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Learn16039-1-AP
antibody from Proteintech Group
Targeting: TUSC3
MagT2, MGC13453, MRT22, MRT7, N33, OST3A, SLC58A2
Western blotAntibody data
- Antibody Data
- Antigen structure
- References [10]
- Comments [0]
- Validations [0]
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- Product number
- 16039-1-AP - Provider product page
- Provider
- Proteintech Group
- Product name
- TUSC3 antibody
- Antibody type
- Polyclonal
- Description
- KD/KO validated TUSC3 antibody (Cat. #16039-1-AP) is a rabbit polyclonal antibody that shows reactivity with human, mouse, rat and has been validated for the following applications: WB, ELISA.
- Reactivity
- Human, Mouse, Rat
- Host
- Rabbit
- Conjugate
- Unconjugated
- Isotype
- IgG
- Vial size
- 20ul, 150ul
Submitted references Integrated bioinformatics analysis of differences between EAC and ESCC.
TUSC3 regulates ERMA-mediated Mg(2+) uptake for synaptic function and neurodevelopment.
Systematic profiling of mitochondria-related transcriptome in tumorigenesis, prognosis, and tumor immune microenvironment of intrahepatic cholangiocarcinoma: a multi-center cohort study.
Epigenetic activation of the TUSC3 gene as a potential therapy for XMEN disease.
ER entry pathway and glycosylation of GPI-anchored proteins are determined by N-terminal signal sequence and C-terminal GPI-attachment sequence.
Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma progression through LIPC/AKT axis.
Mutations in MAGT1 lead to a glycosylation disorder with a variable phenotype.
miRNA-mediated TUSC3 deficiency enhances UPR and ERAD to promote metastatic potential of NSCLC.
Mammalian cells lacking either the cotranslational or posttranslocational oligosaccharyltransferase complex display substrate-dependent defects in asparagine linked glycosylation.
Oxidoreductase activity is necessary for N-glycosylation of cysteine-proximal acceptor sites in glycoproteins.
Lyu Q, Chai Y, Chen W, Chen Y, Li Y
BMC cancer 2025 Oct 29;25(1):1668
BMC cancer 2025 Oct 29;25(1):1668
TUSC3 regulates ERMA-mediated Mg(2+) uptake for synaptic function and neurodevelopment.
Park G, Kim N, Kim SY, Lee H, Li CM, Seol JH, Choi SY, Jung YK
Nature communications 2025 Nov 7;16(1):9752
Nature communications 2025 Nov 7;16(1):9752
Systematic profiling of mitochondria-related transcriptome in tumorigenesis, prognosis, and tumor immune microenvironment of intrahepatic cholangiocarcinoma: a multi-center cohort study.
Chen B, Lu M, Chen Q, Zou E, Bo Z, Li J, Zhao R, Zhao J, Yu Z, Chen G, Wu L
Frontiers in genetics 2024;15:1430885
Frontiers in genetics 2024;15:1430885
Epigenetic activation of the TUSC3 gene as a potential therapy for XMEN disease.
Ding H, Li Y, Fang M, Chen J, Liu L, Lu Z, Hou J, Luo M
The Journal of allergy and clinical immunology 2023 Jun;151(6):1622-1633.e10
The Journal of allergy and clinical immunology 2023 Jun;151(6):1622-1633.e10
ER entry pathway and glycosylation of GPI-anchored proteins are determined by N-terminal signal sequence and C-terminal GPI-attachment sequence.
Hirata T, Yang J, Tomida S, Tokoro Y, Kinoshita T, Fujita M, Kizuka Y
The Journal of biological chemistry 2022 Oct;298(10):102444
The Journal of biological chemistry 2022 Oct;298(10):102444
Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma progression through LIPC/AKT axis.
Deng R, Lu X, Hong C, Cai R, Wang P, Xiong L, Wang X, Chen Q, Lin J
Journal of translational medicine 2022 Oct 23;20(1):485
Journal of translational medicine 2022 Oct 23;20(1):485
Mutations in MAGT1 lead to a glycosylation disorder with a variable phenotype.
Blommaert E, Péanne R, Cherepanova NA, Rymen D, Staels F, Jaeken J, Race V, Keldermans L, Souche E, Corveleyn A, Sparkes R, Bhattacharya K, Devalck C, Schrijvers R, Foulquier F, Gilmore R, Matthijs G
Proceedings of the National Academy of Sciences of the United States of America 2019 May 14;116(20):9865-9870
Proceedings of the National Academy of Sciences of the United States of America 2019 May 14;116(20):9865-9870
miRNA-mediated TUSC3 deficiency enhances UPR and ERAD to promote metastatic potential of NSCLC.
Jeon YJ, Kim T, Park D, Nuovo GJ, Rhee S, Joshi P, Lee BK, Jeong J, Suh SS, Grotzke JE, Kim SH, Song J, Sim H, Kim Y, Peng Y, Jeong Y, Garofalo M, Zanesi N, Kim J, Liang G, Nakano I, Cresswell P, Nana-Sinkam P, Cui R, Croce CM
Nature communications 2018 Nov 30;9(1):5110
Nature communications 2018 Nov 30;9(1):5110
Mammalian cells lacking either the cotranslational or posttranslocational oligosaccharyltransferase complex display substrate-dependent defects in asparagine linked glycosylation.
Cherepanova NA, Gilmore R
Scientific reports 2016 Feb 11;6:20946
Scientific reports 2016 Feb 11;6:20946
Oxidoreductase activity is necessary for N-glycosylation of cysteine-proximal acceptor sites in glycoproteins.
Cherepanova NA, Shrimal S, Gilmore R
The Journal of cell biology 2014 Aug 18;206(4):525-39
The Journal of cell biology 2014 Aug 18;206(4):525-39
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