atpF Antibody

^{Rare Species}

Datasheet

Code	CSB-PA002358XA02ENV1
Size	US$166
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Target Background

Product Details

Uniprot No.

P0ABA0

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

ELISA Protocol

Troubleshooting and FAQs

Antibody 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.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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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

Data indicate the juxtaposition of subunits b and a in the ATP synthase. PMID: 23416299
subunit b dimer of the FOF1-ATP synthase interacts with F1-ATPase PMID: 15339903
the b subunit of ATP synthase serves an active function in energy coupling rather than just holding on to the F1 sector PMID: 16531410
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
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

KEGG: ecj:JW3714

STRING: 316385.ECDH10B_3923

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7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA

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