ATP1B2 Membrane Protein Introduction

Introduction of ATP1B2

ATP1B2 is encoded by ATP1B2 gene, and it belongs to the family of Na⁺/K⁺ and H⁺/K⁺ ATPases beta chain proteins, which is the subfamily of Na⁺/K⁺-ATPases. ATP1B2 gene is located on human chromosome 17p13.1 and there are two transcript variants encoding different isoforms have been found. The beta subunit of Na⁺/K⁺ -ATPases can be encoded by many genes, ATP1B2 gene encodes a beta 2 subunit. ATP1B2 is predominantly expressed in brain and ovary, with a preferential binding to ATP1A2, which is mainly found in astrocytes after completion of development.

Function of ATP1B2 Membrane Protein

As a smaller glycoprotein subunit (beta) of the active Na⁺/K⁺ -ATPase, ATP1B2 may participant in the ATP hydrolysis along with the exchange of Na⁺ and K⁺ ions across the cytomembrane. Na⁺ and K⁺ ions gradients are essential to maintain membrane potential and drive the transport of other solutes Na⁺/K⁺-ATPase, which is necessary for osmoregulation, electrical excitability of nerve and muscle, and for sodium-coupled transport of various organic and inorganic molecules. In astrocytes, ATP1B2 mainly binds with ATP1A2 to restore extracellular K⁺ homeostasis following neuronal depolarization. It is documented that ATP1B2 is stably expressed in multiple models of CNS injury. In addition, ATP1B2 is associated with various diseases, including Juvenile Retinoschisis and Thyrotoxic Periodic Paralysis. Fig.1 shows a predicted structure of ATP1B2 from ModBase.

Fig.1 Predicted structure of ATP1B2 structure in ModBase. (Pieper, 2014)

Application of ATP1B2 Membrane Protein in Literature

1. Wang Z., et al. Novel SNPs in the ATP1B2 gene and their associations with milk yield, milk composition and heat-resistance traits in Chinese Holstein cows. Mol Biol Rep. 2011, 38(3): 1749-55. PubMed ID: 20842439
   
   

   This article suggests that the ATP1B2 mutated C2833T in Chinese Holstein cows is a genetic marker of heat-resistance traits. Cows with the TT genotype of ATP1B2 show the desirable characteristics of low red blood cell K(⁺) and rectal temperature, low red blood cell NKA activity and low decline rate in milk yield.

2. Mauri N., et al. A SINE Insertion in ATP1B2 in Belgian Shepherd Dogs Affected by Spongy Degeneration with Cerebellar Ataxia (SDCA2). G3 (Bethesda). 2017, 7(8): 2729-2737. PubMed ID: 28620085
   
   

   This article identified a SINE insertion in exon 2 of the gene ATP1B2, leading to different splicing and blocked protein expression of ATP1B2 in the CNS. Additionally, it suggests that ATP1B2 represents a candidate gene for human inherited cerebellar ataxias. On the other hand, SDCA2-affected Malinois puppies may serve as a natively occurring animal model for this ataxias.

3. Batiuk M.Y., et al. An immunoaffinity-based method for isolating ultrapure adult astrocytes based on ATP1B2 targeting by the ACSA-2 antibody. J Biol Chem. 2017, 292(21): 8874-8891. PubMed ID: 28373281
   
   

   This article shows that the expression of ATP1B2 is stable in multiple models of CNS injury and disease, and ATP1B2 can act as an astrocyte marker with widespread distribution in the brain throughout the entire development.

4. Friedrich U., et al. The Na/K-ATPase is obligatory for membrane anchorage of retinoschisin, the protein involved in the pathogenesis of X-linked juvenile retinoschisis. Hum Mol Genet. 2011, 20(6): 1132-42. PubMed ID: 21196491
   
   

   This article demonstrates that co-expression of ATP1B2 and ATP1A3 is necessary for retinoschisin binding to intact Hek293 cells. It is also proved that changed localization of ATP1B2 and ATP1A3 is a dominant consequence of the deficiency of retinoschisin and thus may function in downstream of cellular pathology in XLRS.

5. Demircan B., et al. Comparative epigenomics of human and mouse mammary tumors. Genes Chromosomes Cancer. 2009, 48(1): 83-97. PubMed ID: 18836996
   
   

   This article observes that the human orthologs of SMPD3, FOXJ1, and ATP1B2 are obviously hypermethylated in the human disease, whereas DUSP2 is not hypermethylated in primary breast tumors.

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Reference

1. Pieper U, et al. (2014). ModBase, a database of annotated comparative protein structure models and associated resources. Nucleic Acids Res. 42: D336-46.

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