Anti-human Neuropilin-1 b1b2 [clone 1A4; mAb1]

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._x000D_ _x000D_ 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…

Contributors

Institute
University of Tartu
Cat. #: 160469
Unit size: 100 ug
Research Fields: Microbiology
Application: IHC ; IF ; WB
Target: human Neuropillin-1 b1b2 domain
Reactivity: Human
Host: Mouse
Class: Monoclonal
Alternate name: 1A4, mAB1 (mAB1 in studies published in Science)
Product 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.
Conjugation: Unconjugated
Immunogen: See Xbio/UOT/V/b1b2wt and Xbio/UOT/V/b1b2tm
Myeloma used: P3X63Ag8.653
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.
Format: Liquid
Shipping conditions: Dry ice
References:

Cantuti-Castelvetri et al. 2020. Science. 370(6518):856-860. PMID: 33082293.

Daly et al. 2020. Science. 370(6518):861-865. PMID: 33082294.

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