VRC-01 

VRC-01 is a broadly neutralizing IgG1 monoclonal antibody that targets HIV-1 envelope glycoprotein gp120 Protein. VRC-01 blocks HIV-1 viral entry by mimicking CD4 receptor interaction with HIV-1 gp120 and neutralizes broad HIV-1 clades. VRC-01 can be used for the research of HIV-1 infection^[1][2][3][4].

Human IgG1 kappa

Human IgG1 kappa, Isotype Control

Human

VRC-01 binds HIV-1 gp120 IIIB with K_d values of 1.68 nM and 1.39 nM for transient and stable tobacco plant-produced VRC-01, respectively^[2].
VRC-01 (1-24 h) from transient and stable tobacco plants neutralize HIV-1 BaL in TZM-bl cells with IC₅₀ values of 0.339 μg/mL and 0.407 μg/mL, respectively^[2].
VRC-01 (1-48 h) from transient tobacco plants neutralizes a panel of 10 HIV-1 Env pseudoviruses (clades A, B, C, G), while stable plant-produced VRC-01 shows slightly reduced potency against the same panel^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

VRC-01 (topical gel) protects humanized mice against vaginal HIV-1 infection^[2].
VRC-01 protects nonhuman primates against mucosal challenge with chimeric SHIV^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

P03377

ELISA, FACS, Functional assay

Unconjugated

The product can be reconstituted/diluted with sterile PBS or saline.

145.87 kDa

1412901-55-3

Liquid

Colorless to light yellow

[VRC-01]

Shipping with dry ice.

Please refer to the lot-specific COA for specific buffer information.

Please store the product under the recommended conditions in the Certificate of Analysis.

• 
  Immobilized envelope glycoprotein gp120 Protein, HIV-1 (AAC31819, HEK293, His, HY-P76390) can bind VRC-01. The EC₅₀ for this effect is 6.987 ng/mL.

• [1]. Boesch AW, et al. Highly parallel characterization of IgG Fc binding interactions. MAbs. 2014;6(4):915-927.

  [2]. Teh AY, et al. Characterization of VRC01, a potent and broadly neutralizing anti-HIV mAb, produced in transiently and stably transformed tobacco. Plant Biotechnol J. 2014;12(3):300-311.  [Content Brief]

  [3]. Sullivan MA, et al. Anti-idiotypic monobodies derived from a fibronectin scaffold. Biochemistry. 2013;52(10):1802-1813.

  [4]. Stelter S, et al. Engineering the interactions between a plant-produced HIV antibody and human Fc receptors. Plant Biotechnol J. 2020;18(2):402-414.