total alkalinity gran titration system as-alk2 Search Results


as-alk2 gran titrator  (Apollo SciTech)
90
Apollo SciTech as-alk2 gran titrator
As Alk2 Gran Titrator, supplied by Apollo SciTech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/as-alk2 gran titrator/product/Apollo SciTech
Average 90 stars, based on 1 article reviews
as-alk2 gran titrator - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
instrument as-c3  (Apollo SciTech)
90
Apollo SciTech instrument as-c3
Instrument As C3, supplied by Apollo SciTech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/instrument as-c3/product/Apollo SciTech
Average 90 stars, based on 1 article reviews
instrument as-c3 - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
t. saccharolyticum strains ll1049 (also known as m1442 or mo1442)  (Mascoma LLC)
90
Mascoma LLC t. saccharolyticum strains ll1049 (also known as m1442 or mo1442)
Primary structures of AdhE proteins of wild-type C. thermocellum and T. saccharolyticum. (A) The ALDH domain is at positions 1 to 423 for C. thermocellum and 1 to 420 for T. saccharolyticum, the ADH domain is at positions 463 to 873 for C. thermocellum and 460 to 860 for T. saccharolyticum, and the linker sequence is at positions 424 to 462 for C. thermocellum and 421 to 459 for T. saccharolyticum. NADH binding site 1 is at positions 200 to 221 for C. thermocellum and 199 to 220 for T. saccharolyticum; NADH binding site 2 is at positions 551 to 553 for C. thermocellum and 543 to 545 for T. saccharolyticum. Mutated residues discussed in this study are annotated at the appropriate positions as follows: D494G in LL350; P704L and H734R in LL346; V52A, K451N, and a 13-amino-acid (a.a.) insertion in <t>LL1040;</t> and G544D in LL1049. All elements are drawn to scale. Panels B and C show the sequence conservation of the NADH binding motifs (highlighted in yellow in the consensus sequence) of AdhE from Thermoanaerobacter ethanolicus, Thermoanaerobacter mathranii, T. saccharolyticum, Entamoeba histolytica, E. coli, C. thermocellum, Leuconostoc mesenteroides, Lactococcus lactis, Oenococcus oeni, and Streptococcus equinus. The residues highlighted in red are the most conserved, and those highlighted in blue are the least conserved. The numbering of amino acids is based on the AdhE sequence of C. thermocellum.
T. Saccharolyticum Strains Ll1049 (Also Known As M1442 Or Mo1442), supplied by Mascoma LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/t. saccharolyticum strains ll1049 (also known as m1442 or mo1442)/product/Mascoma LLC
Average 90 stars, based on 1 article reviews
t. saccharolyticum strains ll1049 (also known as m1442 or mo1442) - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
orion 8102bn ross electrode  (Apollo SciTech)
90
Apollo SciTech orion 8102bn ross electrode
Primary structures of AdhE proteins of wild-type C. thermocellum and T. saccharolyticum. (A) The ALDH domain is at positions 1 to 423 for C. thermocellum and 1 to 420 for T. saccharolyticum, the ADH domain is at positions 463 to 873 for C. thermocellum and 460 to 860 for T. saccharolyticum, and the linker sequence is at positions 424 to 462 for C. thermocellum and 421 to 459 for T. saccharolyticum. NADH binding site 1 is at positions 200 to 221 for C. thermocellum and 199 to 220 for T. saccharolyticum; NADH binding site 2 is at positions 551 to 553 for C. thermocellum and 543 to 545 for T. saccharolyticum. Mutated residues discussed in this study are annotated at the appropriate positions as follows: D494G in LL350; P704L and H734R in LL346; V52A, K451N, and a 13-amino-acid (a.a.) insertion in <t>LL1040;</t> and G544D in LL1049. All elements are drawn to scale. Panels B and C show the sequence conservation of the NADH binding motifs (highlighted in yellow in the consensus sequence) of AdhE from Thermoanaerobacter ethanolicus, Thermoanaerobacter mathranii, T. saccharolyticum, Entamoeba histolytica, E. coli, C. thermocellum, Leuconostoc mesenteroides, Lactococcus lactis, Oenococcus oeni, and Streptococcus equinus. The residues highlighted in red are the most conserved, and those highlighted in blue are the least conserved. The numbering of amino acids is based on the AdhE sequence of C. thermocellum.
Orion 8102bn Ross Electrode, supplied by Apollo SciTech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/orion 8102bn ross electrode/product/Apollo SciTech
Average 90 stars, based on 1 article reviews
orion 8102bn ross electrode - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier
apollo sci-tec as-alk2  (Apollo Scientific Ltd)
90
Apollo Scientific Ltd apollo sci-tec as-alk2
Primary structures of AdhE proteins of wild-type C. thermocellum and T. saccharolyticum. (A) The ALDH domain is at positions 1 to 423 for C. thermocellum and 1 to 420 for T. saccharolyticum, the ADH domain is at positions 463 to 873 for C. thermocellum and 460 to 860 for T. saccharolyticum, and the linker sequence is at positions 424 to 462 for C. thermocellum and 421 to 459 for T. saccharolyticum. NADH binding site 1 is at positions 200 to 221 for C. thermocellum and 199 to 220 for T. saccharolyticum; NADH binding site 2 is at positions 551 to 553 for C. thermocellum and 543 to 545 for T. saccharolyticum. Mutated residues discussed in this study are annotated at the appropriate positions as follows: D494G in LL350; P704L and H734R in LL346; V52A, K451N, and a 13-amino-acid (a.a.) insertion in <t>LL1040;</t> and G544D in LL1049. All elements are drawn to scale. Panels B and C show the sequence conservation of the NADH binding motifs (highlighted in yellow in the consensus sequence) of AdhE from Thermoanaerobacter ethanolicus, Thermoanaerobacter mathranii, T. saccharolyticum, Entamoeba histolytica, E. coli, C. thermocellum, Leuconostoc mesenteroides, Lactococcus lactis, Oenococcus oeni, and Streptococcus equinus. The residues highlighted in red are the most conserved, and those highlighted in blue are the least conserved. The numbering of amino acids is based on the AdhE sequence of C. thermocellum.
Apollo Sci Tec As Alk2, supplied by Apollo Scientific Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/apollo sci-tec as-alk2/product/Apollo Scientific Ltd
Average 90 stars, based on 1 article reviews
apollo sci-tec as-alk2 - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier

