Anti-human Neuropilin-1 b1b2 [clone 3E7; mAB2]

Tool Details

*FOR RESEARCH USE ONLY (for other uses, please contact the licensing team)

• Name: Anti-human Neuropilin-1 b1b2 [clone 3E7; mAB2]
• Alternate name: 3E7, mAB2, (mAB2 in studies published in Science)
• Class: Monoclonal
• Conjugation: 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

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.

Applications

• Application: IHC ; IF ; WB

Handling

• Format: Liquid
• Unit size: 100 ug
• Shipping conditions: Shipping at 4° C

References

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