Recombinant Anti-HIV-1 nef VHH Single Domain Antibody (PNBL-022)
CAT#: PNBL-022
Anti-HIV-1 Nef VHH Single Domain Antibody is a recombinant protein produced in E. coli.
Published Data
FuncS
Figure 1 Structure of the tripartite SH3B₆–Nef–sdAb19 complex.
Binding of the camelid antibody sdAb19 to HIV-1 Nef showed a dissociation constant of 39 nM.
Lülf, S., Matz, J., Rouyez, M. C., Järviluoma, A., Saksela, K., Benichou, S., & Geyer, M. (2014). Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody. Retrovirology, 11(1), 24.
FuncS
Figure 2 Functional analyses of Nef–sdAb19 interactions.
Mutation of D60R in sdAb19 gradually attenuated binding to Nef as determined by ITC measurements.
Lülf, S., Matz, J., Rouyez, M. C., Järviluoma, A., Saksela, K., Benichou, S., & Geyer, M. (2014). Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody. Retrovirology, 11(1), 24.
FuncS
Figure 3 Functional analyses of Nef–sdAb19 interactions.
Mutation of G102R/S103E in sdAb19 gradually attenuated binding to Nef as determined by ITC measurements.
Lülf, S., Matz, J., Rouyez, M. C., Järviluoma, A., Saksela, K., Benichou, S., & Geyer, M. (2014). Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody. Retrovirology, 11(1), 24.
FuncS
Figure 4 Functional analyses of Nef–sdAb19 interactions.
Mutation of the combined triple mutant D60R/G102R/S103E in sdAb19 gradually attenuated binding to Nef as determined by ITC measurements.
Lülf, S., Matz, J., Rouyez, M. C., Järviluoma, A., Saksela, K., Benichou, S., & Geyer, M. (2014). Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody. Retrovirology, 11(1), 24.
FuncS
Figure 5 Functional analyses of Nef–sdAb19 interactions.
Mutant sdAb19 proteins abrogate the inhibitory effect of sdAb19 on CD4 internalization. HeLa-CD4 cells were transfected with plasmids for expression of either Nef-GFP or GFP in combination with the plasmid for expression of wild-type or mutated sdAb19.
Lülf, S., Matz, J., Rouyez, M. C., Järviluoma, A., Saksela, K., Benichou, S., & Geyer, M. (2014). Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody. Retrovirology, 11(1), 24.
FuncS
Figure 6 Neffin binding to Nef results in a 2:2 complex formation.
Isothermal titration calorimetry confirms tight binding between Nef and Neffin exhibiting a Kd of 1.6 nM.
Lülf, S., Matz, J., Rouyez, M. C., Järviluoma, A., Saksela, K., Benichou, S., & Geyer, M. (2014). Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody. Retrovirology, 11(1), 24.
Inhib
Figure 7 Binding of sdAb19 in Neffin correlates with the inhibition of CD4 internalization.
HeLa-CD4 cells were transfected with plasmids for expression of either Nef-GFP or GFP in combination with the plasmid for expression of wild-type or mutated sdAb19 (1:3 Nef:sdAb19 plasmid ratio). Transfected cells were analyzed for CD4 cell surface expression and cell lysates were analyzed by Western blotting.
Lülf, S., Matz, J., Rouyez, M. C., Järviluoma, A., Saksela, K., Benichou, S., & Geyer, M. (2014). Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody. Retrovirology, 11(1), 24.
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Specifications
- Immunogen
- HIV-1 p27
- Host Species
- Llama
- Derivation
- Llama
- Type
- Llama VHH
- Species Reactivity
- HIV-1
- Clone
- PNBL-022
- Applications
- Inhib, WB, FuncS
Product Property
- Purity
- >95% by SDS-PAGE and HPLC analysis
- Storage
- Store the antibody (in aliquots) at -20°C. Avoid repeated freezing and thawing of samples.
Applications
- Application Notes
- The antibody was validated for Inhibition, Functional Assay, Western Blot. For details, refer to Published Data.
Target
- Alternative Names
- HIV Nef; Human Immunodeficiency Viruse Nef; Human Immunodeficiency Viruse; HIV Nef protein; HIV Nef-protein
- Gene ID
- 156110
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(Creative Biolabs Cat# PNBL-022, RRID: AB_3111724)
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Product Notes
This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:
• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production
See more details about Hi-Affi™ recombinant antibody benefits.
Datasheet
MSDS
COA
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| CAT | Product Name | Application | Type |
|---|---|---|---|
| MOB-472 | Recombinant Anti-HIV Nef Antibody | ELISA, WB, FuncS | IgG |
| MHH-472 | Recombinant Human Anti-HIV Nef Antibody | FC, Neut, Biosensors, FuncS | IgG |
| MRO-754CQ | Mouse Anti-HIV Nef Recombinant Antibody (MRO-754CQ) | ELISA, IP, IF, WB | Mouse IgG1, κ |
| VS-0625-FY777 | Mouse Anti-nef Recombinant Antibody (clone 2506W0672) | ELISA | Mouse IgG |
| CAT | Product Name | Application | Type |
|---|---|---|---|
| MOB-472-F(E) | Recombinant Anti-HIV Nef Antibody Fab Fragment | WB, FuncS | Fab |
| MHH-472-F(E) | Recombinant Human Anti-HIV Nef Antibody Fab Fragment | WB, Dot, FuncS | Fab |
| CAT | Product Name | Application | Type |
|---|---|---|---|
| MOB-472-S(P) | Recombinant Anti-HIV Nef Antibody scFv Fragment | IP, IF, Biosensors, FuncS | scFv |
| MHH-472-S(P) | Recombinant Human Anti-HIV Nef Antibody scFv Fragment | ELISA, WB, IF, FuncS | scFv |
| CAT | Product Name | Application | Type |
|---|---|---|---|
| MHC-YF576 | A*02:01/HIV Nef (LTFGWCFKL) MHC Pentamer | FCM | |
| MHC-YF577 | A*03:01/HIV Nef (QVPLRPMTYK) MHC Pentamer | FCM | |
| MHC-YF578 | A*11:01/HIV Nef (AVDLSHFLK) MHC Pentamer | FCM | |
| MHC-YF579 | A*24:02/HIV Nef (RYPLTFGWCF) MHC Pentamer | FCM | |
| MHC-YF580 | A*24:02/HIV Nef (RYPLTFGWCY) MHC Pentamer | FCM |
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