This ALDH18A1 protein is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
ALDH18A1 encodes the bifunctional enzyme pyrroline-5-carboxylate synthetase (P5CS), which is essential for the conversion of glutamate to β-pyrroline-5-carboxylate (P5C), a key step in the de novo biosynthesis of proline and ornithine [1][2][3]. This enzyme is expressed in various tissues, contributing significantly to glutamine metabolism [3][4]. ALDH18A1 is associated with diseases such as hereditary spastic paraplegia and cutis laxa due to its role in amino acid and antioxidant metabolism [2][3]. Furthermore, ALDH18A1 influences cell growth through proline biosynthesis in melanoma and neuroblastoma [5][6][7]. Upregulation of ALDH18A1 has been observed in steatohepatitis-related hepatocellular carcinoma, suggesting its involvement in dysregulated metabolism and cancer progression [8].
References:
[1] M. Colonna, T. Moss, S. Mokashi, S. Srikanth, J. Jones, J. Foleyet al., Functional assessment of homozygous aldh18a1 variants reveals alterations in amino acid and antioxidant metabolism, Human Molecular Genetics, vol. 32, no. 5, p. 732-744, 2022. https://doi.org/10.1093/hmg/ddac226
[2] M. Coutelier, C. Goizet, A. Dürr, F. Habarou, S. Morais, A. Dionne‐Laporteet al., Alteration of ornithine metabolism leads to dominant and recessive hereditary spastic paraplegia, Brain, vol. 138, no. 8, p. 2191-2205, 2015. https://doi.org/10.1093/brain/awv143
[3] X. Tao, Y. Liang, X. Yang, J. Pang, Z. Zhong, X. Chenet al., Transcriptomic profiling in muscle and adipose tissue identifies genes related to growth and lipid deposition, Plos One, vol. 12, no. 9, p. e0184120, 2017. https://doi.org/10.1371/journal.pone.0184120
[4] S. Marchitti, C. Brocker, D. Stagos, & V. Vasiliou, Non-p450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily, Expert Opinion on Drug Metabolism & Toxicology, vol. 4, no. 6, p. 697-720, 2008. https://doi.org/10.1517/17425255.4.6.697
[5] J. Phang, Proline metabolism in cell regulation and cancer biology: recent advances and hypotheses, Antioxidants & Redox Signaling, vol. 30, no. 4, p. 635-649, 2019. https://doi.org/10.1089/ars.2017.7350
[6] Y. Ye, Y. Wu, & J. Wang, Pyrroline-5-carboxylate reductase 1 promotes cell proliferation via inhibiting apoptosis in human malignant melanoma, Cancer Management and Research, vol. Volume 10, p. 6399-6407, 2018. https://doi.org/10.2147/cmar.s166711
[7] Y. Guo, J. Duan, J. Wang, L. Lin, D. Wang, X. Liuet al., Inhibition of the aldh18a1-mycn positive feedback loop attenuates mycn-amplified neuroblastoma growth, Science Translational Medicine, vol. 12, no. 531, 2020. https://doi.org/10.1126/scitranslmed.aax8694
[8] Q. Liang, N. Teoh, L. Xu, S. Pok, X. Li, E. Chuet al., Dietary cholesterol promotes steatohepatitis related hepatocellular carcinoma through dysregulated metabolism and calcium signaling, Nature Communications, vol. 9, no. 1, 2018. https://doi.org/10.1038/s41467-018-06931-6
