|Detection of Mouse and Rat Neuropilin‑2 by Western Blot. Western blot shows lysates of C6 rat glioma cell line, LL/2 mouse Lewis lung carcinoma cell line, and bEnd.3 mouse endothelioma cell line. PVDF membrane was probed with 0.5 µg/mL of Goat Anti-Mouse/Rat Neuropilin‑2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF567) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for Neuropilin‑2 at approximately 110 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Neuropilin‑2 in Rat Brain. Neuropilin‑2 was detected in perfusion fixed frozen sections of rat brain using Goat Anti-Mouse/Rat Neuropilin‑2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF567) at 15 µg/mL overnight at 4 °C. Tissue was stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm in neurons. View our protocol for Fluorescent IHC Staining of Frozen Tissue Sections.|
|Detection of Mouse and Rat Neuropilin‑2 by Simple WesternTM. Simple Western lane view shows lysates of C6 rat glioma cell line, LL/2 mouse Lewis lung carcinoma cell line, and bEnd.3 mouse endothelioma cell line, loaded at 0.2 mg/mL. A specific band was detected for Neuropilin‑2 at approximately 140 kDa (as indicated) using 5 µg/mL of Goat Anti-Mouse/Rat Neuropilin‑2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF567) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.|
Neuropilin-1 (Npn-1, previously known as Neuropilin) and Npn-2 (previously known as Npn-1-related molecule) are type I transmembrane proteins that bind members of the class III secreted semaphorin subfamily which are implicated in repulsive axon guidance. The extracellular domain of these proteins is composed of two N-terminal CUB (complement-binding) domains (domains a1 and a2), two domains with homology to coagulation factors V and VIII (domains b1 and b2) and a MAM (meprin) domain (domain c). In the absence of ligands, neuropilins can form homo- and hetero-oligomers via homophilic interactions of their MAM domains. At the amino acid sequence level, Npn-1and Npn-2 share 44% identity. Npn-1 and Npn-2 show different binding specificities for different members of the semaphorin family. The expression patterns of Npn-1 and Npn-2 in developing neurons of the central and peripheral nervous systems are largely, though not completely nonoverlapping. Npn‑1 and Npn-2 are also expressed by endothelial and tumor cells and have been shown to be isoform-specific receptors for VEGF165. Npn‑1 was also reported to bind PlGF-2 and the VEGF-like protein from of virus NZ2.
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|Excellent||Whole mount immunofluorescence||Mouse||Anonymous||09/07/2016||
Whole mount immunofluorescence: Mouse/Rat Neuropilin-2 Antibody [AF567]
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