- Peptide (C)RDLAGKEQRTLTK, corresponding to amino acid residues 301-313 of rat P2X4 receptor (Accession P51577). Extracellular.
Western blot analysis of rat brain membrane (lanes 1 and 5), mouse brain membrane (lanes 2 and 6), C6 rat brain glioma cell line lysate (lanes 3 and 7) and SH-SY5Y human brain neuroblastoma cell line lysate (lanes 4 and 8):1-4. Anti-P2X4 Receptor (extracellular) Antibody (#APR-024), (1:200).
5-8. Anti-P2X4 Receptor (extracellular) Antibody, preincubated with P2X4 Receptor (extracellular) Blocking Peptide (#BLP-PR024).
Expression of P2RX4 in rat pheochromocytoma cell line (PC12)Cell surface detection of P2RX4 in intact living PC12 cells. A. Extracellular staining of cells with Anti-P2X4 (extracellular) Antibody (#APR-024), (red, 1:50) followed by goat anti-rabbit-AlexaFluor-594 secondary antibody. B. Nuclear staining of cells using DAPI (blue). C. Merged images of A and B.
- Prasad, M. et al. (2001) J. Physiol. 537, 667.
- Florenzano, F. et al. (2002) Neuroscience 115, 425.
- Ashcroft, F.M. et al. (2000) Ion Channels and Disease Ed 1, p. 405, Academic Press, San Diego.
- Khakh, B.S. et al. (2001) Pharmacol. Rev. 53, 107.
- Ding, Y. et al. (2000) J. Auton. Nerv. Syst. 81, 289.
- Le, K.T. et al. (1998) J. Neurosci. 18, 7152.
- Robertson, S.J. et al. (2001) Curr. Opin. Neurobiol. 11, 378.
- Dunn, P.M. et al. (2001) Prog. Neurobiol. 65, 107.
- Kim, M. et al. (2001) EMBO J. 20, 6347.
- Inoue, K. et al. (2004) J. Pharmacol. Sci. 94, 112.
The P2X purinergic receptors belong to the ligand-gated ion channel family and are activated by extracellular ATP.
The structure and function of the P2X receptors, which were mainly investigated using in vitro models, indicate their involvement in synaptic communication, cell death, and differentiation.
Seven mammalian P2X receptor subtypes (P2X1–P2X7) have been identified and cloned.1,2,3 All P2X receptor subtypes share the same structure of intracellular N- and C-termini, two membrane-spanning domains and a large extracellular loop.
All P2X subunits can assemble to form homomeric or heteromeric functional channels with the exception of P2X6, which only appears to function as part of a heteromeric complex.4-9
The various P2X receptors show distinct expression patterns. P2X1-6 have been found in the central and peripheral nervous system, while the P2X7 receptor is predominantly found in cells of the immune system.4
The P2X2 receptor subunit has a widespread tissue distribution in autonomic neurons, but it is generally found to be co-expressed with one or more subtypes.
Overexpression of P2X4 was demonstrated in microglia and in the spinal dorsal horn following peripheral nerve injury. It has been suggested that activation of P2X4 along with p38 MAPK is essential for the development of allodynia (pain from a stimulus that doesn't normally elicit pain) following nerve injury. Inhibition of P2X4 expression in spinal microglia has been suggested as a novel therapeutic approach for the treatment of allodynia.10
Anti-P2X4 Receptor (extracellular) Antibody (#APR-024) is a highly specific antibody directed against an epitope of the rat protein. The antibody can be used in western blot and immunocytochemistry applications. Anti-P2X4 Receptor (extracellular) Antibody recognizes an extracellular epitope and is thus ideal for detecting the receptor in living cells. It has been designed to recognize P2X4 purinergic receptor from mouse, human, and rat samples.
Applications
Specifications
Scientific Background
Citations
- Mouse T-cells.
Elkhal, A. et al. (2016) Sci. Rep. 6, 1.
- Mouse brain sections.
Srivastava, P. et al. (2010) Exp. Neurol. 329, 113308.
- Mouse brain sections.
Srivastava, P. et al. (2010) Exp. Neurol. 329, 113308.
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