Recombinant Vibrio fischeri ATP synthase subunit c (atpE), partial

中文名稱：

Recombinant Vibrio fischeri ATP synthase subunit c(atpE),partial
貨號(hào)：

CSB-YP479666VFC1
說明書：

MSDS Datasheet
規(guī)格：
來源：

Yeast
其他：

中文名稱：

Recombinant Vibrio fischeri ATP synthase subunit c(atpE),partial
貨號(hào)：

CSB-EP479666VFC1
說明書：

MSDS Datasheet
規(guī)格：
來源：

E.coli
其他：

中文名稱：

Recombinant Vibrio fischeri ATP synthase subunit c(atpE),partial
貨號(hào)：

CSB-EP479666VFC1-B
說明書：

MSDS Datasheet
規(guī)格：
來源：

E.coli
共軛：

Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
其他：

中文名稱：

Recombinant Vibrio fischeri ATP synthase subunit c(atpE),partial
貨號(hào)：

CSB-BP479666VFC1
說明書：

MSDS Datasheet
規(guī)格：
來源：

Baculovirus
其他：

中文名稱：

Recombinant Vibrio fischeri ATP synthase subunit c(atpE),partial
貨號(hào)：

CSB-MP479666VFC1
說明書：

MSDS Datasheet
規(guī)格：
來源：

Mammalian cell
其他：

產(chǎn)品詳情
產(chǎn)品評(píng)價(jià)
相關(guān)產(chǎn)品
靶點(diǎn)詳情

產(chǎn)品詳情

純度：

>85% (SDS-PAGE)
基因名：

atpE
Uniprot No.：

B5FCZ6
別名：

atpE; VFMJ11_2704; ATP synthase subunit c; ATP synthase F(0 sector subunit c; F-type ATPase subunit c; F-ATPase subunit c; Lipid-binding protein
種屬：

Vibrio fischeri (strain MJ11)
蛋白長(zhǎng)度：

Partial
蛋白標(biāo)簽：

Tag?type?will?be?determined?during?the?manufacturing?process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
產(chǎn)品提供形式：

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
復(fù)溶：

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
儲(chǔ)存條件：

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
保質(zhì)期：

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.
貨期：

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
注意事項(xiàng)：

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet ：

Please contact us to get it.

產(chǎn)品評(píng)價(jià)

靶點(diǎn)詳情

功能：

F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.; Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
亞細(xì)胞定位：

Cell inner membrane; Multi-pass membrane protein.
蛋白家族：

ATPase C chain family
數(shù)據(jù)庫(kù)鏈接：

KEGG: vfm:VFMJ11_2704