fd 1 50 vacuum freeze dryer Search Results


90
Dynavac Engineering Pty Limited benchtop vacuum freeze- drier
Benchtop Vacuum Freeze Drier, supplied by Dynavac Engineering Pty Limited, 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/product/fd+1+50+vacuum+freeze+dryer/benchtop+vacuum+freeze++drier/10__1111_slash_jac__12603-99-23-27
Average 90 stars, based on 1 article reviews
benchtop vacuum freeze- drier - by Bioz Stars, 2026-10
90/100 stars
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86
Beijing Boyikang Laboratory fd 1 50 vacuum freeze dryer
Fd 1 50 Vacuum Freeze Dryer, supplied by Beijing Boyikang Laboratory, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fd+1+50+vacuum+freeze+dryer/1+50e+a+dryer+fd+freeze+vacuum/pmc13112376-61-0-4
Average 86 stars, based on 1 article reviews
fd 1 50 vacuum freeze dryer - by Bioz Stars, 2026-10
86/100 stars
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96
MACHEREY NAGEL fd1 genomic dna
Figure 1. Hydrophobic interaction chromatography of <t>FD1</t> formaldehyde dismutase. The solid line, relative formaldehyde dismutase activity; the dashed line, the concentration of ammonium sulfate. (A) and (B) were the fractions with relatively high formaldehyde dismutase activity. Experimental conditions are specified in Materials and methods.
Fd1 Genomic Dna, supplied by MACHEREY NAGEL, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fd+1+50+vacuum+freeze+dryer/NucleoSpin+Virus%2C+Mini+kit+for+viral+RNA+%2F+DNA+purification/pm29173106-69-13-29
Average 96 stars, based on 1 article reviews
fd1 genomic dna - by Bioz Stars, 2026-10
96/100 stars
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90
Shanghai Bilon Instrument freeze-dryer fd-1 a-50
Figure 1. Hydrophobic interaction chromatography of <t>FD1</t> formaldehyde dismutase. The solid line, relative formaldehyde dismutase activity; the dashed line, the concentration of ammonium sulfate. (A) and (B) were the fractions with relatively high formaldehyde dismutase activity. Experimental conditions are specified in Materials and methods.
Freeze Dryer Fd 1 A 50, supplied by Shanghai Bilon Instrument, 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/product/fd+1+50+vacuum+freeze+dryer/freeze+dryer+fd+1+a+50/pm40158976-69-8-13
Average 90 stars, based on 1 article reviews
freeze-dryer fd-1 a-50 - by Bioz Stars, 2026-10
90/100 stars
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95
ATS Scientific Inc freeze dryer
Figure 1. Hydrophobic interaction chromatography of <t>FD1</t> formaldehyde dismutase. The solid line, relative formaldehyde dismutase activity; the dashed line, the concentration of ammonium sulfate. (A) and (B) were the fractions with relatively high formaldehyde dismutase activity. Experimental conditions are specified in Materials and methods.
Freeze Dryer, supplied by ATS Scientific Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/fd+1+50+vacuum+freeze+dryer/SMART+Freeze+Dryer+Technology/pm41075660-37-41-44
Average 95 stars, based on 1 article reviews
freeze dryer - by Bioz Stars, 2026-10
95/100 stars
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Standard format: Plasmid sent in bacteria as agar stab
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N/A
This is a rabbit polyclonal antibody against TRAFD1. It was validated on Western Blot and immunohistochemistry by Aviva Systems Biology. At Aviva Systems Biology we manufacture rabbit polyclonal antibodies on a large scale (200-1000 products/month)
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The MTERFD1 Antibody [DyLight 350] from Novus is a MTERFD1 antibody to MTERFD1. This antibody reacts with Human, Mouse. The MTERFD1 antibody has been validated for the following applications: Western Blot, ELISA, Immunocytochemistry/ Immunofluorescence.
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N/A
The MTERFD1 Antibody [DyLight 550] from Novus is a MTERFD1 antibody to MTERFD1. This antibody reacts with Human, Mouse. The MTERFD1 antibody has been validated for the following applications: Western Blot, ELISA, Immunocytochemistry/ Immunofluorescence.
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N/A
The MTERFD1 Antibody [DyLight 650] from Novus is a MTERFD1 antibody to MTERFD1. This antibody reacts with Human, Mouse. The MTERFD1 antibody has been validated for the following applications: Western Blot, ELISA, Immunocytochemistry/ Immunofluorescence.
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N/A
The MTERFD1 Antibody [Janelia Fluor® 646] from Novus is a MTERFD1 antibody to MTERFD1. This antibody reacts with Human, Mouse. The MTERFD1 antibody has been validated for the following applications: Western Blot, ELISA, Immunocytochemistry/ Immunofluorescence.
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Image Search Results


