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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 [4]
- 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 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.
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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