#160471

Anti-human Neuropilin-1 b1b2 [clone 7E8; mAB3]

Please Enter Your Email ID
Email ID

Cat. #160471

Anti-human Neuropilin-1 b1b2 [clone 7E8; mAB3]

Cat. #: 160471

Unit size: 100 ug

Availability: 3-5 days

Target: human Neuropillin-1 b1b2 domain

Class: Monoclonal

Application: IHC ; IF ; WB

Reactivity: Human

Host: Mouse

£300.00

This fee is applicable only for non-profit organisations. If you are a for-profit organisation or a researcher working on commercially-sponsored academic research, you will need to contact our licensing team for a commercial use license.

Contributor

Institute: University of Tartu

Tool Details
Target Details
Applications
Handling
References

Tool Details

*FOR RESEARCH USE ONLY

  • Name: Anti-human Neuropilin-1 b1b2 [clone 7E8; mAB3]
  • Alternate name: 7E8, mAb3 (mAB3 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 7E8 (mAB3 in studies published in Science). Complete blockade 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
  • Isotype: IgG1 kappa
  • Myeloma used: P3X63Ag8.653

Target Details

  • Target: human Neuropillin-1 b1b2 domain
  • Target background: Monoclonal antibody raised against human NRP-1 b1b2 domain, clone 7E8 (mAB3 in studies published in Science). Complete blockade 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
  • Concentration: 1mg/ml
  • Unit size: 100 ug
  • Storage buffer: PBS with 0.02% azide
  • Storage conditions: -15° C to -25° C
  • 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.