Recombinant Buchnera aphidicola subsp. Baizongia pistaciae NADH-quinone oxidoreductase subunit G (nuoG), partial

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Description

Introduction to Recombinant Buchnera aphidicola subsp. Baizongia pistaciae NADH-quinone Oxidoreductase Subunit G (nuoG), Partial

Recombinant Buchnera aphidicola subsp. Baizongia pistaciae NADH-quinone oxidoreductase subunit G (nuoG), partial, refers to a genetically engineered fragment of the nuoG subunit derived from Buchnera aphidicola subsp. Baizongia pistaciae . Buchnera aphidicola is a genus of Gram-negative bacteria that exists as an obligate endosymbiont in aphids, providing essential nutrients that are lacking in the aphids' sap diet .

NADH-quinone oxidoreductase (Complex I) is a large enzyme complex found in the respiratory chain of many organisms, including bacteria and mitochondria . It catalyzes the transfer of electrons from NADH to quinone, coupled with the translocation of protons across the membrane, contributing to the generation of a proton gradient that drives ATP synthesis . Subunit G (nuoG) is one of the subunits of this complex, playing a crucial role in the electron transfer process.

The term "partial" indicates that the recombinant protein represents only a fragment of the full-length NuoG subunit . This fragment is produced using recombinant DNA technology, where the gene encoding the subunit or a portion thereof is inserted into a host organism (e.g., E. coli) for expression and production . The recombinant protein can then be isolated and used for various research purposes.

Buchnera aphidicola as an Endosymbiont

Buchnera aphidicola are critical symbiotic bacteria that reside within specialized cells called bacteriocytes in aphids . These bacteria have co-evolved with aphids for millions of years, with different strains specific to different aphid lineages . Buchnera provides essential amino acids and other nutrients that are scarce in the phloem sap that aphids feed on . In return, the bacteria receive a stable and protected environment within the aphid host.

The Baizongia pistaciae subspecies of Buchnera aphidicola is found in aphids that feed on pistachio trees . The genome of this subspecies has been sequenced, revealing a high degree of gene-order conservation compared to other Buchnera strains, suggesting a long history of symbiotic association with aphids .

Function and Significance of NADH-quinone Oxidoreductase

NADH-quinone oxidoreductase (Complex I) is a vital enzyme complex in the respiratory chain of bacteria and mitochondria . It catalyzes the transfer of electrons from NADH to quinone, coupled with the translocation of protons across the membrane. This process contributes to the generation of a proton gradient that drives ATP synthesis.

The enzyme complex consists of several subunits, each with a specific function. Subunit G (nuoG) is involved in the electron transfer process. The recombinant, partial subunit may be used to study the structure, function, and interactions of this subunit within the larger complex.

Recombinant Production and Applications

Recombinant Buchnera aphidicola subsp. Baizongia pistaciae NADH-quinone oxidoreductase subunit G (nuoG), partial is produced using recombinant DNA technology . The gene encoding the subunit or a portion thereof is inserted into a host organism (E. coli) for expression and production. The recombinant protein is then isolated and purified for research purposes.

Applications of the recombinant protein include:

  • Structural studies: to determine the three-dimensional structure of the subunit and its interactions with other subunits in Complex I.

  • Functional studies: to investigate the role of the subunit in electron transfer and proton translocation.

  • Drug discovery: to identify compounds that inhibit the activity of Complex I, which could be useful as antibacterial agents.

  • Immunological studies: to develop antibodies against the subunit for use in immunoassays and other applications.

Product Specs

Form
Lyophilized powder
Note: While we prioritize shipping the format currently in stock, please specify your format preference in order notes for customized preparation.
Lead Time
Delivery times vary depending on the purchase method and location. Please contact your local distributor for precise delivery estimates.
Note: Standard shipping includes blue ice packs. Dry ice shipping requires prior arrangement and incurs additional charges.
Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Centrifuge the vial briefly before opening to consolidate the contents. Reconstitute the protein in sterile, deionized water to a concentration of 0.1-1.0 mg/mL. For long-term storage, we recommend adding 5-50% glycerol (final concentration) and aliquoting at -20°C/-80°C. Our standard glycerol concentration is 50% and can serve as a reference.
Shelf Life
Shelf life depends on storage conditions, buffer composition, temperature, and protein stability. Generally, liquid formulations have a 6-month shelf life at -20°C/-80°C, while lyophilized forms have a 12-month shelf life at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquot to prevent repeated freeze-thaw cycles.
Tag Info
Tag type is determined during manufacturing.
The tag type is determined during production. If you require a specific tag, please inform us for preferential development.
Synonyms
nuoG; bbp_148NADH-quinone oxidoreductase subunit G; EC 7.1.1.-; NADH dehydrogenase I subunit G; NDH-1 subunit G
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Protein Length
Partial
Purity
>85% (SDS-PAGE)
Species
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Target Names
nuoG
Uniprot No.

Target Background

Function

NDH-1 Function: NDH-1 facilitates electron transfer from NADH to quinones within the respiratory chain, utilizing FMN and iron-sulfur (Fe-S) centers as intermediates. This redox reaction is coupled to proton translocation; for every two electrons transferred, four protons are translocated across the cytoplasmic membrane, conserving redox energy within a proton gradient.

Database Links

KEGG: bab:bbp_148

STRING: 224915.bbp148

Protein Families
Complex I 75 kDa subunit family

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