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Monoclonal antibodies against Manduca sexta (Sphingidae, Carolina sphinx, tobacco hornworm, moth) 120 kDa MsAPN1 receptor to CryIA(c)protein from Bacillus thuringiensis (9 lines)

Detailed Technology Description
ApplicationsThismouse monoclonal antibody was generated against gut and and is reactive for a120-kDa CryIA(c) aminopeptidase identified in brush-border membrane vesicles ofM. sexta, and it is applicable tostudies of agricultural parasite-host interactions and development ofpest-resistant crops.CryIA(c) delta-endotoxin, is a member of the C4 I family of Bacillusthuringiensis insecticidal proteins that, specifically recognize andbind with high affinity to target proteins (Aminopeptidase-N (APN1) andalkaline phosphatase (ALP) proteins) in the midgut of susceptible insects suchas Manducasexta or Carolina sphinx moth.
*Abstract

ReagentDescription           

Antigen:  120 kDA CryIA(c) aminopeptidase from M. sexta

CloneNames:  12B8.G2;  2B3.H4; 5D8.A3; 3H1.B6; 5F6.F2; 8G1.B1;12B8.C4; 2B3.H4.F1; 8G1.A2

Immunogen:  120kDA CryIA(c) aminopeptidase from M. sexta

SpeciesImmunized:  Mouse

Buffer:  Cell culture supernatant

Storage:  -80oC

Reference

Sangadala S, Walters FS, English LH, Adang MJ. A mixture ofManduca sexta aminopeptidase and phosphatase enhances Bacillus thuringiensisinsecticidal CryIA(c) toxin binding and 86Rb(+)-K+ efflux in vitro. J Biol Chem. 1994 Apr1;269(13):10088-92.

Country/Region
USA

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