SLC29A1 Membrane Protein Introduction

Introduction of SLC29A1

Equilibrative nucleoside transporter 1 (ENT1) or SLC29A1 is a protein encoded by the SLC29A1 gene in humans. This gene has been found to have multiple alternative splice variants encoding the same protein. The protein is glycosylated after translation and expressed in all tissues except skeletal muscle. The highest levels are found in the liver, heart, testes, spleen, lungs, kidneys and brain.

Basic Information of SLC29A1
Protein Name Equilibrative nucleoside transporter 1
Gene Name SLC29A1
Aliases ENT1, solute carrier family 29 member 1
Organism Homo sapiens (Human)
UniProt ID Q99808
Transmembrane Times 11
Length (aa) 456

Function of SLC29A1 Membrane Protein

SLC29A1 gene is a member of the equilibrative nucleoside transporter family. It encodes a transmembrane glycoprotein that localizes to the plasma and mitochondrial membranes and mediates the cellular uptake of nucleosides from the surrounding medium. SLC29A1 is categorized as an equilibrative (as opposed to concentrative) transporter that is sensitive to inhibition by nitrobenzylmercaptopurine ribonucleoside (NBMPR). Nucleoside transporters are required for nucleotide synthesis in cells that lack de novo nucleoside synthesis pathways and are also necessary for the uptake of cytotoxic nucleosides used for cancer and viral chemotherapies.

Structure of SLC29A1 membrane protein. Fig.1 Structure of SLC29A1 membrane protein.

Application of SLC29A1 Membrane Protein in Literature

  1. Lum P.Y., et al. Human intestinal es nucleoside transporter: molecular characterization and nucleoside inhibitory profiles. Cancer Chemother Pharmacol. 2000, 45(4)273-8. PubMed ID: 107553314

    This article suggests that the es transporter does not appear to be functionally variant in the human placenta, small intestine or erythrocytes.

  2. Sankar N., et al. Comparative genomic analysis of equilibrative nucleoside transporters suggests conserved protein structure despite limited sequence identity. Nucleic Acids Res. 2002, 30(20): 4339-50. PubMed ID: 12384580

    This article reveals predicted topologies of ENT proteins are strikingly similar, suggesting evolutionary conservation of a prototypic structure.

  3. Mangravite L.M., et al. Localization of human equilibrative nucleoside transporters, hENT1 and hENT2, in renal epithelial cells. Am J Physiol Renal Physiol. 2003, 284(5):F902-10. PubMed ID: 12527552

    This article suggests that hENT1 and hENT2 on the basolateral membrane function with concentrative nucleoside transporters on the apical membrane to mediate active reabsorption of nucleosides within the kidney.

  4. Griffiths M., et al. Cloning of a human nucleoside transporter implicated in the cellular uptake of adenosine and chemotherapeutic drugs. Nat Med. 1997, 3(1): 89-93. PubMed ID: 8986748

    Study of this protein should not only provide insights into the physiological roles of nucleoside transport but also open the way to improved therapies.

  5. Rungaldier S., et al. Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains. Biochim Biophys Acta. 2013, 1828(3), 956-66. PubMed ID: 23219802

    This article evaluates nucleoside transporter (SLC29A1) was identified as stomatin-interacting proteins. This finding is in line with the hypothesis that stomatin plays a role as membrane-bound scaffolding protein modulating transport proteins.

SLC29A1 Preparation Options

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC29A1 antibody development services.

As a forward-looking organization as well as a leading customer service provider in the field of membrane protein, Creative Biolabs has won good reputation among our worldwide customers for successfully accomplishing numerous challenging projects including generation of many functional membrane proteins. Please feel free to contact us for more information.

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