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| Size | List Price | Price | Cart |
|---|---|---|---|
| 150 ul | $348.00 | Add to Cart | |
| 50 ul | $155.00 | Add to Cart |
P2X2 is a subunit in the family of ion channels activated by extracellular ATP. It was cloned from PC12 cells. P2X2 has two putative transmembrane domains with intracellular N- and C-termini. It can form homomeric channels and heteromeric channels with other members of the family. P2X2 is expressed in brain, spinal cord, sensory and autonomic ganglia as well as in neuroendocrine cells. Product Highlights: |
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- Product Publications
Product Publications
- Hiroki Saito, Takuya Yokoyama, Nobuaki Nakamuta, and Yoshio Yamamoto. (2024). Immunohistochemical Distribution of Cannabinoid Receptor Type 1 (CB1) and Type 2 (CB2) in the Rat Carotid Body. Acta Histochemica, 126(8), 152205. doi: 10.1016/j.acthis.2024.152205
- Kentaro Nishida, Yuka Nomura, Kanako Kawamori, Akihiro Ohishi, Kazuki Nagasawa. ATP metabolizing enzymes ENPP1, 2 and 3 are localized in sensory neurons of rat dorsal root ganglion. European Journal of Histochemistry 2018; volume 62:2877. doi:10.4081/ejh.2018.2877
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Images
P2x2 staining of Cerebellar Purjinke cell layer. ~50 μm sections from 3 brains from P15 rats. http://stke.sciencemag.org/cgi/data/sigtrans;1/41/ra8/DC1/1
P2x2 staining of Cerebellar Purjinke cell layer. ~50 μm sections from 3 brains from P15 rats. http://stke.sciencemag.org/cgi/data/sigtrans;1/41/ra8/DC1/1
The constitutive interaction between P2X2 receptors and VILIP1 is calcium independent. www.sciencesignaling.org/cgi/content/full/1/41/ra8/DC1
The constitutive interaction between P2X2 receptors and VILIP1 is calcium independent. www.sciencesignaling.org/cgi/content/full/1/41/ra8/DC1