Anti-Laminin-Binding Lectin monoclonal antibody (DMAB9553)

Rat anti-Mouse PDCD1 monoclonal antibody for IP, WB Datasheet

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Host Species
Species Reactivity
Laminin-binding lectin from chicken.


Alternative Names
LBL; Laminin-Binding Lectin

Product Background

Antigen Description
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.


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de Oliveira, EP; Silveira, LPD; et al. EFFECT OF SHADE AND FOULING OF SEED ON THE DEVELOPMENT OF CULTIVARS OF Panicum maximum Jacq.. BIOSCIENCE JOURNAL 30:1682-1691(2014).
Villares, A; Moreau, C; et al. Impact of Ionic Strength on Chitin Nanocrystal-Xyloglucan Multilayer Film Growth. BIOPOLYMERS 101:924-930(2014).

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