Figure 1. Hydrophobic interaction chromatography of FD1 formaldehyde dismutase. The solid line, relative formaldehyde dismutase activity; the dashed line, the concentration of ammonium sulfate. (A) and (B) were the fractions with relatively high formaldehyde dismutase activity. Experimental conditions are specified in Materials and methods.

Journal: Bioscience, biotechnology, and biochemistry

Article Title: Biodegradation of high concentrations of formaldehyde using Escherichia coli expressing the formaldehyde dismutase gene of Methylobacterium sp. FD1.

doi: 10.1080/09168451.2017.1397497

Figure Lengend Snippet: Figure 1. Hydrophobic interaction chromatography of FD1 formaldehyde dismutase. The solid line, relative formaldehyde dismutase activity; the dashed line, the concentration of ammonium sulfate. (A) and (B) were the fractions with relatively high formaldehyde dismutase activity. Experimental conditions are specified in Materials and methods.

Article Snippet: Polymerase chain reaction (PCR) amplification of the formaldehyde dismutase gene of Methylobacterium sp. FD1 Genomic DNA was extracted from FD1 cells cultured in tryptic soy broth using NucleoSpin® Tissue (MACHEREYNAGEL, Düren, Germany), according to the manufacturer’s instructions.

Techniques: Hydrophobic Interaction Chromatography, Activity Assay, Concentration Assay

Figure 4. SDS-PAGE of protein extracts and precipitate fractions of E. coli transformed with the formaldehyde dismutase gene of FD1. For all samples, 10 μg of total protein were loaded. Lanes 1–4, the recombinant E. coli with pRham-FDM; lanes 5 and 6, the recombinant E. coli with pRham (no insert); lanes 1, 3, and 5, cell-free protein extracts; lanes 2, 4, and 6, precipitate fractions; lanes 1 and 2, no rhamnose induction; lanes 3, 4, 5, and 6, rhamnose induction. A triangle indicates a specific band. Experimental conditions are specified in Materials and methods.

Journal: Bioscience, biotechnology, and biochemistry

Article Title: Biodegradation of high concentrations of formaldehyde using Escherichia coli expressing the formaldehyde dismutase gene of Methylobacterium sp. FD1.

doi: 10.1080/09168451.2017.1397497

Figure Lengend Snippet: Figure 4. SDS-PAGE of protein extracts and precipitate fractions of E. coli transformed with the formaldehyde dismutase gene of FD1. For all samples, 10 μg of total protein were loaded. Lanes 1–4, the recombinant E. coli with pRham-FDM; lanes 5 and 6, the recombinant E. coli with pRham (no insert); lanes 1, 3, and 5, cell-free protein extracts; lanes 2, 4, and 6, precipitate fractions; lanes 1 and 2, no rhamnose induction; lanes 3, 4, 5, and 6, rhamnose induction. A triangle indicates a specific band. Experimental conditions are specified in Materials and methods.

Article Snippet: Polymerase chain reaction (PCR) amplification of the formaldehyde dismutase gene of Methylobacterium sp. FD1 Genomic DNA was extracted from FD1 cells cultured in tryptic soy broth using NucleoSpin® Tissue (MACHEREYNAGEL, Düren, Germany), according to the manufacturer’s instructions.

