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hca ii  (R&D Systems)


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    R&D Systems hca ii
    Hca Ii, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/hca+ii/Recombinant+Human+Carbonic+Anhydrase+II+Protein%2C+CF/pmc12455828-115-34-40
    Average 94 stars, based on 3 article reviews
    hca ii - by Bioz Stars, 2026-09
    94/100 stars

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    Recombinant:

    Article Title: Sustainable leads for hypoxic tumor therapy: allosteric selective inhibition of carbonic anhydrase IX by abietane-type resin acids
    Article Snippet: .. Recombinant human carbonic anhydrase IX catalytic domain (hCA IX; residues 59– 414, C-terminal His10 tag), hCA I (Ala 2–Phe261) and hCA II (Ser2– Lys260) were purchased from R&D Systems (Minneapolis, MN, USA) at >95% purity. .. 4-Nitrophenyl acetate (4-NPA, $98%), bromothymol blue, HEPES, tris, sodium sulfate, dimethylsulfoxide (DMSO), acetazolamide (AAZ) and all other analytical-grade chemicals came from Sigma-Aldrich/Merck.

    Article Title: Sustainable leads for hypoxic tumor therapy: allosteric selective inhibition of carbonic anhydrase IX by abietane-type resin acids
    Article Snippet: .. Recombinant human carbonic anhydrase IX catalytic domain (hCA IX; residues 59–414, C-terminal His 10 tag), hCA I (Ala 2 –Phe 261 ) and hCA II (Ser 2 –Lys 260 ) were purchased from R&D Systems (Minneapolis, MN, USA) at >95% purity. .. 4-Nitrophenyl acetate (4-NPA, ≥98%), bromothymol blue, HEPES, tris, sodium sulfate, dimethyl-sulfoxide (DMSO), acetazolamide (AAZ) and all other analytical-grade chemicals came from Sigma-Aldrich/Merck.

    Article Title: Entrance-channel plugging by natural sulfonamide antibiotics yields isoform-selective carbonic anhydrase IX inhibitors: an integrated in silico / in vitro discovery of the lead SB-203207
    Article Snippet: .. Recombinant catalytic domains of human CA IX (residues 59–414, C-terminal His10 tag), CA I and CA II (all ≥ 95% purity; R&D Systems, Minneapolis, USA) were employed as enzyme sources. hCA I (Ala2–Phe261) and hCA II (Ser2–Lys260) were obtained from R&D Systems (Minneapolis, MN, USA) at > 95% purity. .. The chromogenic reporter 4-nitrophenyl acetate (pNPA, ≥ 98%), buffer components (HEPES, Tris), sodium sulfate, bromothymol blue, dimethyl-sulfoxide (DMSO) and reference inhibitor acetazolamide (AAZ) were obtained from Sigma-Aldrich/Merck, and all solutions were prepared in 18.2 MΩ cm water immediately before use.



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    Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and <t>HCA</t> <t>II:AZM</t> MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .
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    Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and <t>HCA</t> <t>II:AZM</t> MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .
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    Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and <t>HCA</t> <t>II:AZM</t> MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .
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    Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and <t>HCA</t> <t>II:AZM</t> MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .
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    Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and <t>HCA</t> <t>II:AZM</t> MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .
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    Image Search Results


    Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and HCA II:AZM MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .

    Journal: Acta Crystallographica Section D: Structural Biology

    Article Title: Limiting the effects of radiation damage in MicroED through dose selection during data processing

    doi: 10.1107/S205979832500912X

    Figure Lengend Snippet: Effect of electron dose on the strength of integrated and unmerged mean reflection intensities 〈 I 〉. The flux density is approximately 0.10 e − Å −2 s −1 (dose rate 0.45 MGy s −1 at 200 keV and 0.38 MGy s −1 at 300 keV) and the exposure time is 1.5 s per frame. ( a ) Loss of diffraction-spot strength/intensity and resolution due to radiation damage with increasing frame number. Panels (I) and (II) show the trend of intensity decay in lysozyme:native and HCA II:AZM MicroED data, respectively, collected on a Timepix detector installed on a Jeol JEM-2100 microscope operated at 200 kV. Panel (III) shows diffraction patterns of lysozyme:GdCl 3 collected on a OneView Themis Z microscope operated at 300 kV. ( b ) Intensity of diffraction spots as a function of resolution for the four data sets. 1-10F, first ten frames; 1-20F, first 20 frames; 21-35F, frame range 21–35; All F, all data. Overall, the 1-10F data set yielded reflections with higher mean intensities compared with other data sets. Data are plotted as 〈 I 〉 = mean I hkl ± standard error of the mean versus resolution for a representative 24 crystals (lysozyme:native), 16 crystals (HCA II:AZM) and nine crystals (lysozyme:GdCl 3 ). Note that in each case the same crystals are compared for the different doses. Lysozyme:native refers to native tetragonal lysozyme crystals deposited on a holey carbon grid with nylon support, HCA II:AZM refers to HCA II bound to its inhibitor acetazolamide and lastly lysozyme:GdCl 3 refers to lysozyme soaked in GdCl 3 .

