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Showing 1 to 6 of 6 found results for "422549"
Glutamyl-tRNA reductase (hemA)

Recombinant Mycobacterium tuberculosis Glutamyl-tRNA reductase (hemA)

(#MBS1009009)

Gene Names:
hemA
Other Names:
MULTISPECIES: glutamyl-tRNA reductase
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.
Glutamate--tRNA ligase (gltX)

Recombinant Mycobacterium tuberculosis Glutamate--tRNA ligase (gltX)

(#MBS1106182)

Gene Names:
gltX; gltS
Other Names:
MULTISPECIES: glutamate--tRNA ligase
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.
Ferrochelatase (hemH)

Recombinant Mycobacterium tuberculosis Ferrochelatase (hemH)

(#MBS1176264)

Gene Names:
hemH; hemZ
Other Names:
MULTISPECIES: ferrochelatase
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.
Glutamate-1-semialdehyde 2,1-aminomutase (hemL)

Recombinant Mycobacterium tuberculosis Glutamate-1-semialdehyde 2,1-aminomutase (hemL)

(#MBS1079014)

Gene Names:
hemL
Other Names:
MULTISPECIES: glutamate-1-semialdehyde 2,1-aminomutase
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.
Uroporphyrinogen decarboxylase (hemE)

Recombinant Mycobacterium tuberculosis Uroporphyrinogen decarboxylase (hemE)

(#MBS1069752)

Gene Names:
hemE
Other Names:
MULTISPECIES: uroporphyrinogen decarboxylase
Host/Reactivities:
Host: E Coli or Yeast or Baculovirus or Mammalian Cell
Purity:
Greater or equal to 85% purity as determined by SDS-PAGE.
Porphobilinogen deaminase (hemC)

Recombinant Mycobacterium tuberculosis Porphobilinogen deaminase (hemC)

(#MBS1033884)

Gene Names:
hemC
Other Names:
MULTISPECIES: hydroxymethylbilane synthase
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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