Recombinant Candida glabrata V-type proton ATPase 16 kDa proteolipid subunit 2 (VMA11)

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Cat. No.
BT2111501
Source
in vitro E.coli expression system
Synonyms
VMA11; CAGL0E06204g; V-type proton ATPase 16 kDa proteolipid subunit 2; V-ATPase 16 kDa proteolipid subunit 2; Proteolipid protein VMA11; Vacuolar proton pump 16 kDa proteolipid subunit 2
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Description

Introduction to Recombinant Candida glabrata V-type Proton ATPase 16 kDa Proteolipid Subunit 2 (VMA11)

Recombinant Candida glabrata V-type proton ATPase 16 kDa proteolipid subunit 2, referred to here as VMA11, is a component of the vacuolar proton-translocating ATPase (V-ATPase) complex. This complex plays a crucial role in maintaining cellular pH homeostasis by pumping protons across membranes, which is essential for various cellular processes, including protein sorting and degradation in the vacuole .

Structure and Function of V-ATPase

The V-ATPase complex consists of two main domains: the V1 domain, which is cytoplasmic and involved in ATP hydrolysis, and the V0 domain, which is membrane-bound and responsible for proton transport . The VMA11 subunit is part of the V0 domain, contributing to the assembly and function of the V-ATPase complex.

Pathogenicity and Resistance

Candida glabrata is known for its resistance to azole antifungals, partly due to mechanisms involving efflux pumps and mutations in the ERG11 gene . The role of V-ATPase in maintaining cellular homeostasis could indirectly influence resistance by affecting cellular processes that contribute to drug susceptibility.

Cellular Processes

Cellular ProcessRole of V-ATPase
pH HomeostasisEssential for maintaining acidic pH in vacuoles, crucial for protein degradation and sorting .
Oxidative Stress ResponseRegulates expression and activity of antioxidant enzymes like superoxide dismutase .
Ion SensitivityInfluences calcium sensitivity and ion balance within the cell .

Potential Therapeutic Targets

Inhibiting V-ATPase with compounds like bafilomycin B1 can synergize with azole antifungals, enhancing their efficacy against Candida glabrata . This suggests that targeting V-ATPase components, including VMA11, could be a strategy to combat fungal infections.

Product Specs

Form
Lyophilized powder
Note: While we preferentially ship the format we have in stock, we are happy to accommodate special format requests. Please indicate your desired format when placing the order, and we will prepare it accordingly.
Lead Time
Delivery time may vary depending on the purchasing method and location. Please consult your local distributor for specific delivery timeframes.
Note: All of our proteins are shipped with standard blue ice packs. If you require dry ice shipping, please contact us in advance. Additional fees will apply.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Reconstitution
For optimal reconstitution, we recommend briefly centrifuging the vial prior to opening to ensure all contents are at the bottom. Please reconstitute the protein in deionized sterile water to a concentration between 0.1-1.0 mg/mL. For long-term storage, we recommend adding 5-50% glycerol (final concentration) and aliquoting the solution at -20°C/-80°C. Our standard final glycerol concentration is 50%, which can be used as a reference.
Shelf Life
The shelf life of our products is influenced by factors including storage conditions, buffer composition, temperature, and the inherent stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. For lyophilized form, the shelf life is 12 months at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquoting is essential for multiple use. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type will be determined during the manufacturing process.
The tag type is determined during production. If you have a specific tag type in mind, please inform us, and we will prioritize its development for your order.
Synonyms
VMA11; CAGL0E06204g; V-type proton ATPase 16 kDa proteolipid subunit 2; V-ATPase 16 kDa proteolipid subunit 2; Proteolipid protein VMA11; Vacuolar proton pump 16 kDa proteolipid subunit 2
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-164
Protein Length
full length protein
Species
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Target Names
VMA11
Target Protein Sequence
MDMVASDNVYAPLYAPFFGFAGCALAMILSCLGAAIGTAKSGIGIAGIGTFKPELIMKSL IPVVMSGILAIYGLVVAVLIAGNLSPTEEYTLFNGFMHLSCGLCVGFACLSSGYAIGIVG DVGVRKYMHQPRLFVGIVLILIFSEVLGLYGMIIALILNTKGSE
Uniprot No.
Q6FUY5

Target Background

Function
Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Database Links

KEGG: cgr:CAGL0E06204g

STRING: 284593.XP_445959.1

Protein Families
V-ATPase proteolipid subunit family
Subcellular Location
Vacuole membrane; Multi-pass membrane protein.

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