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Recombinant Saccharomyces cerevisiae V-type proton ATPase subunit C (VMA5)

Recombinant Saccharomyces cerevisiae V-type proton ATPase subunit C (VMA5)

Code	CSB-YP339168SVG
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP339168SVG
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP339168SVG-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	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.
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Code	CSB-BP339168SVG
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP339168SVG
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

VMA5

Uniprot No.

P31412

Alternative Names

VMA5; VAT3; VATC; YKL080W; YKL410; V-type proton ATPase subunit C; V-ATPase subunit C; V-ATPase 42 kDa subunit; Vacuolar proton pump subunit C

Species

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Expression Region

2-392

Target Protein Sequence

ATALYTAND FILISLPQNA QPVTAPGSKT DSWFNETLIG GRAFVSDFKI PEFKIGSLDT LIVESEELSK VDNQIGASIG KIIEILQGLN ETSTNAYRTL PINNMPVPEY LENFQWQTRK FKLDKSIKDL ITLISNESSQ LDADVRATYA NYNSAKTNLA AAERKKTGDL SVRSLHDIVK PEDFVLNSEH LTTVLVAVPK SLKSDFEKSY ETLSKNVVPA SASVIAEDAE YVLFNVHLFK KNVQEFTTAA REKKFIPREF NYSEELIDQL KKEHDSAASL EQSLRVQLVR LAKTAYVDVF INWFHIKALR VYVESVLRYG LPPHFNIKII AVPPKNLSKC KSELIDAFGF LGGNAFMKDK KGKINKQDTS LHQYASLVDT EYEPFVMYII NL

Protein Length

Full Length of Mature Protein

Tag Info

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.

Form

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.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

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.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

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.

Lead Time

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.

Notes

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.

Customer Reviews and Q&A

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Target Background

Function

Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C acts as a flexible stator that holds together the catalytic and the membrane sectors of the enzyme. Reversibly leaves the enzyme after glucose depletion, causing the catalytic subcomplex V1 to detach from the V0 section. Binds ATP and is likely to have a specific function in the catalytic activity of the catalytic sector. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

Gene References into Functions

We speculate that the spatial closeness of the a(NT), C(foot), and EG binding sites in the intact V-ATPase results in a high-avidity interaction that is able to resist the torque of rotational catalysis. PMID: 22367203
Domain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G PMID: 20529855
Expression, crystallization and phasing of vacuolar H(+)-ATPase subunit C (Vma5p) of Saccharomyces cerevisiae PMID: 15388948
Vma5 (subunit C) expressed as a glutathione-S-transferase fusion protein in Escherichia coli is able to interact strongly with Vma4 (subunit E) expressed in a cell-free system. PMID: 15751969
VMA5p subunit C localizes to the interface of the V1 and V0 domains, which is consistent with a role for this subunit in controlling assembly of the V-ATPase complex PMID: 15951435
Nucleotide occupancy by subunit C, followed by conformational changes of this subunit has shed light on the mechanism of V-ATPase regulation. PMID: 16042619
The data show that subunit C is binding at the interface of the ATPase and proton channel, opposite from another stalk density previously identified as subunit H. PMID: 16546180