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- 2025年07月13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 Human RPRML 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)
Reprimo-like proteinEditorial/Sponsord
EditorialUniprot ID
Q8N4K4Gene Names
RPRMLOrganism
HumanAASequence
MNATFLNHSGLEEVDGVGGGAGAALGNRTHGLGTWLGCCPGGAPLAASDGVPAGLAPDER SLWVSRVAQIAVLCVLSLTVVFGVFFLGCNLLIKSESMINFLVQERRPSKDVGAAILGLYExpression Region
1-120aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1406Purity
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
Methods for Producing Recombinant Human Cellular Retinaldehyde-Binding Protein
The cellular retinaldehyde-binding protein (CRALBP) is expressed at high levels in vertebrate visual trssue, where it may serve to modulate the interaction of 11-cis -retinol with visual-cycle enzymes in the retinal pigment epithelium (RPE
Medium-Throughput Production of Recombinant Human Proteins: Protein Production in E. coli
In Chapter 4 we described the SGC process for generating multiple constructs of truncated versions of each protein using LIC. In this chapter we provide a step-by-step procedure of our E . coli system for test expressing intracellular
Medium-Throughput Production of Recombinant Human Proteins: Protein Production in Insect Cells
and a screening process established in 2007 as a measure to tackle the more challenging kinase, RNA–DNA processing and integral membrane protein families on our target list. Here, we discuss our platform for identifying soluble proteins from 3 ml of insect cell
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