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b1a  (ATCC)
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ATCC b1a
Comparison of the production of avermectin <t> B1a </t> and its analogs by fermentation of wild‐type and mutants of ZJAV‐Y‐147 and ZJAV‐Y‐HS at 28°C in a water bath shaker for 240 h at 250 r/min
B1a, supplied by ATCC, 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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usp21 cdna  (Addgene inc)
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Addgene inc usp21 cdna
( a ) Immunoblot of lysates from HEK 293T cells transfected with S-tagged versions of mouse USP18 (mUSP18), mouse USP18 with the active site cysteine replaced by alanine (mUSP18 C61A), human <t>USP21</t> (hUSP21), zebrafish USP18 ( dr USP18) and zebrafish USP18 with the active site cysteine replaced by an alanine ( dr USP18 C38A) or from untransfected cells (control). Protein expression was visualized with an antibody directed against the S tag. ( b ) Immunoblot of lysates from cells transfected with the indicated expression constructs, incubated with the active site–directed probe ISG15-PA. Complex formation was monitored on the basis of a size shift detected with an anti-S-tag antibody. ( c ) Immunoblot analyses of protein lysates from cells transfected with the indicated expression constructs, incubated with the active site–directed probe Ub-PA. Complex formation was monitored on the basis of a size shift detected with an anti-S-tag antibody. USP21 is cross-reactive for ISG15, and ubiquitin served as a positive control for Ub binding. Results shown in a – c are representative of three independent experiments.
Usp21 Cdna, supplied by Addgene inc, 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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Comparison of the production of avermectin B1a and its analogs by fermentation of wild‐type and mutants of ZJAV‐Y‐147 and ZJAV‐Y‐HS at 28°C in a water bath shaker for 240 h at 250 r/min

Journal: Engineering in Life Sciences

Article Title: Effects of heavy‐ion beam irradiation on avermectin B1a and its analogues production by Streptomyces avermitilis

doi: 10.1002/elsc.201800094

Figure Lengend Snippet: Comparison of the production of avermectin B1a and its analogs by fermentation of wild‐type and mutants of ZJAV‐Y‐147 and ZJAV‐Y‐HS at 28°C in a water bath shaker for 240 h at 250 r/min

Article Snippet: In the same way, the production of an industrial overproducer increased from 3582 to 4450 mg/L and improved by 24%. table ft1 table-wrap mode="anchored" t5 Table 2 caption a7 Production of time (h), avermectin B1a and its analogs (μg/mL) S. avermitilis Avermectin 48 h 72 h 96 h 120 h 144 h 168 h 192 h 216 h 240 h ATCC 31267 (Wild‐type) B2b 178.64 111.63 25.71 40.51 30.64 48.39 55.45 67.97 105.23 B2a – 89.43 462.32 675.12 581.52 814.49 567.46 1401.23 1026.67 A2b 82.24 90.62 – – – – 24.67 64.27 145.92 A2a 106.19 315.94 630.7 771.45 407.23 842.39 1115.24 1267.36 1326.76 B1b – 56.53 119.62 190.73 153.05 197.08 186.91 243.89 391.93 B1a 42.12 180.93 346.30 521.64 730.92 965.83 1312.53 1827.6 2335.6 ZJAV‐Y‐147 (Mutant) A1a 88.96 79.33 190.24 239.23 233.52 318.65 404.43 511.52 711.37 B2b 179.56 91.56 – – – – 50.84 69.49 100.83 B2a – 95.17 407.63 423.42 476.25 563.09 946.28 1204.25 1726.23 A2b 30.68 93.62 – – – 19.72 52.08 119.92 152.56 A2a 56.78 323.24 490.73 662.47 575.43 681.14 1134.76 1290.72 1810.62 B1b – – 95.59 124.83 141.89 160.36 242.16 295.36 390.73 B1a 63.91 281.12 798.14 1621.23 2465.62 2676.43 3434.85 3835.24 4822.23 ZJAV‐Y‐HS (Mutant) A1a – 79.33 186.93 205.79 231.65 286.21 429.28 541.39 733.26 B2b 162.83 233.99 – – – – 78.22 96.76 121.37 B2a – 186.37 516.34 806.13 1109.33 114.45 1451.16 1677.26 1901.66 A2b 28.63 – – – – – 157.49 166.99 167.45 A2a 52.06 349.49 621.27 1258.34 1367.34 1348.24 1743.66 1801.84 1994.85 B1b – – 121.76 236.24 331.74 317.39 371.49 460.67 428.22 B1a 48.88 313.79 836.16 1558.89 2194.86 2487.87 3123.41 3694.18 4632.17 A1a – 110.22 236.63 393.34 547.89 566.47 658.87 755.74 826.73 Open in a separate window Comparison of the production of avermectin B1a and its analogs by fermentation of wild‐type and mutants of ZJAV‐Y‐147 and ZJAV‐Y‐HS at 28°C in a water bath shaker for 240 h at 250 r/min Among other analogue parameters studied here, the results demonstrated that the mutants ZJAV‐Y‐147 and ZJAV‐Y‐HS produced maximal levels of avermectin B1a after 240 h of fermentation in a medium of pH 7.5 using 5% (v/v) inoculum medium.