Techniques: SDS Page, Transformation Assay, Recombinant

Figure 3. Degradation of formaldehyde and production of formic acid and methanol by resting cells of E. coli transformed with the FD1 formaldehyde dismutase gene and decrease in viable cells of the recombinant E. coli. The reaction mixture contained 1 OD-unit/mL of the cells. The solid lines, the recombinant E. coli with pRham-FDM; the dashed line, the recombinant E. coli with pRham (no insert); Closed circles, formaldehyde; closed triangles, formic acid; closed squares, methanol; open circles, viable cells of the recombinant E. coli in the buffer with 0.33 M formaldehyde; open triangles viable cells of the recombinant E. coli in the buffer without formaldehyde. Experimental conditions are specified in Materials and methods. All experiments were performed in triplicates, and the mean ± standard deviation is shown.

Journal: Bioscience, biotechnology, and biochemistry

Article Title: Biodegradation of high concentrations of formaldehyde using Escherichia coli expressing the formaldehyde dismutase gene of Methylobacterium sp. FD1.

doi: 10.1080/09168451.2017.1397497

Figure Lengend Snippet: Figure 3. Degradation of formaldehyde and production of formic acid and methanol by resting cells of E. coli transformed with the FD1 formaldehyde dismutase gene and decrease in viable cells of the recombinant E. coli. The reaction mixture contained 1 OD-unit/mL of the cells. The solid lines, the recombinant E. coli with pRham-FDM; the dashed line, the recombinant E. coli with pRham (no insert); Closed circles, formaldehyde; closed triangles, formic acid; closed squares, methanol; open circles, viable cells of the recombinant E. coli in the buffer with 0.33 M formaldehyde; open triangles viable cells of the recombinant E. coli in the buffer without formaldehyde. Experimental conditions are specified in Materials and methods. All experiments were performed in triplicates, and the mean ± standard deviation is shown.

Article Snippet: Polymerase chain reaction (PCR) amplification of the formaldehyde dismutase gene of Methylobacterium sp. FD1 Genomic DNA was extracted from FD1 cells cultured in tryptic soy broth using NucleoSpin® Tissue (MACHEREYNAGEL, Düren, Germany), according to the manufacturer’s instructions.

Techniques: Transformation Assay, Recombinant, Standard Deviation

Figure 5 Amino acid alignment of the formaldehyde dismutase of FD1 with (putative) enzymes related to formaldehyde dismutase. The sequences used for the alignment are as follows: MspFD1-FDM, formaldehyde dismutase of Methylobacterium sp. FD1 (accession No. LS269930) in class Alphaproteobacteria; CspSK3-ADM, putative aldehyde dismutase of Cupriavidus sp. SK-3 (WP_051648669) in class Betaproteobacteria; Tbo-ADM, putative aldehyde dismutase of T. bouteillei (WP_038092476) in class Cyanobacteria; MspGXS13- ADM, putative aldehyde dismutase of Methylobacterium sp. GXS13 (WP_058191240) in class Alphaproteobacteria; Pbo-FDH, putative glutathione-independent formaldehyde dehydrogenase of P. borealis (WP_076349806) in class Planctomycetia; Rsp-ADM, putative aldehyde dismutase of Rhodococcus spp. (WP_003943355) in class Actinobacteria; SspTu6071-ADM, putative aldehyde dismutase of Streptomyces sp. Tu6071 (WP_043257889) in class Actinobacteria; Fsp-ADM, putative aldehyde dismutase of Flavobacteriaceae (WP_027374817) in class Flavobacteriia; PpuF61-FDM, formaldehyde dismutase of P. putida F61 (L25862) of Gammaproteobacteria; PpuC83-FDH, glutathione-independent formaldehyde dehydrogenase of P. putida C83 (D21201) of Gammaproteobacteria. Identical residues in all of the (putative) enzymes are indicated by black highlight. Asterisks, the NAD(H)-binding residues; open circles, catalytic zinc-binding residues; closed circles, structural zinc-binding residues of the glutathione-independent formaldehyde dehydrogenase of P. putida C83 [2].

