Human Anti-HIV-1 Env Recombinant Antibody (clone VRC06c) (CAT#: MRO-2805CQ)

This product is a recombinant human anti-HIV-1 monoclonal antibody. VRC06c specifically binds to Env.


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ELISA

Figure 1 Binding specificity of VRC06 to gp120 defined by ELISA.

Figure 1 Binding specificity of VRC06 to gp120 defined by ELISA.

VRC06 binding to YU2 gp120 was sensitive to gp120 mutations in both the CD4bs (D368R) and the CoRbs (I420R).

Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M., ... & Chakrabarti, B. K. (2012). HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelopglycoproteins. Journal of virology, 86(20), 11231-11241.

ELISA

Figure 2 VRC06 and VRC06b displayed unique binding properties for Env gp120.

Figure 2 VRC06 and VRC06b displayed unique binding properties for Env gp120.

VRC06 and VRC06b preferred recognition of Env of CD4-bound conformation (stabilized core, 2CC) and of trimeric context YU2 gp140-F trimer. The CoRbs MAb 17b was used as control.

Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M., ... & Chakrabarti, B. K. (2012). HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelopglycoproteins. Journal of virology, 86(20), 11231-11241.

FC

Figure 3 VRC06 and related MAbs recognized quaternary epitopes on Env functional trimer.

Figure 3 VRC06 and related MAbs recognized quaternary epitopes on Env functional trimer.

Binding of VRC06 to JR-FL gp160 CTtransfected 293T cell surface by FACS assay, represented by MFI (mean of fluorescence intensity).

Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M., ... & Chakrabarti, B. K. (2012). HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelopycoproteins. Journal of virology, 86(20), 11231-11241.

Neu

Figure 4 VRC06 neutralization potency against JR-FL gp160 CT virus was affected by Env mutations leading to an alteration of neutralization sensitivity.

Figure 4 VRC06 neutralization potency against JR-FL gp160 CT virus was affected by Env mutations leading to an alteration of neutralization sensitivity.

Env mutants 301 and T569A/I675V display enhanced neutralization sensitivity to CD4bs MAb F105 but substantially decreased neutralization sensitivity to VRC06.

Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M., ... & Chakrabarti, B. K. (2012). HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelopycoproteins. Journal of virology, 86(20), 11231-11241.

Neu

Figure 5 Neutralization potency of VRC06 against JR-FL gp160 CT virus.

Figure 5 Neutralization potency of VRC06 against JR-FL gp160 CT virus.

The bar graphs depict the effects of the Env mutations 301 and T569A/I675V on the HIV sensitivity (IC50 values) to VRC06 and other CD4bs ligands.

Li, Y., O'Dell, S., Wilson, R., Wu, X., Schmidt, S. D., Hogerkorp, C. M., ... & Chakrabarti, B. K. (2012). HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelopoproteins. Journal of virology, 86(20), 11231-11241.

FC

Figure 6 FACS-based binding curves of MAbs to the cell surface JRFL-cleaved trimers.

Figure 6 FACS-based binding curves of MAbs to the cell surface JRFL-cleaved trimers.

The CD4bs-directed bNabs

Chakrabarti, B. K., Feng, Y., Sharma, S. K., McKee, K., Hedestam, G. B. K., LaBranche, C. C., ... & Wyatt, R. T. (2013). Robust neutralizing antibodies elicited by HIV-1 JRFL envelope glycoprotein trimers in nonhuman primates. Journal of virology, 87(24), 13239-13251.


Specifications

  • Host Species
  • Human
  • Type
  • Human IgG1
  • Specificity
  • Recognizes HIV-1 Env
  • Species Reactivity
  • HIV-1
  • Clone
  • VRC06c
  • Applications
  • ELISA, FC, Neut

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.

Applications

  • Application Notes
  • The HIV-1 Env antibody has been reported in applications of Enzyme-linked Immunosorbent Assay, Flow Cytometry, Neutralization.

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.

Downloads

Download resources about recombinant antibody development and antibody engineering to boost your research.

See other products for "Clone VRC06c"

See other products for "HIV-1 Env"

Single-domain Antibody

CAT Product Name Application Type
NABG-057 Recombinant Anti-HIV-1 env VHH Single Domain Antibody ELISA, IHC, FC, FuncS Llama VHH

Recombinant Antibody

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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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