Nrp1 (Mouse) ELISA Kit

Regulatory status: For research use only, not for use in diagnostic procedures.

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COA

SDS

Datasheet

Sample

Serum

Species Reactivity

Mouse

Intended Use

Nrp1 (Mouse) ELISA kit comprises of one 96-well microplate, some buffers, some diluents, the substrate solution and the stop solution. Mouse neuropilin-1 can be measured quantitatively and specifically. This product is intended for research use only.

Contents of Kit

1. Mouse Neuropilin-1 standard: Recombinant mouse Neuropilin-1 (lyophilized powder): 1 vial. Dilution ratio: 1:10 – 1:640.
2. Anti-Mouse Neuropilin-1 capture antibody: Rat anti-mouse Neuropilin-1 monoclonal antibody (50% Glycerol/PBS): 60 μL × 1 vial. Dilution ratio: 1:200.
3. Anti- Mouse Neuropilin-1 detection antibody: Biotin conjugated rat anti-Mouse Neuropilin-1 monoclonal antibody: 110 μL × 1 vial. Dilution ratio: 1:101.
4. Streptavidin conj. peroxidase: Streptavidin conjugated peroxidase (SA-HRP), 110 μL × 1 vial. Dilution ratio: 1:101.
5. Microwell strips: Non coated microwell strips, 8-well × 12 strips.
6. Coating Buffer: Carbonate buffer solution (ready-to-use), 12 mL × 1 bottle.
7. Blocking Agent: Contains BSA and sucrose (ready-to-use), 24 mL × 1 bottle.
8. Sample Diluent: Buffer mostly for diluting samples (ready-to-use). Contains BSA, Tween 20 and HAMA-Blocker, 50 mL × 1 bottle.
9. Wash Concentrate: Buffer for washing microwells (20X) Contains Tween 20, 50 mL × 1 bottle.
10. SA-HRP Diluent: Buffer mostly for diluting SA-HRP (ready-to-use) Contains BSA, 15 mL × 1 bottle.
11. Substrate Solution: TMB/H₂O₂ solution (ready-to-use), 20 mL × 1 bottle.
12. Stop Solution: 0.25 mol/L sulfuric acid (ready-to-use), 20 mL × 1 bottle.
Note:
1. Reconstitute "Standard" by dissolving lyophilized Mouse Neuropilin-1 with distilled water. The volume of distilled water is specific for each lot, and it is indicated in the label on the tube of "Mouse Neuropilin-1 standard. To avoid repeated freezing and thawing, prepare aliquots.
2. Kit components must be brought to room temperature (20-30°C) prior to use.

Storage

The Mouse Neuropilin-1 standard, Anti-Mouse Neuropilin-1 capture antibody, Anti- Mouse Neuropilin-1 detection antibody, Streptavidin conj. peroxidase, must be stored at -20 ~ -30°C, other components stored at 2-8°C. All reagents are stable for 12 months after shipment.

Citations

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Axon-Seq Decodes the Motor Axon Transcriptome and Its Modulation in Response to ALS

STEM CELL REPORTS

Authors: Nijssen, Jik; Aguila, Julio; Hoogstraaten, Rein; Kee, Nigel; Hedlund, Eva

Abstract

Spinal motor axons traverse large distances to innervate target muscles, thus requiring local control of cellular events for proper functioning. To interrogate axon-specific processes we developed Axon-seq, a refined method incorporating microfluidics, RNA sequencing (RNA-seq), and bioinformatic quality control. We show that the axonal transcriptome is distinct from that of somas and contains fewer genes. We identified 3,500-5,000 transcripts in mouse and human stem cell-derived spinal motor axons, most of which are required for oxidative energy production and ribogenesis. Axons contained transcription factor mRNAs, e.g., Ybx1, with implications for local functions. As motor axons degenerate in amyotrophic lateral sclerosis (ALS), we investigated their response to the SOD1(G93A) mutation, identifying 121 ALS-dysregulated transcripts. Several of these are implicated in axonal function, including Nrp1, Dbn1, and Nek1, a known ALS-causing gene. In conclusion, Axon-seq provides an improved method for RNA-seq of axons, increasing our understanding of peripheral axon biology and identifying therapeutic targets in motor neuron disease.

Ablation of Neuropilin 1 in Myeloid Cells Exacerbates High-Fat Diet-Induced Insulin Resistance Through Nlrp3 Inflammasome In Vivo

DIABETES

Authors: Dai, Xiaoyan; Okon, Imoh; Liu, Zhaoyu; Bedarida, Tatiana; Wang, Qilong; Ramprasath, Tharmarajan; Zhang, Miao; Song, Ping; Zou, Ming-Hui

Abstract

Neuropilin 1 (Nrp1), a coreceptor for class 3 semaphorins and growth factors, is highly expressed in vascular cells and myeloid cells, including macrophages. Unlike well-characterized proangiogenic functions of endothelial cell Nrp1, the contributions of macrophage Nrp1 within the context of metabolic dysfunction remain to be established. The aim of this study was to determine the contributions of macrophage Nrp1 in high-fat diet (HFD)-instigated insulin resistance in vivo. Insulin sensitivity and Nlrp3 inflammasome activation were monitored in wild-type (WT) and myeloid cell-specific Nrp1 knockout (Nrp1(myel-KO)) mice fed an HFD (60% kcal) for 16 weeks. HFD-fed mice exhibited insulin resistance with reduced levels of Nrp1 in macrophages compared with chow-fed mice. Further, HFD-fed Nrp1(myel-KO) mice displayed accentuated insulin resistance, enhanced systemic inflammation, and dramatically increased Nlrp3 inflammasome priming and activation. Importantly, knockout of Nlrp3 ablated HFD-induced insulin resistance and inflammation in Nrp1myel-KO mice, indicating that Nrp1 reduction in macrophages instigates insulin resistance by increasing macrophage Nlrp3 inflammasome activation. Mechanistically, Nrp1 deletion activates the nuclear factor-kappa B pathway, which in turn accentuates the priming of Nlrp3, promotes Nlrp3-ASC inflammasome assembly, and results in the activation of Nlrp3. We conclude that the HFD-instigated Nrp1 reduction in macrophages exacerbates insulin resistance by promoting Nlrp3 inflammasome priming and activation.