Recombinant-Saccharomyces-cere
visiae-Putative-uncharacterized-protein-YLR379W-YLR379WPutative uncharacterized protein YLR379W- ￥9884
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- CN
- CSB-CF517546SVG
- 2025年07月11日
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- 文献和实验
- 技术资料
- 保存条件：
"-20°C/-80°C"
- 保质期：
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
- 英文名：
Customized Saccharomyces cerevisiae YLR379W Protein (in vitro E.coli)
- 库存：
200
- 供应商：
武汉华美生物工程有限公司
- 规格：
20ug
Alternative Name(s)
Putative uncharacterized protein YLR379WEditorial/Sponsord
EditorialUniprot ID
O13579Gene Names
YLR379WOrganism
Saccharomyces cerevisiaeAASequence
MMGETPNSSKVPRLEASMARSQYRGSEVSLDTIPYSGIWPRIKKISRETPVQISFWLYGT FLSGAITSGRKDSNGLNKSRTRLEDIFKVKREPVSVFLLATIFNYVFFFCFHQLNLVVNG VRLNExpression Region
1-124aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1412Purity
Greater than 85% as determined by SDS-PAGE.Storage Buffer
Tris/PBS-based buffer, 6% TrehaloseStorage
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.Endotoxin
Not Test. Endotoxin removal service is available for free upon you request.产品类型
Transmembrane-Protein备注
**产品信息可能有变动，请以官网信息为准
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文献和实验**产品信息可能有变动，请以官网信息为准
Detection of Protein‐Protein Interactions by Coprecipitation
. Wang, Y., Chen, W., Simpson, D.M., and Elion, E.A. 2005. Cdc24 regulates nuclear shuttling and recruitment of the Ste5 scaffold to a heterotrimeric G protein in Saccharomyces cerevisiae. J. Biol. Chem. 280:1304‐13096
浅析染色质免疫沉淀（ChIP）技术在 DNA 与蛋白质相互作用研究中的重要性
immunity and fatty acid-induced insulin resistance. J Clin Invest, 2006. 116(11): p. 3015-25. [17] Tsukuda, T., et al., Chromatin remodelling at a DNA double-strand break site in Saccharomyces cerevisiae. Nature, 2005. 438(7066): p. 379-83. [18] Bernstein
Secondary structure of prion mRNA
as the origin of the transformation of PrP C into PrP Sc is an attractive model (for review see Prusiner, 1994). It might be that putative structural elements in the PrP mRNA influence the kinetics of sequential folding of the protein during translation
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