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Contributor Information

  • Institute University of Tartu

Tool Details

  • Tool name: Anti-human Neuropilin-1 b1b2 [clone 1A4; mAb1]
  • Alternate names: 1A4, mAB1 (mAB1 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 1A4 (mAB1 in studies published in Science). Partially 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: See Xbio/UOT/V/ b1b2wt and Xbio/UOT/V/ b1b2tm
  • Research area: Microbiology
  • 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 1A4 (mAB1 in studies published in Science). Partially 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

References

  •   Cantuti-Castelvetri et al. 2020. Science. 370(6518):856-860. PMID: 33082293.
  •   Daly et al. 2020. Science. 370(6518):861-865. PMID: 33082294.