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Human Anti-Virus HIV gp120-CD4 Binding Heterohybridoma [559-E]   (CSC-H0846)  


This hybridoma produces mAbs (IgG1 kappa) against virus HIV gp120-CD4 Binding           Datasheet

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General Information
Isotype
IgG1 kappa
Fusion Species
Human X Mouse Heterohybridoma
Immunological Donor
Human
Clone
559-E
Cell Line Description
Human peripheral blood mononuclear cells from HIV seropositive patients were transformed with Epstein-Barr virus (EBV). Antibody producing clones were expanded and fused with SHM-D33 heterohybridoma cells . The antibody is specific for the CD4-binding domain of the gp120 protein of HIV-1; it inhibits CD4-rgp120 binding. It has broad HIV group specificity and reacts with the HTLV-IIIB, MN and SF-2 strains of HIV-1.
Application Notes
ELISA and neutralization assays.
Morphology
Lymphoblast
Growth Properties
Suspension
Culture Method
Complete Growth Medium
RPMI 1640 with 2 mM L-glutamine, 10 mM HEPES, 1 mM sodium pyruvate, 4500 mg/L glucose and 1500 mg/L sodium bicarbonate

, supplemented with FBS.
Subculturing
Incubate cells at 37°C with 5% CO2 in air atmosphere, renew medium every 2-3 days, start cells at 2x10^5 cells/mL and maintain cultures between 1x10^5-2x10^6 cells/ml
Storage
Liquid nitrogen vapor phase.
Target
Introduction
HIV infection is initiated by the selective interaction between the cellular receptor CD4 and gp120, the external envelope glycoprotein of the virus. We used analytical ultracentrifugation, titration calorimetry, and surface plasmon resonance biosensor analysis to characterize the assembly state, thermodynamics, and kinetics of the CD4-gp120 interaction. The binding thermodynamics were of unexpected magnitude; changes in enthalpy, entropy, and heat capacity greatly exceeded those described for typical proteinprotein interactions. These unusual thermodynamic properties were observed with both intact gp120 and a deglycosylated and truncated form of gp120 protein that lacked hypervariable loops V1, V2, and V3 and segments of its N and C termini. Together with previous crystallographic studies, the large changes in heat capacity and entropy reveal that extensive structural rearrangements occur within the core of gp120 upon CD4 binding. CD spectral studies and slow kinetics of binding support this conclusion. These results indicate considerable conformational ?exibility within gp120, which may relate to viral mechanisms for triggering infection and disguising conserved receptor-binding sites from the immune system.
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