5524 | MyBioSource

Probable manganese-dependent inorganic pyrophosphatase (ppaC), Recombinant Protein

Recombinant Clostridium acetobutylicum Probable manganese-dependent inorganic pyrophosphatase (ppaC)

(#MBS1486088)

Gene Names:

ppaC; CA_C2138

Other Names:

manganese-dependent inorganic pyrophosphatase

Host/Reactivities:

Host: E Coli or Yeast or Baculovirus or Mammalian Cell

Purity:

Greater or equal to 85% purity as determined by SDS-PAGE.

0.02 mg (Baculovirus)

$1440

0.02 mg (Mammalian-Cell)

0.1 mg (Mammalian-Cell)

$2770

1 mg (Baculovirus)

$4035

0.5 mg (Mammalian-Cell)

$7215

More Sizes/Prices

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ATP synthase subunit a (atpB), Recombinant Protein

Recombinant Clostridium acetobutylicum ATP synthase subunit a (atpB)

(#MBS1022456)

Gene Names:

atpB; atpA

Other Names:

Recombinant ATP synthase subunit a (atpB); ATP synthase subunit a; ATP synthase F0 sector subunit a F-ATPase subunit 6; ATP synthase F0F1 subunit A

Host/Reactivities:

Host: E Coli or Yeast or Baculovirus or Mammalian Cell

Purity:

Greater or equal to 85% purity as determined by SDS-PAGE.

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ATP synthase subunit c (atpE), Recombinant Protein

Recombinant Clostridium acetobutylicum ATP synthase subunit c (atpE)

(#MBS1247636)

Gene Names:

atpE; atpC

Other Names:

Recombinant ATP synthase subunit c (atpE); ATP synthase subunit c; ATP synthase F(0) sector subunit c F-type ATPase subunit c; F-ATPase subunit c Lipid-binding protein; ATP synthase F0F1 subunit C

Host/Reactivities:

Host: E Coli or Yeast or Baculovirus or Mammalian Cell

Purity:

Greater or equal to 85% purity as determined by SDS-PAGE.

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ATP synthase subunit b (atpF), Recombinant Protein

Recombinant Clostridium acetobutylicum ATP synthase subunit b (atpF)

(#MBS1192121)

Gene Names:

atpF; atpB; CA_C2869

Other Names:

ATP synthase subunit b; ATP synthase F(0) sector subunit b; ATPase subunit I; F-type ATPase subunit b; F-ATPase subunit b; ATP synthase F0F1 subunit B

Host/Reactivities:

Host: E Coli or Yeast or Baculovirus or Mammalian Cell

Purity:

Greater or equal to 85% purity as determined by SDS-PAGE.

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