atpF Antibody

Code CSB-PA002358XA02ENV1
Size US$166
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Product Details

Uniprot No.
Target Names
atpF
Alternative Names
ATP synthase subunit b (ATP synthase F(0) sector subunit b) (ATPase subunit I) (F-type ATPase subunit b) (F-ATPase subunit b), atpF, papF uncF
Species Reactivity
E.coli
Immunogen
Synthetic Peptide (33-60aa)
Immunogen Species
Escherichia coli(strain K12)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
Affinity-chromatography
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
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
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.; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Gene References into Functions
  1. Data indicate the juxtaposition of subunits b and a in the ATP synthase. PMID: 23416299
  2. subunit b dimer of the FOF1-ATP synthase interacts with F1-ATPase PMID: 15339903
  3. the b subunit of ATP synthase serves an active function in energy coupling rather than just holding on to the F1 sector PMID: 16531410
  4. The results indicate a right-handed coiled-coil structure with intrinsic asymmetry, the two helices being offset rather than in register. A function for the right-handed coiled coil in rotational catalysis is proposed. PMID: 17028022
  5. The first solution structure of b30-82, including the tether region and part of the dimerization domain, has been solved by nuclear magnetic resonance, revealing an alpha-helix between residues 39 and 72. PMID: 19820091

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Subcellular Location
Cell inner membrane; Single-pass membrane protein.
Protein Families
ATPase B chain family
Database Links
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301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
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7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
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