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Contributor Information

  • Institute University of Tartu

Tool Details

  • Tool name: Anti-human Neuropilin-1 b1b2 [clone 3E7; mAB2]
  • Alternate names: 3E7, mAB2, (mAB2 in studies published in Science)
  • Tool type: Antibodies
  • Class: Monoclonal
  • Conjugate: Unconjugated
  • Reactivity: Human
  • Host: Mouse
  • Application: IHC ; IF ; WB
  • Description: Monoclonal antibody raised against human NRP-1 b1b2 domain, clone 3E7 (mAB2 in studies published in Science). No blocking binding of CendR peptides to b1 domain of NRP-1. In recent years the relevance of CendR pathway for cellular uptake of biological nanoparticles – viruses - has been demonstrated in several independent studies. A direct role of Neuropilin (NRP) in virus entry has been demonstrated for three viruses, the retrovirus Human T-cell lymphotropic virus type 1 (HTLV-1) and the herpes viruses EBV and CMV5-8. In the case of CMV, NRP-2 acts as a receptor only for specific cell types, while in fibroblasts the virus uses a different molecule for entry. Viruses that display CendR peptides on their surface are expected to bind a specific CendR binding pocket on the extracellular domain of NRP. Ample evidence obtained with synthetic and phage-displayed CendR peptides shows that they bind to conserved binding pocket in b1 domain of NRP-1. The inventors have developed a monoclonal antibody that specifically interacts with the CendR binding pocket of the b1 domain of Neuropilin-1 and blocks binding of CendR peptides. This monoclonal antibody has potential applications in the research of SARS-CoV2 in that the antibody is capable to reduce/block the internalisation of SARS-CoV2 into cells, thus to stop viral replication.
  • Immunogen: Human wild-type Neuropilin-1 CendR b1b2 region
  • Myeloma used: P3X63Ag8.653

  • For Research Use Only

Target Details

  • Target: human Neuropillin-1 b1b2 domain
  • Target background: Monoclonal antibody raised against human NRP-1 b1b2 domain, clone 3E7 (mAB2 in studies published in Science). No blocking binding of CendR peptides to b1 domain of NRP-1. In recent years the relevance of CendR pathway for cellular uptake of biological nanoparticles – viruses - has been demonstrated in several independent studies. A direct role of Neuropilin (NRP) in virus entry has been demonstrated for three viruses, the retrovirus Human T-cell lymphotropic virus type 1 (HTLV-1) and the herpes viruses EBV and CMV5-8. In the case of CMV, NRP-2 acts as a receptor only for specific cell types, while in fibroblasts the virus uses a different molecule for entry. Viruses that display CendR peptides on their surface are expected to bind a specific CendR binding pocket on the extracellular domain of NRP. Ample evidence obtained with synthetic and phage-displayed CendR peptides shows that they bind to conserved binding pocket in b1 domain of NRP-1. The inventors have developed a monoclonal antibody that specifically interacts with the CendR binding pocket of the b1 domain of Neuropilin-1 and blocks binding of CendR peptides. This monoclonal antibody has potential applications in the research of SARS-CoV2 in that the antibody is capable to reduce/block the internalisation of SARS-CoV2 into cells, thus to stop viral replication.

Application Details

  • Application: IHC ; IF ; WB

Handling

  • Format: Liquid
  • Shipping conditions: Shipping at 4°C

Documentation

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References

  • •  Canturi-Castelvetri et al,. 2020doi:10.1101/2020.06.07.137802
  • •  Cantuti-Castelvetri et al. 2020. Science. 370(6518):856-860. PMID: 33082293.