    Article Snippet: MicroED data for lysozyme:native, lysozyme:Na_I 3 C, lysozyme:Gd, HCA II and HCA II:AZM were collected on a Jeol JEM-2100 transmission electron microscope with a LaB 6 filament operated at 200 kV, equipped with a hybrid electron detector (Amsterdam Scientific Instruments, Timepix).

    Techniques: Microscopy

    Site-specific damage of aspartic and glutamic acids in the HCA II:AZM protein complex. The 2 mF o − DF c maps are shown as blue meshes with a contour level of 1.5σ above the mean. The mF o − DF c difference densities are shown in green and red for positive and negative density, respectively, contoured at 3.0σ above and below the mean. A section covering 2 Å around atoms is shown for all densities. The electron doses are as specified in the figure.

    Journal: Acta Crystallographica Section D: Structural Biology

    Article Title: Limiting the effects of radiation damage in MicroED through dose selection during data processing

    doi: 10.1107/S205979832500912X

    Figure Lengend Snippet: Site-specific damage of aspartic and glutamic acids in the HCA II:AZM protein complex. The 2 mF o − DF c maps are shown as blue meshes with a contour level of 1.5σ above the mean. The mF o − DF c difference densities are shown in green and red for positive and negative density, respectively, contoured at 3.0σ above and below the mean. A section covering 2 Å around atoms is shown for all densities. The electron doses are as specified in the figure.

    Article Snippet: MicroED data for lysozyme:native, lysozyme:Na_I 3 C, lysozyme:Gd, HCA II and HCA II:AZM were collected on a Jeol JEM-2100 transmission electron microscope with a LaB 6 filament operated at 200 kV, equipped with a hybrid electron detector (Amsterdam Scientific Instruments, Timepix).

    Techniques:

    How radiation damage affects the quality of protein–ligand binding properties. ( a ) Polar contacts between HCA II and its inhibitor AZM. ( b ) The quality of the density maps around the HCA II:AZM complex and zinc atomic B factors. 2 mF o − DF c maps are shown as blue meshes with a contour level of 1.5σ above the mean. mF o − DF c difference densities are shown in green and red for positive and negative density, respectively, contoured at 3σ above and below the mean. The 1-10F (6.75 MGy) structure shows some signs of incompleteness, while the 21-35F and All F structures exhibit signs of radiation damage as judged from 2 mF o − DF c maps and increased mF o − DF c features. The 1-20F data set is more complete with low signs of radiation damage and has the lowest isotropic B factor for the active-site zinc metal. The electron doses are as specified in the figure.

    Journal: Acta Crystallographica Section D: Structural Biology

    Article Title: Limiting the effects of radiation damage in MicroED through dose selection during data processing

    doi: 10.1107/S205979832500912X

    Figure Lengend Snippet: How radiation damage affects the quality of protein–ligand binding properties. ( a ) Polar contacts between HCA II and its inhibitor AZM. ( b ) The quality of the density maps around the HCA II:AZM complex and zinc atomic B factors. 2 mF o − DF c maps are shown as blue meshes with a contour level of 1.5σ above the mean. mF o − DF c difference densities are shown in green and red for positive and negative density, respectively, contoured at 3σ above and below the mean. The 1-10F (6.75 MGy) structure shows some signs of incompleteness, while the 21-35F and All F structures exhibit signs of radiation damage as judged from 2 mF o − DF c maps and increased mF o − DF c features. The 1-20F data set is more complete with low signs of radiation damage and has the lowest isotropic B factor for the active-site zinc metal. The electron doses are as specified in the figure.

    Article Snippet: MicroED data for lysozyme:native, lysozyme:Na_I 3 C, lysozyme:Gd, HCA II and HCA II:AZM were collected on a Jeol JEM-2100 transmission electron microscope with a LaB 6 filament operated at 200 kV, equipped with a hybrid electron detector (Amsterdam Scientific Instruments, Timepix).

    Techniques: Ligand Binding Assay