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

Overview

Anti-Neuropilin 1 Antibody Picoband® (monoclonal, 8G6G7) is an antibody reagent for detection of NRP1 (replication protein A1). Researchers commonly use anti-NRP1 antibodies to measure relative expression and localization across biological samples, with assay selection guided by the listed applications (WB, IHC, IF, ICC, Flow, ELISA).

Boster Bio Anti-Neuropilin 1 Antibody Picoband® (monoclonal, 8G6G7) catalog # M01324-2. Tested in Flow Cytometry, IF, ICC, WB applications. This antibody reacts with Human, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.

Key elements and design rationale

• Target: NRP1 (replication protein A1). Alternative names: 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
• Antibody format: Monoclonal; clone 8G6G7; Mouse IgG2a
• Species context: Host: Mouse, Reactivity: Human,Rat
• Purification: Immunogen affinity purified.
• Immunogen: 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.
• Molecular weight context: observed 120 kDa (reported)
• Provided application(s): WB, IHC, IF, ICC, Flow, ELISA

These attributes help contextualize how the antibody is commonly selected (host/clonality/isotype/label) and how signals are interpreted across sample types and assay formats.

Biological background

Function: 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).

Cellular localization: Nucleus

Tissue details: Expressed in lung fibroblasts (at protein level). Expressed in monocytes. Highly expressed in liver, also found in kidney and brain.

Background: 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.

Cross reactivity: No cross-reactivity with other proteins.

Research relevance and current trends

• Quantitative and spatial profiling: expression patterns are increasingly studied across cell states using multiplex imaging and omics-informed validation.
• Isoforms and post-translational modifications: researchers often evaluate how isoform composition and PTMs can shift apparent molecular weight or localization.
• Context-aware interpretation: comparative studies commonly include perturbations (stimulation, inhibition, genetic models) to relate target changes to pathway behavior.

Common research applications

• Western blot (WB): compare relative target abundance and apparent size shifts (e.g., isoforms/PTMs) across conditions.
• Immunohistochemistry (IHC): assess distribution across tissue compartments and compare staining patterns between groups.
• Immunofluorescence / ICC: evaluate subcellular localization and co-localization with compartment markers.
• Flow cytometry: quantify target-positive populations and compare shifts after stimulation or differentiation.

Across these uses, researchers typically interpret changes in signal as relative differences between matched sample groups, considering sample preparation and biological context.

Notes for experimental interpretation

• Apparent molecular weight can vary due to isoforms, proteolysis, glycosylation, phosphorylation, and sample preparation differences.
• Species reactivity and epitope conservation can influence observed signal patterns, especially in cross-species studies.
• Control concepts: include appropriate negative controls (e.g., isotype controls where relevant) and, when feasible, genetic or orthogonal controls (KO/KD, peptide competition, or independent assays) to support interpretation.

For antibody reagents, monoclonal antibodies are often chosen for epitope consistency across lots, while polyclonals may recognize multiple epitopes and can show different background characteristics depending on context.

Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.