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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 Xenopus tropicalis spcs2 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)
Probable signal peptidase complex subunit 2 EC= 3.4.-.- Alternative name(s): Microsomal signal peptidase 25 kDa subunit; SPase 25 kDa subunitEditorial/Sponsord
EditorialUniprot ID
Q5M8Y1Gene Names
spcs2Organism
Xenopus tropicalisAASequence
MAARGGKNGLLEKWKIDDKPVKIDKWDGSAVKNSLDDAAKKVLLEKYRYVENFCLIDGRL IICTISCVFAIVALVWDYLHPFPESKPVLAICVISYFLMMGILTIYTSYKEKSIFLVAHR KDPAGMDPDDIWHLSSSLKRFDDKYTLKVTYISGKTKAQRDAEFTKSIARFFDDNGTLVM DLFEPEVSKLHDSLAMEKKTKExpression Region
1-201aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1510Purity
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
【资源】全面归类网址:毕赤酵母表达各种来源蛋白(细菌,真菌,植物,人类等)
α-amylaseS, 240 mg/L ,activeMouse sonic hedgehog proteinS, α-MF, 500 mg/L, active392Mouse major urinary protein complex (MUP)S, 270 mg/L, native[165]Recombinant non-hydroxlated gelatins(based on rat and mouse collagen)S, 14.8 g/L, α-MF385Ostrich egg
complex was not known. Analysis by 2-D phosphoprotein mapping identified two distinct proteins that were greatly increased in phosphate content in reg1 mutants. Mixed-peptide sequencing identified these proteins as hexokinase II (Hxk2p) and the E1 subunit
among subunits of a multi-subunit complex. By an “ordered fragment ladder” far-Western analysis, they were able to identify the interaction domains of E. coli RNA polymerase ß subunit. The protein was expressed as a polyhistidine-tagged fusion, then partially
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