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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 Danio rerio tmem160 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 160Editorial/Sponsord
EditorialUniprot ID
B3DJK0Gene Names
tmem160Organism
Danio rerioAASequence
MASIRWLMGSRLSRFVCPFAQLVRQPVLRYVRPPVRALHRGSVRRAAEKNPLNSRARAVE QQYITELDKADALMLRKSHETGFLSWFRNGLLATGIGVIAFVQSDVGREAGYAFFILGGM CVSFGGASYVTSLLSLRRIMLLSLPAVLLHTAVVSSAALFWLCAVSLYIGRLEVEIIHDE DDEEHGADESSECAECRARRDREKGQDKExpression Region
1-208aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1518Purity
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
Carboxypeptidase Y (EC 3.4.16.1)
(no suitable chemical method exists for the sequential removal of C-terminal amino acids from a polypeptide). The protein or peptide being analyzed is digested with carboxypeptidase and aliquots removed at timed intervals, and analyzed for the presence of free
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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