Sodium Pervanadate.

Western Blotting Analysis: A 1:1,000 dilution of this antibody detected Paxillin phosphorylated on tyrosine 118 in lysate from overnight serum starved C2C12 cells treated with 5 mM sodium pervanadate, but not in untreated cells.

Tested applications

Flow Cytometry Analysis: 0.1 μg from a representative lot detected p-Paxillin-Tyr118 in untreated and Sodium Pervanadate treated C2C12 cells.

Peptide Inhibition Assay: Target band detection in a lysate from C2C12 cells treated sodium pervanadate was prevented by preblocking of a representative lot with the immunogen phosphopeptide, but not the corresponding non-phosphopeptide.

Immunocytochemistry Analysis: A 1:100 dilution from a representative lot detected p-Paxillin-Tyr118 in C2C12 treated with pervanadate cell line.

Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user

Target description

Paxillin (UniProt: P49023; also known as PXN) is encoded by the PXN gene (Gene ID: 5829) in human. Paxillin is a multi-functional, focal adhesion-associated, phosphotyrosine-containing cytoskeletal protein that is involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix. It is primarily within focal adhesions that transmembrane integrin molecules connect the actin cytoskeleton to the extracellular matrix. When phosphorylated on specific serine ant tyrosine residues, it serves an important scaffolding role at focal adhesions by recruiting structural and signal transduction molecules involved in cell movement and migration. The N-terminal half of paxillin contains a proline-rich region that could serve as an SH3 domain-binding site. Several tyrosine residues conforming to SH2 domain binding sites are also present. The N-terminal region also contains five LD motifs that are known to function as binding sites for other proteins. The C-terminal half of paxillin is comprised of four LIM domains that are zinc-binding structures resembling a double zinc finger domain. The third LIM domain is shown to play a major role in targeting paxillin to focal adhesions. These various motifs serve as docking sites for cytoskeletal proteins, tyrosine kinases, serine/threonine kinases, GTPase activating proteins, and other adaptor proteins that recruit additional enzymes into complex with paxillin. Paxillin is phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation, and following stimulation by mitogens. Phosphorylation of paxillin at tyrosine 31 and tyrosine 118 by protein tyrosine kinase 6 (PTK6) is reported to promote the activation of RAC1 via CRK/CrKII, which promotes migration and invasion. This ZooMAbZooMAb^® recombinant monoclonal antibody, generated by our propriety technology, offers significantly enhanced specificity, affinity, reproducibility, and stability over conventional monoclonals. (Ref.: López-Colomé, A.M., et al. (2017). J Hematol Oncol 10(1); 50; Schaller, M. (2001). Oncogene 20(44); 6459 6472; Salgia, R., et al. (1995). J. Biol. Chem. 270(10); 5039-5047).

Physical form

Purified recombinant rabbit monoclonal antibody IgG, lyophilized in PBS, 5% Trehalose, normal appearance a coarse or translucent resin. The PBS/trehalose components in the ZooMAb formulation can have the appearance of a semi-solid (bead like gel) after lyophilization. This is a normal phenomenon. Please follow the recommended reconstitution procedure in the data sheet to dissolve the semi-solid, bead-like, gel-appearing material. The resulting antibody solution is completely stable and functional as proven by full functional testing. Contains no biocide or preservatives, such as azide, or any animal by-products. Larger pack sizes provided as multiples of 25 μL.

Reconstitution

300 μg/mL after reconstitution at 25 μL per vial. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.

Storage and Stability

Recommend storage of lyophilized product at 2-8°C; Before reconstitution, micro-centrifuge vials briefly to spin down material to bottom of the vial; Reconstitute each vial by adding 25 μL of filtered lab grade water or PBS; Reconstituted antibodies can be stored at 2-8°C, or -20°C for long term storage. Avoid repeated freeze-thaws.

Legal Information

ZooMAb 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.