- ￥1868
- abinScience
- France
- HA650012
- 2026年03月03日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.
- 保质期：
1 year
- 英文名：
Recombinant Human TRAPPC10 Protein, N-His
- 库存：
999
- 供应商：
abinScience
- 规格：
100ug
| Product name | Recombinant Human TRAPPC10 Protein, N-His |
|---|---|
| Catalog No. | HA650012 |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| Purity | >90% as determined by SDS-PAGE. |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Endotoxin level | Please contact with the lab for this information. |
| Expression system | E. coli |
| Accession | P48553 |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Alternative Names | Trafficking protein particle complex subunit 10; Epilepsy holoprosencephaly candidate 1 protein; EHOC-1; Protein GT334; Trafficking protein particle complex subunit TMEM1; Transport protein particle subunit TMEM1; TRAPP subunit TMEM1; TRAPPC10; EHOC1; TMEM1 |
| Species | Homo sapiens (Human) |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
abinScience, founded in 2023 in Strasbourg, France, is committed to developing and producing high-quality life science reagents. Rooted in one of Europe’s leading hubs for scientific innovation, abinScience empowers global research through reliable, efficient experimental solutions. Guided by the vision of “Empowering Bioscience Discovery,” we support scientists worldwide in advancing the frontiers of bioscience.
Technology and Innovation
Relying on the global leading position in antibody and protein research and more than 20 years of industry experience of its parent company ProteoGenix since 2003...
Product categories and application fields.
Main products...
Application field: Infectious disease research, Neuroscience, Immunology, Oncology
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文献和实验• Introducing a novel TRAPPC10 gene variant as a potential cause of developmental delay and intellectual disability in an Iranian family., PMID:39560797
• TRAPPC6B biallelic variants cause a neurodevelopmental disorder with TRAPP II and trafficking disruptions., PMID:37713627
• Genetic and expressional insights into the association of TRAPPC10 variants with neurodevelopmental disorders., PMID:39891754
• Discovery of new Longin and Roadblock domains that form platforms for small GTPases in Ragulator and TRAPP-II., PMID:23511850
• Biochemical Insight into Novel Rab-GEF Activity of the Mammalian TRAPPIII Complex., PMID:34229011
• The adaptor function of TRAPPC2 in mammalian TRAPPs explains TRAPPC2-associated SEDT and TRAPPC9-associated congenital intellectual disability., PMID:21858081
• Novel candidate genes and variants underlying autosomal recessive neurodevelopmental disorders with intellectual disability., PMID:30167849
• lncRNA TMEM51-AS1 and RUSC1-AS1 function as ceRNAs for induction of laryngeal squamous cell carcinoma and prediction of prognosis., PMID:31565549
• Multi-omics approaches identify SF3B3 and SIRT3 as candidate autophagic regulators and druggable targets in invasive breast carcinoma., PMID:34094830
High Throughput Production of Recombinant Human Proteins for Crystallography
This chapter presents in detail the process used in high throughput bacterial production of recombinant human proteins for crystal structure determination. The core principles are: (1 ) Generating at least 10 truncated constructs
The Use of TAGZyme for the Efficient Removal of N-Terminal His-Tags
The use of affinity tags and especially histidine tags (His-tags) has become widespread in molecular biology for the efficient purification of recombinant proteins. In some cases, the presence of the affinity tag in the recombinant protein
Recombinant antigens for immunodiagnosis of cystic echinococcosis
) and with sera from mice infected with E. granulosus oncospheres. The cDNAs were subcloned into a pET vector, expressed as fusion proteins tagged with GST and affinity purified against the GST tag. Of the three recombinant proteins, EpC1 achieved the highest
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