Rat anti-Mouse PDCD1 monoclonal antibody for IP, WB
A 190/220-kDa complex found in integrin preparations was purified, and monoclonal antibodies were raised against it. The immunoaffinity-purified complex appears to be a trimer of very similar or identical 70-kDa subunits. It is a novel extracellular matrix molecule as determined by its subunit composition, N-terminal amino acid sequence, and in vivo localization. It is distributed widely in basement membranes including those from muscle, nerve, and kidney. It is also present in connective tissue regions such as perineurium and perimysium. It has the unusual property that it is initially expressed very late in avian development near the time of hatching. This protein is found to copurified with integrin because it binds to the carbohydrate support in Sepharose. Hemagglutination assays with mono- and disaccharides show that it functions as a lectin with galactoside-binding specificity. This protein is also found to bind strongly and specifically to laminin at a site distinct from its lectin activity, but does not bind to fibronectin or type IV collagen. The protein appears to be conserved and is a common contaminant of many laminin preparations. We call this novel protein "LBL" for laminin-binding lectin.
Peake, NJ; Pavlov, AM; et al. Controlled Release of C-Type Natriuretic Peptide by Microencapsulation Dampens Proinflammatory Effects Induced by IL-1 beta in Cartilage Explants. BIOMACROMOLECULES 16:524-531(2015).
Naseer, R; Mal, SS; et al. Redox, surface and electrocatalytic properties of layer-by-layer films based upon Fe(III)-substituted crown polyoxometalate [P8W48O184Fe16(OH)(28)(H2O)(4)](20-). ELECTROCHIMICA ACTA 134:450-458(2014).
Custom Antibody Labeling
We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody.