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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 Xenopus laevis tmem18 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)
Transmembrane protein 18Editorial/Sponsord
EditorialUniprot ID
Q4V7N7Gene Names
tmem18Organism
Xenopus laevisAASequence
MAEEPGVWSLLERAPIDWTEPWLIGLAAFHILCFIVTYISFKSYPLQICHFLLMVVLVSC AEYINEFAAMHWRAYSKQQYFDSSGMFISLAFSAPLLCNTIIIVVHWVYKTLCVMTELKT LQQKRKESREKRKKKEExpression Region
1-136aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1428Purity
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
Reticulocyte Lysate as a Model System to Study Endoplasmic Reticulum Membrane Protein Degradation
membranes, the RRL system faithfully carries out ER targeting, translocation, glycosylation, and membrane integration events and therefore provides a ready source of 35S-labeled protein with defined transmembrane topology. These substrates can be rapidly
Analysis of Molecular Chaperones Using a Xenopus Oocyte Protein Refolding Assay
in folding. In this chapter, we describe the production and purification of a Xenopus laevis recombinant small Hsp, Hsp30C, and an in vivo luciferase (LUC) refolding assay employing microinjected Xenopus oocytes. This assay tests whether LUC can be maintained
Sequences derived from the respiratory syncytial virus (RSV) fusion (F) protein were expressed in insect cells as recombinant glutathione-S -transferase (GST)-tagged proteins. The sequence covering the F2 subunit (GST-F2), and a truncated
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