Journal: Bioscience, biotechnology, and biochemistry

Article Title: Biodegradation of high concentrations of formaldehyde using Escherichia coli expressing the formaldehyde dismutase gene of Methylobacterium sp. FD1.

doi: 10.1080/09168451.2017.1397497

Figure Lengend Snippet: Figure 5 Amino acid alignment of the formaldehyde dismutase of FD1 with (putative) enzymes related to formaldehyde dismutase. The sequences used for the alignment are as follows: MspFD1-FDM, formaldehyde dismutase of Methylobacterium sp. FD1 (accession No. LS269930) in class Alphaproteobacteria; CspSK3-ADM, putative aldehyde dismutase of Cupriavidus sp. SK-3 (WP_051648669) in class Betaproteobacteria; Tbo-ADM, putative aldehyde dismutase of T. bouteillei (WP_038092476) in class Cyanobacteria; MspGXS13- ADM, putative aldehyde dismutase of Methylobacterium sp. GXS13 (WP_058191240) in class Alphaproteobacteria; Pbo-FDH, putative glutathione-independent formaldehyde dehydrogenase of P. borealis (WP_076349806) in class Planctomycetia; Rsp-ADM, putative aldehyde dismutase of Rhodococcus spp. (WP_003943355) in class Actinobacteria; SspTu6071-ADM, putative aldehyde dismutase of Streptomyces sp. Tu6071 (WP_043257889) in class Actinobacteria; Fsp-ADM, putative aldehyde dismutase of Flavobacteriaceae (WP_027374817) in class Flavobacteriia; PpuF61-FDM, formaldehyde dismutase of P. putida F61 (L25862) of Gammaproteobacteria; PpuC83-FDH, glutathione-independent formaldehyde dehydrogenase of P. putida C83 (D21201) of Gammaproteobacteria. Identical residues in all of the (putative) enzymes are indicated by black highlight. Asterisks, the NAD(H)-binding residues; open circles, catalytic zinc-binding residues; closed circles, structural zinc-binding residues of the glutathione-independent formaldehyde dehydrogenase of P. putida C83 [2].

Article Snippet: Polymerase chain reaction (PCR) amplification of the formaldehyde dismutase gene of Methylobacterium sp. FD1 Genomic DNA was extracted from FD1 cells cultured in tryptic soy broth using NucleoSpin® Tissue (MACHEREYNAGEL, Düren, Germany), according to the manufacturer’s instructions.

Techniques: Binding Assay

Figure 6. Degradation of high concentrations of formaldehyde by resting and lyophilized cells of E. coli transformed with the formaldehyde dismutase gene of FD1. (A) Resting cells. The reaction mixture contained 1 OD-unit/mL (circles) and 2 OD-units/mL (triangles) of the cells. (B) Lyophilized cells. The reaction mixture contained 1 OD-unit/mL (circles), 2 OD-units/mL (triangles), 5 OD- units/mL (squares), and 10 OD-units/mL (diamonds) of the cells. Experimental conditions are specified in Materials and methods. All experiments were performed in triplicates, and the mean ± standard deviation is shown.

Journal: Bioscience, biotechnology, and biochemistry

Article Title: Biodegradation of high concentrations of formaldehyde using Escherichia coli expressing the formaldehyde dismutase gene of Methylobacterium sp. FD1.

doi: 10.1080/09168451.2017.1397497

Figure Lengend Snippet: Figure 6. Degradation of high concentrations of formaldehyde by resting and lyophilized cells of E. coli transformed with the formaldehyde dismutase gene of FD1. (A) Resting cells. The reaction mixture contained 1 OD-unit/mL (circles) and 2 OD-units/mL (triangles) of the cells. (B) Lyophilized cells. The reaction mixture contained 1 OD-unit/mL (circles), 2 OD-units/mL (triangles), 5 OD- units/mL (squares), and 10 OD-units/mL (diamonds) of the cells. Experimental conditions are specified in Materials and methods. All experiments were performed in triplicates, and the mean ± standard deviation is shown.

Article Snippet: Polymerase chain reaction (PCR) amplification of the formaldehyde dismutase gene of Methylobacterium sp. FD1 Genomic DNA was extracted from FD1 cells cultured in tryptic soy broth using NucleoSpin® Tissue (MACHEREYNAGEL, Düren, Germany), according to the manufacturer’s instructions.

Techniques: Transformation Assay, Standard Deviation