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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 Caenorhabditis elegans vha-17 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)
V-type proton ATPase subunit e; V-ATPase subunit e Alternative name(s): Vacuolar proton pump subunit eEditorial/Sponsord
EditorialUniprot ID
Q20591Gene Names
vha-17Organism
Caenorhabditis elegansAASequence
MGILIPLVSVSAFWAIIGFGGPWIVPKGPNRGIIQLMIIMTAVCCWMFWIMVFLHQLNPL IGPQINVKTIRWISEKWGDAPNVINNExpression Region
1-86aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1364Purity
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
Application of Amide Proton Exchange Mass Spectrometry for the Study of Protein‐Protein Interactions
buffer (e.g., 25 mM Tris·Cl, 25 mM NaCl, 50 mM Na/KHPO 4 ) Purified receptor and ligand proteins 0.1% and 2.0% (v/v
Single-Molecule Observation of Rotation of F1-ATPase Through Microbeads
, and is thus called F1 -ATPase. Rotation of a shaft domain in F0 F1 -ATP synthase has been hypothesized by Paul Boyer, and ultimately was confirmed by direct observation as rotation of the γ-subunit in an isolated α3 β3 γ subcomplex. Unitary turnover of ATP induces 120�
Strategies to Optimize Protein Expression in E. coli
Collinsracie, L.A., McColgan, J.M., Grant, K.L., Diblasio‐Smith, E.A., McCoy, J.M., and Lavallie, E.R. 1995. Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner Dsba
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