Search results for: miRNASelect™ pEP-hsa-let-7c Expression Vector
#38647896 
2022/11/17
To Up
Expression, characterization, and application potentiality evaluation of recombinant human-like collagen in Pichia pastoris.
CLingling Ma, Xiaolin Liang, Shiqin Yu, Jingwen Zhou
1449 related Products with: Expression, characterization, and application potentiality evaluation of recombinant human-like collagen in Pichia pastoris.
10.00 ug 100ul2 100ug Lyophilized20 10 2 10 10 mg1mg2 10
Related Pathways
-
No related Items
#38647895 2023/01/21
To Up
Expression of recombinant human Apolipoprotein A-I in Nicotiana tabacum.
Apolipoprotein A-I (Apo A-I) is a natural mutant of Apolipoprotein. It is currently the only protein that can clear arterial wall thrombus deposits and promptly alleviate acute myocardial ischemia. Apo A-I is considered as the most promising therapeutic protein for treating atherosclerotic diseases without obvious toxic or side effects. However, the current biopharmaceutical platforms are not efficient for developing Apo A-I. The objectives of this research were to express Apo A-I using the genetic transformation ability of N. tabacum. The method is to clone the coding sequence of Apo A-I into the plant binary expression vector pCHF3 with a Flag/His6/GFP tag. The constructed plasmid was transformed into N. tabacum by a modified agrobacterium-mediated method, and transformants were selected under antibiotic stress. PCR, RT-qPCR, western blot and co-localization analysis was used to further verify the resistant N. tabacum. The stable expression and transient expression of N. tabacum were established, and the pure product of Apo A-I was obtained through protein A/G agarose. The results showed that Apo A-I was expressed in N. tabacum with a yield of 0.05 mg/g leaf weight and the purity was 90.58% ± 1.65. The obtained Apo A-I protein was subjected to amino acid sequencing. Compared with the theoretical sequence of Apo A-I, the amino acid coverage was 86%, it is also found that Cysteine replaces Arginine at position 173, which indicates that Apo A-I, a mutant of Apo A-I, is accurately expressed in N. tabacum. The purified Apo A-I protein had a lipid binding activity. The established genetic modification N. tabacum will provide a cost-effective system for the production of Apo A-I. Regarding the rapid propagation of N. tabacum, this system provides the possibility of large-scale production and accelerated clinical translation of Apo A-I.Wei Zhao, Lu-Yang Zhou, Jing Kong, Ze-Hao Huang, Ya-Di Gao, Zhong-Xia Zhang, Yong-Jie Zhou, Ruo-Yu Wu, Hong-Jun Xu, Sheng-Jun An
2722 related Products with: Expression of recombinant human Apolipoprotein A-I in Nicotiana tabacum.
10 10 25 mg5 2 2 10 25 10 50 100 mg100
Related Pathways
#38647454 2024/04/22
To Up
A robust high-throughput functional screening assay for plant pathogen effectors using the TMV-GFP vector.
UPeng Cao, Haotian Shi, Shuangxi Zhang, Jialan Chen, Rongbo Wang, Peiqing Liu, Yingfang Zhu, Yuyan An, Meixiang Zhang
2838 related Products with: A robust high-throughput functional screening assay for plant pathogen effectors using the TMV-GFP vector.
400Tests100 assays4 Sample Kit100 tests1 kit(96 Wells)100 assays100 assays1 kit(96 Wells)100 assays40 assays
Related Pathways
-
No related Items
#38646789 2024/04/22
To Up
Sodium-glucose co-transporter 1 promotes the bio-functions of perivascular preadipocytes mediated by Akt/mTOR/p70S6K signaling pathway.
TZhiquan Liu, Jiayu Wang, Peiqing Tian, Yixuan Liu, Liyun Xing, Caihua Fu, Xianwei Huang, Ping Liu
1198 related Products with: Sodium-glucose co-transporter 1 promotes the bio-functions of perivascular preadipocytes mediated by Akt/mTOR/p70S6K signaling pathway.
100ug100ug100ug 100 G2.5 mg100 ml100 MG100ug2 Pieces/Box100ug1 mg100 ml
Related Pathways
-
No related Items
#38646644 2024/03/25
To Up