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92
LGC Standards 412
412, supplied by LGC Standards, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ATCC m bovis 10 tmc 412
Mycobacterium species tested
M Bovis 10 Tmc 412, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ADInstruments powerlab chart 4 1 2 software
Mycobacterium species tested
Powerlab Chart 4 1 2 Software, supplied by ADInstruments, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 98 stars, based on 1 article reviews
powerlab chart 4 1 2 software - by Bioz Stars, 2026-05
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90
RStudio rstudio version 2021.09.0
Mycobacterium species tested
Rstudio Version 2021.09.0, supplied by RStudio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
Jena Bioscience gtpγs
Effect <t>of</t> <t>GTP</t> hydrolysis on the kinetics of 70S IC maturation. 30S IC was rapidly mixed with 50S subunits (1 μM) in a stopped-flow ( A – E ) or a quench-flow ( F ) machine and the time courses of indicated reactions were monitored in the presence of GTP (black) or <t>GTPγS</t> (green). An inset in ( F ) shows the extended time window for peptide bond formation. Smooth lines (A–E) show fits obtained by global evaluation of all time courses using numerical integration.
Gtpγs, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 1 article reviews
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91
Jena Bioscience atto 425
Effect <t>of</t> <t>GTP</t> hydrolysis on the kinetics of 70S IC maturation. 30S IC was rapidly mixed with 50S subunits (1 μM) in a stopped-flow ( A – E ) or a quench-flow ( F ) machine and the time courses of indicated reactions were monitored in the presence of GTP (black) or <t>GTPγS</t> (green). An inset in ( F ) shows the extended time window for peptide bond formation. Smooth lines (A–E) show fits obtained by global evaluation of all time courses using numerical integration.
Atto 425, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 91 stars, based on 1 article reviews
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86
Boehringer Ingelheim bicyclic p38α
Effect <t>of</t> <t>GTP</t> hydrolysis on the kinetics of 70S IC maturation. 30S IC was rapidly mixed with 50S subunits (1 μM) in a stopped-flow ( A – E ) or a quench-flow ( F ) machine and the time courses of indicated reactions were monitored in the presence of GTP (black) or <t>GTPγS</t> (green). An inset in ( F ) shows the extended time window for peptide bond formation. Smooth lines (A–E) show fits obtained by global evaluation of all time courses using numerical integration.
Bicyclic P38α, supplied by Boehringer Ingelheim, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 86 stars, based on 1 article reviews
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SCILOGEX Inc scilogex® dmo 412
Effect <t>of</t> <t>GTP</t> hydrolysis on the kinetics of 70S IC maturation. 30S IC was rapidly mixed with 50S subunits (1 μM) in a stopped-flow ( A – E ) or a quench-flow ( F ) machine and the time courses of indicated reactions were monitored in the presence of GTP (black) or <t>GTPγS</t> (green). An inset in ( F ) shows the extended time window for peptide bond formation. Smooth lines (A–E) show fits obtained by global evaluation of all time courses using numerical integration.
Scilogex® Dmo 412, supplied by SCILOGEX Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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WiCell Research Institute Inc ucsd033i-41-2
Effect <t>of</t> <t>GTP</t> hydrolysis on the kinetics of 70S IC maturation. 30S IC was rapidly mixed with 50S subunits (1 μM) in a stopped-flow ( A – E ) or a quench-flow ( F ) machine and the time courses of indicated reactions were monitored in the presence of GTP (black) or <t>GTPγS</t> (green). An inset in ( F ) shows the extended time window for peptide bond formation. Smooth lines (A–E) show fits obtained by global evaluation of all time courses using numerical integration.
Ucsd033i 41 2, supplied by WiCell Research Institute Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
LECO Corporation multiphase carbon/moisture analyzer rc 412
Effect <t>of</t> <t>GTP</t> hydrolysis on the kinetics of 70S IC maturation. 30S IC was rapidly mixed with 50S subunits (1 μM) in a stopped-flow ( A – E ) or a quench-flow ( F ) machine and the time courses of indicated reactions were monitored in the presence of GTP (black) or <t>GTPγS</t> (green). An inset in ( F ) shows the extended time window for peptide bond formation. Smooth lines (A–E) show fits obtained by global evaluation of all time courses using numerical integration.
Multiphase Carbon/Moisture Analyzer Rc 412, supplied by LECO Corporation, 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/multiphase carbon/moisture analyzer rc 412/product/LECO Corporation
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LECO Corporation rc-412 c species analyzer
Effect <t>of</t> <t>GTP</t> hydrolysis on the kinetics of 70S IC maturation. 30S IC was rapidly mixed with 50S subunits (1 μM) in a stopped-flow ( A – E ) or a quench-flow ( F ) machine and the time courses of indicated reactions were monitored in the presence of GTP (black) or <t>GTPγS</t> (green). An inset in ( F ) shows the extended time window for peptide bond formation. Smooth lines (A–E) show fits obtained by global evaluation of all time courses using numerical integration.
Rc 412 C Species Analyzer, supplied by LECO Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
LECO Corporation leco ir-412 analyzer
Effect <t>of</t> <t>GTP</t> hydrolysis on the kinetics of 70S IC maturation. 30S IC was rapidly mixed with 50S subunits (1 μM) in a stopped-flow ( A – E ) or a quench-flow ( F ) machine and the time courses of indicated reactions were monitored in the presence of GTP (black) or <t>GTPγS</t> (green). An inset in ( F ) shows the extended time window for peptide bond formation. Smooth lines (A–E) show fits obtained by global evaluation of all time courses using numerical integration.
Leco Ir 412 Analyzer, supplied by LECO Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Mycobacterium species tested

Journal:

Article Title: Identification of Mycobacterium Species by PCR-Restriction Fragment Length Polymorphism Analyses Using Fluorescence Capillary Electrophoresis

doi:

Figure Lengend Snippet: Mycobacterium species tested

Article Snippet: Nonmycobacterial species included Corynebacterium diphtheriae , Tsukamurella sp., Corynebacterium pseudotuberculosis , Nocardia brasiliensis , and Gordona sputi ( 3 ). table ft1 table-wrap mode="anchored" t5 TABLE 1 caption a7 Species No. of isolates tested Reference strains a M. tuberculosis 16 TMC 119 (ATCC 35810) M. bovis 10 TMC 412 (ATCC 35726) M. bovis BCG (BCG Tice) 10 TMC 1028 (ATCC 35743) M. africanum 2 CDC72-1432 M. microti 2 TMC 1608 (ATCC 35782) M. avium 10 TMC 716 (ATCC 35717) M. intracellulare 3 TMC 1469 (ATCC 35772) M. simiae 7 TMC 1226 (ATCC 25275) M. gordonae 13 TMC 1324 (ATCC 14470) M. kansasii 10 TMC 1214 (ATCC 35777) M. fortuitum 5 CDC85-1098 M. peregrinum 3 TMC 1547 (ATCC 14467) M. chelonae 5 TMC 1524 (ATCC 35749) M. abscessus 5 TMC 1542 (ATCC 35751) M. celatum 9 ATCC 51131 M. marinum 10 909 b M. asiaticum 8 CDC88-334 M. mucogenicum 10 CDC86-650 M. malmoense 9 01355 b M. gastri 8 ATCC 25127 M. scrofulaceum 8 CDC89-447 M. szulgai 9 954 b M. xenopi 8 CDC90-TI-723 Total 180 Open in a separate window a Strain used for development and standardization of the procedure. b Strain provided by W. R. Butler.

Techniques:

Effect of GTP hydrolysis on the kinetics of 70S IC maturation. 30S IC was rapidly mixed with 50S subunits (1 μM) in a stopped-flow ( A – E ) or a quench-flow ( F ) machine and the time courses of indicated reactions were monitored in the presence of GTP (black) or GTPγS (green). An inset in ( F ) shows the extended time window for peptide bond formation. Smooth lines (A–E) show fits obtained by global evaluation of all time courses using numerical integration.

Journal: Nucleic Acids Research

Article Title: Directional transition from initiation to elongation in bacterial translation

doi: 10.1093/nar/gkv869

Figure Lengend Snippet: Effect of GTP hydrolysis on the kinetics of 70S IC maturation. 30S IC was rapidly mixed with 50S subunits (1 μM) in a stopped-flow ( A – E ) or a quench-flow ( F ) machine and the time courses of indicated reactions were monitored in the presence of GTP (black) or GTPγS (green). An inset in ( F ) shows the extended time window for peptide bond formation. Smooth lines (A–E) show fits obtained by global evaluation of all time courses using numerical integration.

