PANX2 Membrane Protein Introduction

Introduction of PANX2

Pannexin 2 (PANX2), encoded by the PANX2 gene in humans, is a member of pannexin family. PANX2 is a membrane protein with 4 transmembrane domains and a cytoplasmic N and C termini. PANX2 can be detected in the eye, thyroid, prostate, kidney, liver, spinal cord and brain, including cortex, striatum, olfactory bulb, hippocampus, thalamus, and cerebellum. PANX2 gene is mapped to chromosome 22q13. There are multiple transcript variants encoding different isoforms have been found for this gene.

Basic Information of PANX2
Protein Name Pannexin-2
Gene Name PANX2
Aliases None
Organism Homo sapiens (Human)
UniProt ID Q96RD6
Transmembrane Times 4
Length (aa) 677

Function of PANX2 Membrane Protein

As the structural component of gap junctions, PANX2 can combine with PANX1 or by itself to form cell type-specific gap junctions with distinct properties. PANX2 is capable of forming large pore channels that allow the passage of ions and macromolecules involved in paracrine and autocrine signaling. By interacting with PANX1, PANX2 can form heteromeric channels with reduced channel properties compared to homomeric ones. Recent studies show that N-glycosylation is necessary for proper processing of PANX2 at the endoplasmic reticulum, regulating its intracellular distribution, but it is not required for interacting with PANX1. PANX2 is identified as a novel target gene of miR-423-3p, and the knockdown of PANX2 attenuates the effects of miR-423-3p inhibition on glioma cell proliferation and apoptosis. So, up-regulation of PANX2 may be a potential approach to inhibit glioma growth by targeting miR-423-3p.

Asn86 is the N-glycosylation site of PANX2. Fig.1 Asn86 is the N-glycosylation site of PANX2. (Sanchez-Pupo, 2018)

Application of PANX2 Membrane Protein in Literature

  1. Xu J., et al. MicroRNA-423-3p promotes glioma growth by targeting PANX2. Oncol Lett. 2018, 16: 179-188. PubMed ID: 29928399

    In this article, the authors reveal that targeting miR-423-3p may inhibit glioma growth via the upregulation of PANX2.

  2. Sanchez-Pupo R.E., et al. N-Glycosylation Regulates Pannexin 2 Localization but Is Not Required for Interacting with Pannexin 1. Int J Mol Sci. 2018, 19. PubMed ID: 29932112

    This article indicates that N-glycosylation is important for folding and trafficking of Panx2, and the un-glycosylated Panx2 can readily interact with Panx1 to regulate their localization and potentially their channel function in cells.

  3. Berchtold L.A., et al. Pannexin-2-deficiency sensitizes pancreatic beta-cells to cytokine-induced apoptosis in vitro and impairs glucose tolerance in vivo. Mol Cell Endocrinol. 2017, 448: 108-121. PubMed ID: 28390953

    This article suggests that Panx2 is an important regulator of the insulin secretory capacity and apoptosis in pancreatic β-cells.

  4. Diezmos E.F., et al. Pannexin-2 is expressed in the human colon with extensive localization in the enteric nervous system. Neurogastroenterol Motil. 2015, 27: 672-683. PubMed ID: 25773474

    This article reveals the dense expression of Panx2 in the enteric nervous system and the co-localization of Panx2 with a spectrum of neuronal markers, indicating that Panx2 may be involved in mediating neurotransmission in the colon.

  5. Le Vasseur M., et al. Pannexin 2 protein expression is not restricted to the CNS. Front Cell Neurosci. 2014, 8: 392. PubMed ID: 25505382

    This report demonstrates that the endogenous expression of Panx2 protein is not restricted to the CNS and can also be expressed in other tissues such as skin, kidney, and liver through real-time qPCR, Western blotting and immunofluorescence test.

PANX2 Preparation Options

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Creative Biolabs provides high-quality membrane protein preparation service to facilitate the development of worldwide customer’s research. During the past years, we have successfully established a powerful Magic™ membrane protein platform which enables us to provide a series of membrane protein preparation services. For more detailed information, please feel free to contact us.


  1. Sanchez-Pupo R E, et al. (2018). N-Glycosylation Regulates Pannexin 2 Localization but Is Not Required for Interacting with Pannexin 1. Int J Mol Sci. 19.

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