This TECPR2 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.
TECPR2 is a large multi-domain protein that plays a crucial role in cellular processes related to autophagy and the early secretory pathway. Mutations in the TECPR2 gene are associated with autophagy defects, affecting axonal integrity and leading to progressive neurodegenerative and neuromuscular diseases such as hereditary spastic paraplegia (HSP) [1]. TECPR2 has been found to cooperate with LC3C in regulating COPII-dependent ER export [2]. Additionally, TECPR2 has been linked to neuroaxonal dystrophy in Spanish Water Dogs [3].
TECPR2 is involved in stabilizing SEC24D protein levels, maintaining functional ER exit sites (ERES), and facilitating efficient ER export by binding to lipidated LC3C [4]. This interaction with LC3C is essential for its function as a positive regulator of COPII-dependent ER export [5]. Furthermore, TECPR2 is implicated in neurodegenerative diseases, as it is a human ATG8-binding protein and a positive regulator of autophagy, which is crucial for maintaining cellular homeostasis and preventing neurodegeneration [6] [7]. Studies have shown that TECPR2 is part of a neurodevelopmental gene expression program that includes other genes associated with neurological diseases, highlighting its importance in neuronal function and health [8] [9].
References:
[1] P. Patwari, L. Wolfe, & E. Berry-Kravis, tecpr2 mutation–associated respiratory dysregulation: more than central apnea, Journal of Clinical Sleep Medicine, vol. 16, no. 6, p. 977-982, 2020. https://doi.org/10.5664/jcsm.8434
[2] D. Stadel, V. Millarte, K. Tillmann, J. Huber, B. Tamin-Yecheskel, M. Akutsuet al., Tecpr2 cooperates with lc3c to regulate copii-dependent er export, Molecular Cell, vol. 60, no. 1, p. 89-104, 2015. https://doi.org/10.1016/j.molcel.2015.09.010
[3] K. Hahn, C. Rohdin, V. Jagannathan, P. Wohlsein, W. Baumgärtner, F. Seehusenet al., Tecpr2 associated neuroaxonal dystrophy in spanish water dogs, Plos One, vol. 10, no. 11, p. e0141824, 2015. https://doi.org/10.1371/journal.pone.0141824
[4] D. Stadel, V. Millarte, K. Tillmann, J. Huber, B. Tamin-Yecheskel, M. Akutsuet al., Tecpr2 cooperates with lc3c to regulate copii-dependent er export, Molecular Cell, vol. 60, no. 1, p. 89-104, 2015. https://doi.org/10.1016/j.molcel.2015.09.010
[5] A. Lystad and A. Simonsen, Mechanisms and pathophysiological roles of the atg8 conjugation machinery, Cells, vol. 8, no. 9, p. 973, 2019. https://doi.org/10.3390/cells8090973
[6] H. Shimazaki, Lysosomal dysfunctions in hereditary spastic paraplegias,, 2017. https://doi.org/10.5772/intechopen.70142
[7] P. Patwari, L. Wolfe, & E. Berry-Kravis, tecpr2 mutation–associated respiratory dysregulation: more than central apnea, Journal of Clinical Sleep Medicine, vol. 16, no. 6, p. 977-982, 2020. https://doi.org/10.5664/jcsm.8434
[8] I. Shalev, J. Somekh, & A. Eran, Integrative functional analyses of the neurodegenerative disease-associated tecpr2 gene reveal its diverse roles,, 2020. https://doi.org/10.21203/rs.2.22274/v1
[9] I. Shalev, J. Somekh, & A. Eran, Multimodal bioinformatic analyses of the neurodegenerative disease-associated tecpr2 gene reveal its diverse roles, Journal of Medical Genetics, vol. 59, no. 10, p. 1002-1009, 2021. https://doi.org/10.1136/jmedgenet-2021-108193
