Human Anti-HIV-1 gp160 Recombinant Antibody (clone VRC16.01) (CAT#: PABL-182)

Recombinant Human Antibody (VRC16.01) is capable of binding to HIV-1 gp160, expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-HIV-1 gp160 mAb and CH1-3 region of human IgG1 and a light chain (LC) encoding VL from anti-HIV-1 gp160 mAb and CL of human light chain. Exists as a disulfide linked dimer of the HC and LC hetero-dimer under non-reducing condition. This antibody neutralized 58% of circulating HIV-1 isolates


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Figure 1 Flow cytometric identification of RSC3-reactive IgG+ B cells from donor 44, C38 and Z258. Gating and percentage of antigen-specific (RSC3+, ΔRSC3-) memory B cells (CD19+, CD20+, IgG+) are indicated. Neighbor-joining trees display the protein distance of gp160 sequences from 176 gp160 sequences. A scale bar denotes 5% distance in amino acid sequence. Tree branches are colored by the neutralization potencies of VRC13.01, VRC16.01, VRC18.02 and VRC27.01 against each virus.

Figure 1 Flow cytometric identification of RSC3-reactive IgG+ B cells from donor 44, C38 and Z258. Gating and percentage of antigen-specific (RSC3+, ΔRSC3-) memory B cells (CD19+, CD20+, IgG+) are indicated. Neighbor-joining trees display the protein distance of gp160 sequences from 176 gp160 sequences. A scale bar denotes 5% distance in amino acid sequence. Tree branches are colored by the neutralization potencies of VRC13.01, VRC16.01, VRC18.02 and VRC27.01 against each virus.

Zhou, T., Lynch, R. M., Chen, L., Acharya, P., Wu, X., Doria-Rose, N. A.,... & Ernandes, M. J. (2015). Structural repertoire of HIV-1-neutralizing antibodies targeting the CD4 supersite in 14 donors. Cell, 161(6), 1280-1292.

Figure 2 Ability of W69 variants to interact with CD4-binding site ligands.

Figure 2 Ability of W69 variants to interact with CD4-binding site ligands.

Comparable amounts of radiolabeled monomeric gp120 from WT and W69 variants were incubated with 5 μg/ml of VRC16 for 1 h at 37°C. The precipitates were washed, run on SDS-polyacrylamide gels, and analyzed by densitometry. All values shown here were evaluated by the ligand binding capacity of WT gp120 (set as 1).

Ding, S., Tolbert, W. D., Prévost, J., Pacheco, B., Coutu, M., Debbeche, O.,... & Finzi, A. (2016). A highly conserved gp120 inner domain residue modulates Env conformation and trimer stability. Journal of virology, JVI-01068.

Figure 3 Viral neutralization by CD4-binding site ligands.

Figure 3 Viral neutralization by CD4-binding site ligands.

Recombinant HIV-1 expressing luciferase and bearing WT or W69 Env variants were normalized by reverse transcriptase activity. Equal amounts of viruses were incubated with serial dilutions of VRC16 for 1 h at 37°C before infecting Cf2Th-CD4-CCR5 cells. Luciferase activity in cell lysates was measured to determine the infectivity. Infectivity was normalized to 100% in the absence of the ligand.

Ding, S., Tolbert, W. D., Prévost, J., Pacheco, B., Coutu, M., Debbeche, O.,... & Finzi, A. (2016). A highly conserved gp120 inner domain residue modulates Env conformation and trimer stability. Journal of virology, JVI-01068.


Specifications

  • Host Species
  • Human
  • Type
  • Human IgG
  • Species Reactivity
  • HIV-1
  • Clone
  • VRC16.01
  • Applications
  • WB, Neut, FuncS

Product Property

  • Purity
  • >95% as determined by SDS-PAGE
  • Concentration
  • Please refer to the vial label for the specific concentration.
  • Buffer
  • PBS
  • Preservative
  • No preservatives
  • Storage
  • Centrifuge briefly prior to opening vial. Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

  • Alternative Names
  • ENV; gp160; envelope glycoprotein; Envelope surface glycoprotein gp160; precursor; hypothetical protein; Envelope surface glycoprotein gp120; Envelope transmembrane domain

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.

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For Research Use Only. Not For Clinical Use.

For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.

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