Anti-Neuropilin 1 Antibody Picoband® (monoclonal, 8G6G7)

This gene encodes one of two neuropilins, which contain specific protein domains which allow them to participate in several different types of signaling pathways that control cell migration. Neuropilins contain a large N-terminal extracellular domain, made up of complement-binding, coagulation factor V/VIII, and meprin domains. These proteins also contain a short membrane-spanning domain and a small cytoplasmic domain. Neuropilins bind many ligands and various types of co-receptors; they affect cell survival, migration, and attraction. Some of the ligands and co-receptors bound by neuropilins are vascular endothelial growth factor (VEGF) and semaphorin family members. Several alternatively spliced transcript variants that encode different protein isoforms have been described for this gene.

Replication protein A 70 kDa DNA-binding subunit; RP-A p70; Replication factor A protein 1; RF-A protein 1; Single-stranded DNA-binding protein; Replication protein A 70 kDa DNA-binding subunit, N-terminally processed; RPA1; REPA1; RPA70

E.coli-derived human Neuropilin 1 recombinant protein (Position: K504-T827) . Human Neuropilin 1 shares 95% and 94% amino acid (aa) sequences identity with mouse and rat Neuropilin 1, respectively.

As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism (PubMed:27723720, PubMed:27723717) . Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682) . In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808) . It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage (PubMed:17765923) . Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716) . Plays also a role in base excision repair (BER) probably through interaction with UNG (PubMed:9765279) . Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance (PubMed:17959650) . As part of the alternative replication protein A complex, aRPA, binds single- stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S- phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105) .

1. Gagnon, M. L., Bielenberg, D. R., Gechtman, Z., Miao, H.-Q., Takashima, S., Soker, S., Klagsbrun, M. Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: in vivo expression and antitumor activity. Proc. Nat. Acad. Sci. 97: 2573-2578, 2000. 2. Gu, C., Rodriguez, E. R., Riemert, D. V., Shu, T., Fritzsch, B., Richards, L. J., Kolodkin, A. L., Ginty, D. D. Neuropilin-1 conveys semaphorin and VEGF signaling during neural and cardiovascular development. Dev. Cell 5: 45-57, 2003.

At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing.