Concanavalin A (Con A) , derived from Canavalia ensiformis beans, is a lectin protein (Mw 104 kDa). Under the condition of p27.0, Con A exists in a homogenous tetrameric structure, consisting of four subunits with a molecular weight of 26 kDa. Under acidic conditions (pH 4.5-5.5), on A dissociates into an activated dimeric structure of 52 kDa. Each monomer, regardless of pH or molecular structure, contains two metal case binding sites. Metal nanoparticles C82+and M2+must bind to both sites in order for Cn A to be active. Awakening is the process of generating a stable form of dimeric structure from other living organisms.
Concanavalin A (Con A) has no blood type specificity and selectively binds to - mannose/residues and a-glucose residues on various proteins, sugars, and class molecules. It requires the presence of Ca2+and Mn2+ions to display its activity. Con A is suitable for carbohydrate research, glycoprotein purification, enzyme labeling, thin membrane studies, Shao cell agglutination, and cell typing studies.
This is Alexa Fluor 594 labeled Concanavalin A (Alexa Fluor 594 ConA), purified by affinity purification at Ex/Em=590/617nm. The recommended working concentration range is 5-25 μ G/ml.