HIV-1 RT p66 (C terminus) Specific Neutra™ Antibody (V3S-0923-XY33), Human IgG (CAT#: V3S-0923-XY33)

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Datasheet

MSDS

COA

Summary
Property
Applications
Protocols
Target

Summary

Description This antibody is a mouse neutralizing antibody clone F-6 binding with HIV-1 RT. It binds to the carboxyl terminus of the large subunit of RT, which contains the ribonuclease H (RNase H) domain, and not the polymerase domain of the protein. F-6 inhibits the RNA-dependent DNA polymerase (RDDP) activity of RT and inhibits also its DNA-dependent DNA polymerase (DDDP) activity.
Clonality Monoclonal
Host Species Human
Target Species HIV-1
Epitope F-6 binds to the carboxyl terminus of the large subunit of RT, which contains the ribonuclease H (RNase H) domain, and not the polymerase domain of the protein.
Neutralization Breath Inhibited 55% of the HIV-1 RT activity.
IC50 60 nM (Inhibition of RDDP activity)
Affinity 43.87 nM
Isotype Human IgG

Property

Expression Species HEK293F or CHO cell line
Conjugation Unconjugated
Purity >95%
Endotoxin <1 EU/mg
Form Liquid
Purification Protein A purified
Sterility 0.2 μM filtered
Formulation PBS, pH 7.4
Preservation No preservatives
Stabilizer No stabilizers
Storage Store at 4°C within one or two weeks. Store at -20°C for long term. Avoid repeated freeze/thaw cycles. Refer to the COA file for specifics.

Applications

Application ELISA; WB; SPR
Application Notes Western blot (WB): The nitrocellulose was washed with PBS and incubated with the antibody overnight at 4°C.
Surface plasmon resonance (SPR): Immobilization resulted in 5600 response units and various concentrations of antibody in PBS were injected over the surface at 30 μL/min at 25°C.

Protocols

ELISA Enzyme-Linked Immunosorbent Assay Protocol
WB Western Blot Protocol
FC Flow Cytometry Protocol

Target

Target HIV-1 RT p66
Alternative Name Human immunodeficiency virus type 1 reverse transcriptase
Research Area Infectious Disease
Related Disease Acquired Immune Deficiency Syndrome
For research use only, not directly for clinical use.
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