Recombinant-Saccharomyces-cere
visiae-Putative-uncharacterized-protein-YDR183C-A-YDR183C-APutative uncharacterized protein YDR183C-A- ￥9534
- CUSABIO
- CN
- CSB-CF313632SVG
- 2025年07月06日
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- 详细信息
- 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 YDR183C-A 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 YDR183C-AEditorial/Sponsord
EditorialUniprot ID
P0C5M3Gene Names
YDR183C-AOrganism
Saccharomyces cerevisiaeAASequence
MKNHPRKVKFRVSSAKFICIYWFFCLYYKDGPILYTIYTTFLSHRYSYSTFIILRNTVAF LSFMYKHYYTHISYLTFYKSPKTFYExpression Region
1-85aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1362Purity
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
Heterologous SERCA1a Ca2+ -ATPase (sarco-endoplasmic reticulum Ca2+ -adenosine triphosphatase isoform 1a) from rabbit was expressed in yeast Saccharomyces cerevisiae as a fusion protein, with a biotin acceptor domain (BAD) linked to the SERCA
Recombinant Yeast mtDNA Helicases Purification and Functional Assays
At least two DNA helicases are important for maintenance of the yeast Saccharomyces cerevisiae mitochondrial DNA (mtDNA). Pif1 protein is a 5′->3′ DNA helicase that affects the stability of mtDNA at higher temperatures but is not essential
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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