Image Search Results


Primary structures of AdhE proteins of wild-type C. thermocellum and T. saccharolyticum. (A) The ALDH domain is at positions 1 to 423 for C. thermocellum and 1 to 420 for T. saccharolyticum, the ADH domain is at positions 463 to 873 for C. thermocellum and 460 to 860 for T. saccharolyticum, and the linker sequence is at positions 424 to 462 for C. thermocellum and 421 to 459 for T. saccharolyticum. NADH binding site 1 is at positions 200 to 221 for C. thermocellum and 199 to 220 for T. saccharolyticum; NADH binding site 2 is at positions 551 to 553 for C. thermocellum and 543 to 545 for T. saccharolyticum. Mutated residues discussed in this study are annotated at the appropriate positions as follows: D494G in LL350; P704L and H734R in LL346; V52A, K451N, and a 13-amino-acid (a.a.) insertion in LL1040; and G544D in LL1049. All elements are drawn to scale. Panels B and C show the sequence conservation of the NADH binding motifs (highlighted in yellow in the consensus sequence) of AdhE from Thermoanaerobacter ethanolicus, Thermoanaerobacter mathranii, T. saccharolyticum, Entamoeba histolytica, E. coli, C. thermocellum, Leuconostoc mesenteroides, Lactococcus lactis, Oenococcus oeni, and Streptococcus equinus. The residues highlighted in red are the most conserved, and those highlighted in blue are the least conserved. The numbering of amino acids is based on the AdhE sequence of C. thermocellum.