Techniques: Mutagenesis

Values of AVMs B1a and Total AVMS for wild‐type and mutants of ZJAV‐Y‐147 and ZJAV‐Y‐HS mutants for different subcultures ( n = 5)

Journal: Engineering in Life Sciences

Article Title: Effects of heavy‐ion beam irradiation on avermectin B1a and its analogues production by Streptomyces avermitilis

doi: 10.1002/elsc.201800094

Figure Lengend Snippet: Values of AVMs B1a and Total AVMS for wild‐type and mutants of ZJAV‐Y‐147 and ZJAV‐Y‐HS mutants for different subcultures ( n = 5)

Article Snippet: In the same way, the production of an industrial overproducer increased from 3582 to 4450 mg/L and improved by 24%. table ft1 table-wrap mode="anchored" t5 Table 2 caption a7 Production of time (h), avermectin B1a and its analogs (μg/mL) S. avermitilis Avermectin 48 h 72 h 96 h 120 h 144 h 168 h 192 h 216 h 240 h ATCC 31267 (Wild‐type) B2b 178.64 111.63 25.71 40.51 30.64 48.39 55.45 67.97 105.23 B2a – 89.43 462.32 675.12 581.52 814.49 567.46 1401.23 1026.67 A2b 82.24 90.62 – – – – 24.67 64.27 145.92 A2a 106.19 315.94 630.7 771.45 407.23 842.39 1115.24 1267.36 1326.76 B1b – 56.53 119.62 190.73 153.05 197.08 186.91 243.89 391.93 B1a 42.12 180.93 346.30 521.64 730.92 965.83 1312.53 1827.6 2335.6 ZJAV‐Y‐147 (Mutant) A1a 88.96 79.33 190.24 239.23 233.52 318.65 404.43 511.52 711.37 B2b 179.56 91.56 – – – – 50.84 69.49 100.83 B2a – 95.17 407.63 423.42 476.25 563.09 946.28 1204.25 1726.23 A2b 30.68 93.62 – – – 19.72 52.08 119.92 152.56 A2a 56.78 323.24 490.73 662.47 575.43 681.14 1134.76 1290.72 1810.62 B1b – – 95.59 124.83 141.89 160.36 242.16 295.36 390.73 B1a 63.91 281.12 798.14 1621.23 2465.62 2676.43 3434.85 3835.24 4822.23 ZJAV‐Y‐HS (Mutant) A1a – 79.33 186.93 205.79 231.65 286.21 429.28 541.39 733.26 B2b 162.83 233.99 – – – – 78.22 96.76 121.37 B2a – 186.37 516.34 806.13 1109.33 114.45 1451.16 1677.26 1901.66 A2b 28.63 – – – – – 157.49 166.99 167.45 A2a 52.06 349.49 621.27 1258.34 1367.34 1348.24 1743.66 1801.84 1994.85 B1b – – 121.76 236.24 331.74 317.39 371.49 460.67 428.22 B1a 48.88 313.79 836.16 1558.89 2194.86 2487.87 3123.41 3694.18 4632.17 A1a – 110.22 236.63 393.34 547.89 566.47 658.87 755.74 826.73 Open in a separate window Comparison of the production of avermectin B1a and its analogs by fermentation of wild‐type and mutants of ZJAV‐Y‐147 and ZJAV‐Y‐HS at 28°C in a water bath shaker for 240 h at 250 r/min Among other analogue parameters studied here, the results demonstrated that the mutants ZJAV‐Y‐147 and ZJAV‐Y‐HS produced maximal levels of avermectin B1a after 240 h of fermentation in a medium of pH 7.5 using 5% (v/v) inoculum medium.

Techniques:

( a ) Immunoblot of lysates from HEK 293T cells transfected with S-tagged versions of mouse USP18 (mUSP18), mouse USP18 with the active site cysteine replaced by alanine (mUSP18 C61A), human USP21 (hUSP21), zebrafish USP18 ( dr USP18) and zebrafish USP18 with the active site cysteine replaced by an alanine ( dr USP18 C38A) or from untransfected cells (control). Protein expression was visualized with an antibody directed against the S tag. ( b ) Immunoblot of lysates from cells transfected with the indicated expression constructs, incubated with the active site–directed probe ISG15-PA. Complex formation was monitored on the basis of a size shift detected with an anti-S-tag antibody. ( c ) Immunoblot analyses of protein lysates from cells transfected with the indicated expression constructs, incubated with the active site–directed probe Ub-PA. Complex formation was monitored on the basis of a size shift detected with an anti-S-tag antibody. USP21 is cross-reactive for ISG15, and ubiquitin served as a positive control for Ub binding. Results shown in a – c are representative of three independent experiments.

Journal: Nature Structural & Molecular Biology

Article Title: Structural basis of the specificity of USP18 toward ISG15

doi: 10.1038/nsmb.3371

Figure Lengend Snippet: ( a ) Immunoblot of lysates from HEK 293T cells transfected with S-tagged versions of mouse USP18 (mUSP18), mouse USP18 with the active site cysteine replaced by alanine (mUSP18 C61A), human USP21 (hUSP21), zebrafish USP18 ( dr USP18) and zebrafish USP18 with the active site cysteine replaced by an alanine ( dr USP18 C38A) or from untransfected cells (control). Protein expression was visualized with an antibody directed against the S tag. ( b ) Immunoblot of lysates from cells transfected with the indicated expression constructs, incubated with the active site–directed probe ISG15-PA. Complex formation was monitored on the basis of a size shift detected with an anti-S-tag antibody. ( c ) Immunoblot analyses of protein lysates from cells transfected with the indicated expression constructs, incubated with the active site–directed probe Ub-PA. Complex formation was monitored on the basis of a size shift detected with an anti-S-tag antibody. USP21 is cross-reactive for ISG15, and ubiquitin served as a positive control for Ub binding. Results shown in a – c are representative of three independent experiments.

Article Snippet: The vector pTriEx2-USP21cd encoding residues 197–565 of human USP21 was generated by amplification of USP21 cDNA from the vector Flag-HA-USP21 (Addgene) with the primers KpnI-USP21cd-for and XhoI-USP21cd-rev.

Techniques: Western Blot, Transfection, Expressing, Construct, Incubation, Positive Control, Binding Assay