Code | CSB-YP009911HU |
MSDS | |
Size | Pls inquire |
Source | Yeast |
Have Questions? | Leave a Message or Start an on-line Chat |
Code | CSB-EP009911HU-B |
MSDS | |
Size | Pls inquire |
Source | E.coli |
Conjugate | Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag. |
Have Questions? | Leave a Message or Start an on-line Chat |
The recombinant human Glutamate receptor ionotropic, NMDA 1 (GRIN1) 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.
GRIN1, also known as GluN1, is a vital subunit of the N-methyl-D-aspartate (NMDA) receptor, an important ionotropic glutamate receptor heavily present in the developing brain [1]. GluN1 is crucial for the NMDA receptor's function and contains the co-agonist binding site [2][3]. This subunit is found throughout the central nervous system [4]. Mutations in GRIN1 are associated with several neuropsychiatric disorders, including schizophrenia, bipolar disorder, and ADHD [5]. GRIN1 is also linked to autism spectrum disorder (ASD) because of its role in synaptic function [6]. Variations in the GRIN1 gene, such as deletions and mutations, can impair NMDA receptor function, potentially contributing to disease mechanisms [7].
References:
[1] A. Fry, K. Fawcett, N. Zelnik, H. Yuan, B. Thompson, L. Shemer-Meiriet al., De novo mutations in grin1 cause extensive bilateral polymicrogyria, Brain, vol. 141, no. 3, p. 698-712, 2018. https://doi.org/10.1093/brain/awx358
[2] G. Moreno‐González, A. López-Colomé, G. Rodrı́guez, & Á. Zarain‐Herzberg, Transcription of the chicken grin1 gene is regulated by the activity of sp3 and nrsf in undifferentiated cells and neurons, Bioscience Reports, vol. 28, no. 4, p. 177-188, 2008. https://doi.org/10.1042/bsr20080058
[3] N. Tsuchida, K. Hamada, M. Shiina, M. Kato, Y. Kobayashi, J. Tohyamaet al., grin2d variants in three cases of developmental and epileptic encephalopathy, Clinical Genetics, vol. 94, no. 6, p. 538-547, 2018. https://doi.org/10.1111/cge.13454
[4] J. Lemke, K. Geider, K. Helbig, H. Heyne, H. Schutz, J. Hentschelet al., Delineating the grin1 phenotypic spectrum, Neurology, vol. 86, no. 23, p. 2171-2178, 2016. https://doi.org/10.1212/wnl.0000000000002740
[5] J. Umemori, K. Takao, H. Koshimizu, T. Furuse, S. Wakana, & T. Miyakawa, Enu-mutagenesis mice with a non-synonymous mutation in grin1 exhibit abnormal anxiety-like behaviors, impaired fear memory, and decreased acoustic startle response, BMC Research Notes, vol. 6, no. 1, 2013. https://doi.org/10.1186/1756-0500-6-203
[6] B. Teng, V. Nikolova, N. Riddick, K. Agster, J. Crowley, L. Bakeret al., Reversal of social deficits by subchronic oxytocin in two autism mouse models, Neuropharmacology, vol. 105, p. 61-71, 2016. https://doi.org/10.1016/j.neuropharm.2015.12.025
[7] Y. Feng, Z. Cui-rong, Z. Wei, G. Li, Y. Gan, C. Liuet al., Gene variations of glutamate metabolism pathway and epilepsy, Acta Epileptologica, vol. 4, no. 1, 2022. https://doi.org/10.1186/s42494-022-00103-2
There are currently no reviews for this product.