Journal: Journal of Bacteriology

Article Title: Cofactor Specificity of the Bifunctional Alcohol and Aldehyde Dehydrogenase (AdhE) in Wild-Type and Mutant Clostridium thermocellum and Thermoanaerobacterium saccharolyticum

doi: 10.1128/JB.00232-15

Figure Lengend Snippet: Primary structures of AdhE proteins of wild-type C. thermocellum and T. saccharolyticum. (A) The ALDH domain is at positions 1 to 423 for C. thermocellum and 1 to 420 for T. saccharolyticum, the ADH domain is at positions 463 to 873 for C. thermocellum and 460 to 860 for T. saccharolyticum, and the linker sequence is at positions 424 to 462 for C. thermocellum and 421 to 459 for T. saccharolyticum. NADH binding site 1 is at positions 200 to 221 for C. thermocellum and 199 to 220 for T. saccharolyticum; NADH binding site 2 is at positions 551 to 553 for C. thermocellum and 543 to 545 for T. saccharolyticum. Mutated residues discussed in this study are annotated at the appropriate positions as follows: D494G in LL350; P704L and H734R in LL346; V52A, K451N, and a 13-amino-acid (a.a.) insertion in LL1040; and G544D in LL1049. All elements are drawn to scale. Panels B and C show the sequence conservation of the NADH binding motifs (highlighted in yellow in the consensus sequence) of AdhE from Thermoanaerobacter ethanolicus, Thermoanaerobacter mathranii, T. saccharolyticum, Entamoeba histolytica, E. coli, C. thermocellum, Leuconostoc mesenteroides, Lactococcus lactis, Oenococcus oeni, and Streptococcus equinus. The residues highlighted in red are the most conserved, and those highlighted in blue are the least conserved. The numbering of amino acids is based on the AdhE sequence of C. thermocellum.

Article Snippet: We thank the Mascoma Corporation for their gift of T. saccharolyticum strains LL1076 (also known as M3223), LL1040 (also known as ALK2 or M0001), LL1049 (also known as M1442 or MO1442), LL1193 (also known as M2203), and LL1194 (also known as M2202).

Techniques: Sequencing, Binding Assay

Strains used in this study

Journal: Journal of Bacteriology

Article Title: Cofactor Specificity of the Bifunctional Alcohol and Aldehyde Dehydrogenase (AdhE) in Wild-Type and Mutant Clostridium thermocellum and Thermoanaerobacterium saccharolyticum

doi: 10.1128/JB.00232-15

Figure Lengend Snippet: Strains used in this study

Article Snippet: We thank the Mascoma Corporation for their gift of T. saccharolyticum strains LL1076 (also known as M3223), LL1040 (also known as ALK2 or M0001), LL1049 (also known as M1442 or MO1442), LL1193 (also known as M2203), and LL1194 (also known as M2202).

Techniques: Mutagenesis, Marker

ALDH and ADH activities in C. thermocellum and T. saccharolyticum cell extracts

Journal: Journal of Bacteriology

Article Title: Cofactor Specificity of the Bifunctional Alcohol and Aldehyde Dehydrogenase (AdhE) in Wild-Type and Mutant Clostridium thermocellum and Thermoanaerobacterium saccharolyticum

doi: 10.1128/JB.00232-15

Figure Lengend Snippet: ALDH and ADH activities in C. thermocellum and T. saccharolyticum cell extracts

Article Snippet: We thank the Mascoma Corporation for their gift of T. saccharolyticum strains LL1076 (also known as M3223), LL1040 (also known as ALK2 or M0001), LL1049 (also known as M1442 or MO1442), LL1193 (also known as M2203), and LL1194 (also known as M2202).