Article Snippet: GTP, GDP, GTPγS, GDPNP, mant-GTP (2′/3′- O -( N -methyl-anthraniloyl)-guanosine-5′-triphosphate, triethylammonium salt) and mant-GTPγS (2′/3′- O -( N -methyl-anthraniloyl)-guanosine-5′-(γ-thio)-triphosphate, triethylammonium salt), were purchased from Jena Biosciences; Bpy-GTP (guanosine 5′-triphosphate, BODIPY FL 2′-(or-3′)- O -( N -(2-aminoethyl)urethane), trisodium salt) and Bpy-GDP (guanosine 5′-diphosphate, BODIPY FL 2′-(or-3′)- O -( N -(2-aminoethyl)urethane), bis-(triethylammonium) salt) from Life Technologies.

Techniques:

Effect of GTP hydrolysis on binding of IF1 and IF2 to mature 70S IC. ( A ) 30S IC formed in the presence of Bpy-Met-tRNA fMet and GTP (12.5 μM) was rapidly mixed with 50S subunits in the presence or absence of GTPγS (0.25 mM). Time courses of Bpy-Met-tRNA fMet fluorescence changes were monitored. ( B ) Interaction of Bpy-Met-tRNA fMet with IF2 upon binding of the factor to 70S IC was followed by mixing purified 70S ICs (containing Bpy-Met-tRNA fMet ) with IF2 bound to GTPγS, GDPNP, GTP or GDP. Similar experiments were performed using an IF2 variant lacking the C2-domain (ΔC2) in the presence of GTPγS. ( C ) 30S S13 (Alx488) IC formed with IF1 4 (Atto540Q) and GTP (12.5 μM) was mixed with 50S subunits in the presence or absence of GTPγS (0.25 mM). ( D ) The binding of the IF1 to mature 70S IC was followed by mixing non-purified 70S ICs (formed with 30S S13 (Alx488) in the absence of IF1) with IF1 4 (Atto540Q), in the presence of GTP or GTPγS.

Journal: Nucleic Acids Research

Article Title: Directional transition from initiation to elongation in bacterial translation

doi: 10.1093/nar/gkv869

Figure Lengend Snippet: Effect of GTP hydrolysis on binding of IF1 and IF2 to mature 70S IC. ( A ) 30S IC formed in the presence of Bpy-Met-tRNA fMet and GTP (12.5 μM) was rapidly mixed with 50S subunits in the presence or absence of GTPγS (0.25 mM). Time courses of Bpy-Met-tRNA fMet fluorescence changes were monitored. ( B ) Interaction of Bpy-Met-tRNA fMet with IF2 upon binding of the factor to 70S IC was followed by mixing purified 70S ICs (containing Bpy-Met-tRNA fMet ) with IF2 bound to GTPγS, GDPNP, GTP or GDP. Similar experiments were performed using an IF2 variant lacking the C2-domain (ΔC2) in the presence of GTPγS. ( C ) 30S S13 (Alx488) IC formed with IF1 4 (Atto540Q) and GTP (12.5 μM) was mixed with 50S subunits in the presence or absence of GTPγS (0.25 mM). ( D ) The binding of the IF1 to mature 70S IC was followed by mixing non-purified 70S ICs (formed with 30S S13 (Alx488) in the absence of IF1) with IF1 4 (Atto540Q), in the presence of GTP or GTPγS.

Article Snippet: GTP, GDP, GTPγS, GDPNP, mant-GTP (2′/3′- O -( N -methyl-anthraniloyl)-guanosine-5′-triphosphate, triethylammonium salt) and mant-GTPγS (2′/3′- O -( N -methyl-anthraniloyl)-guanosine-5′-(γ-thio)-triphosphate, triethylammonium salt), were purchased from Jena Biosciences; Bpy-GTP (guanosine 5′-triphosphate, BODIPY FL 2′-(or-3′)- O -( N -(2-aminoethyl)urethane), trisodium salt) and Bpy-GDP (guanosine 5′-diphosphate, BODIPY FL 2′-(or-3′)- O -( N -(2-aminoethyl)urethane), bis-(triethylammonium) salt) from Life Technologies.

Techniques: Binding Assay, Fluorescence, Purification, Variant Assay