Serratia spp. serological reagents

Application Concanavalin A from Canavalia ensiformis (jack bean) has been used: to induce spleen blastogenesis to generate ConA blast targets from B6 and lpr spleen cells to stimulate splenic lymphocytes from estrogen-and placebo-treated mice

Concanavalin A&nbsp(con A) is a plant lectin refined from jack beans. It is a tetrameric protein, which has four identical 28 kDa subunits.

Concanavalin A&nbsp(con A) is a plant lectin refined from jack beans. It is a tetrameric protein, which has four identical 28 kDa subunits.

Concanavalin A&nbsp(con A) is a plant lectin refined from jack beans. It is a tetrameric protein, which has four identical 28 kDa subunits.

Concanavalin A&nbsp(con A) is a plant lectin refined from jack beans. It is a tetrameric protein, which has four identical 28 kDa subunits.

Concanavalin A is a protein containing only &#946-sheets in its structure, and belongs to the legume lectins family. Application Concanavalin A from Canavalia ensiformis (Jack bean) has been used: in in vitro cell proliferation assay and cell

Concanavalin A is isolated from the from Canavalia ensiformis (Jack bean). It is a mitogenic lectin with a dome-like structures and is a tetrameric protein.

Concanavalin A is isolated from the from Canavalia ensiformis (Jack bean). It is a mitogenic lectin with a dome-like structures and is a tetrameric protein.

Concanavalin A (Con A), isolated from Jack beans ( Canavalia ensiformis ), is a mannose or glucose specific-binding lectin. The lectin is a tetramer and each subunit possesses a saccharide-binding site.

Concanavalin A (Con A), isolated from Jack beans ( Canavalia ensiformis ), is a mannose or glucose specific-binding lectin. The lectin is a tetramer and each subunit possesses a saccharide-binding site.

Concanavalin A (Con A), isolated from Jack beans ( Canavalia ensiformis ), is a mannose or glucose specific-binding lectin. The lectin is a tetramer and each subunit possesses a saccharide-binding site.

Application For the fluorescent detection of glycoproteins containing &#945&#8722 D -mannose or &#945&#8722 D -glucose Biochem/physiol Actions Con A is not blood group specific but has an affinity for terminal &#945- D -mannosyl and &#945- D