Techniques: Activity Assay

Cofactor specificities of purified AdhE proteins

Journal: Journal of Bacteriology

Article Title: Cofactor Specificity of the Bifunctional Alcohol and Aldehyde Dehydrogenase (AdhE) in Wild-Type and Mutant Clostridium thermocellum and Thermoanaerobacterium saccharolyticum

doi: 10.1128/JB.00232-15

Figure Lengend Snippet: Cofactor specificities of purified AdhE proteins

Article Snippet: We thank the Mascoma Corporation for their gift of T. saccharolyticum strains LL1076 (also known as M3223), LL1040 (also known as ALK2 or M0001), LL1049 (also known as M1442 or MO1442), LL1193 (also known as M2203), and LL1194 (also known as M2202).

Techniques: Purification, Activity Assay

Average structure of the ADH domains of AdhE from C. thermocellum wild-type LL1004 (A), the ethanol-tolerant LL346 strain (B), moderate ethanol producer LL350 (C), T. saccharolyticum wild-type LL1025 (D), high ethanol producer LL1049 (E), and high ethanol producer LL1040 (F). The amino acids of interest are shown in blue and red; the NADPH cofactor is shown color coded by elements, with its 2′-phosphate group highlighted (green open circle); and the iron ions (green) are also shown. Additionally, the 39-bp insertion in the high ethanol producer LL1040 is shown in orange (F). The yellow-filled circle represents the binding pocket where the additional 2′-phosphate of NADPH is commonly found in NADPH-dependent AdhE proteins. The locations of D494 and D486 are usually the recognition sites for NADH and do not allow the 2′-phosphate group of NADPH (green circle) to access the preferred binding pocket (yellow circle). When the green open circle and the yellow filled circle overlap, that indicates that the NADPH molecule is able to access its preferred binding pocket. This is present in panels C, E, and F but not in the other panels. Panels C, E, and F correspond to enzymes that can use NADPH as a cofactor. Note that NADPH was used for modeling purposes and does not reflect the actual cofactor specificity of the enzymes but rather was used to explain the observed levels of affinity of the enzymes for NADPH.

Journal: Journal of Bacteriology

Article Title: Cofactor Specificity of the Bifunctional Alcohol and Aldehyde Dehydrogenase (AdhE) in Wild-Type and Mutant Clostridium thermocellum and Thermoanaerobacterium saccharolyticum

doi: 10.1128/JB.00232-15

Figure Lengend Snippet: Average structure of the ADH domains of AdhE from C. thermocellum wild-type LL1004 (A), the ethanol-tolerant LL346 strain (B), moderate ethanol producer LL350 (C), T. saccharolyticum wild-type LL1025 (D), high ethanol producer LL1049 (E), and high ethanol producer LL1040 (F). The amino acids of interest are shown in blue and red; the NADPH cofactor is shown color coded by elements, with its 2′-phosphate group highlighted (green open circle); and the iron ions (green) are also shown. Additionally, the 39-bp insertion in the high ethanol producer LL1040 is shown in orange (F). The yellow-filled circle represents the binding pocket where the additional 2′-phosphate of NADPH is commonly found in NADPH-dependent AdhE proteins. The locations of D494 and D486 are usually the recognition sites for NADH and do not allow the 2′-phosphate group of NADPH (green circle) to access the preferred binding pocket (yellow circle). When the green open circle and the yellow filled circle overlap, that indicates that the NADPH molecule is able to access its preferred binding pocket. This is present in panels C, E, and F but not in the other panels. Panels C, E, and F correspond to enzymes that can use NADPH as a cofactor. Note that NADPH was used for modeling purposes and does not reflect the actual cofactor specificity of the enzymes but rather was used to explain the observed levels of affinity of the enzymes for NADPH.

Article Snippet: We thank the Mascoma Corporation for their gift of T. saccharolyticum strains LL1076 (also known as M3223), LL1040 (also known as ALK2 or M0001), LL1049 (also known as M1442 or MO1442), LL1193 (also known as M2203), and LL1194 (also known as M2202).

Techniques: Binding Assay