nuoF Antibody

Code CSB-PA616770XA01ENV
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Product Details

Full Product Name
Rabbit anti-Escherichia coli (strain K12) nuoF Polyclonal antibody
Uniprot No.
Target Names
nuoF
Alternative Names
nuoF antibody; b2284 antibody; JW2279 antibody; NADH-quinone oxidoreductase subunit F antibody; EC 7.1.1.- antibody; NADH dehydrogenase I subunit F antibody; NDH-1 subunit F antibody; NUO6 antibody
Raised in
Rabbit
Species Reactivity
Escherichia coli (strain K12)
Immunogen
Recombinant Escherichia coli (strain K12) nuoF protein
Immunogen Species
Escherichia coli (strain K12)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Antigen Affinity Purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB (ensure identification of antigen)
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Value-added Deliverables
① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);
Quality Guarantee
① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;
Lead Time
Made-to-order (14-16 weeks)

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Target Background

Function
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Gene References into Functions
  1. Data indicate that the NADH:ubiquinone oxidoreductase chain F (NuoF) E95Q variant of Complex I shows that the single amino acid replacement in the catalytic site caused a strong decrease of NADH binding. PMID: 25283488
  2. Data show that both NuoF mutations E183A and E183G having NADH and NADPH oxidizing ability. PMID: 21205901
  3. two distinct Electron Spin Resonance Spectroscopy, arising from a [4Fe-4S] cluster (g(x,y,z)=1.90, 1.95, and 2.05) in NuoF PMID: 15922336
Protein Families
Complex I 51 kDa subunit family
Database Links
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Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
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Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
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