R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Neuropilin-2 (D39A5) XP® Rabbit mAb #3366
Filter:
- WB
- IP
- IHC
- IF
Supporting Data
| REACTIVITY | M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 130 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| Immunohistochemistry (Paraffin) | 1:200 - 1:800 |
| Immunofluorescence (Frozen) | 1:500 - 1:2000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Neuropilin-2 (D39A5) XP® Rabbit mAb detects endogenous levels of total neuropilin-2 protein.
Species Reactivity:
Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of mouse Neuropilin-2 protein.
Background
Class 3 secreted semaphorin (Sema3A) is a chemorepellent that acts upon a wide variety of axons. As such, it induces a dramatic redistribution and depolymerization of actin filaments that results in growth cone collapse. Plexins are single-pass, transmembrane signaling proteins encompassing Plexin A1, A2, A3, and A4. Plexins form a complex with neuropilin-1 and -2 and the cell adhesion protein L1 to form a functional semaphorin receptor (1,2). The GTPase Rnd1 binds to the cytoplasmic domain of Plexin A1 to trigger cytoskeletal collapse. In contrast, the GTPase RhoD blocks Rnd1-mediated Plexin A1 activation and repulsion of sympathetic axons by Sema3A (3).
Neuropilin-2, a single-pass, transmembrane glycoprotein, can also bind to VEGF165 and VEGF145, but not VEGF121. Thus, in addition to neuronal guidance, neuropilin-2 plays a role in angiogenesis and cardiovascular functions (4). Although neuropilin-2 has been linked to tumor biology (e.g. pancreatic cancer, bladder cancer, lung cancer, and neuroblastoma), its role in tumor pathogenesis is still under investigation (4,5).
Neuropilin-2, a single-pass, transmembrane glycoprotein, can also bind to VEGF165 and VEGF145, but not VEGF121. Thus, in addition to neuronal guidance, neuropilin-2 plays a role in angiogenesis and cardiovascular functions (4). Although neuropilin-2 has been linked to tumor biology (e.g. pancreatic cancer, bladder cancer, lung cancer, and neuroblastoma), its role in tumor pathogenesis is still under investigation (4,5).
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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