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  • 99
    Thermo Fisher protein a sepharose beads
    RSV promotes NLRC5 expression in A549 cells through IFN-β secretion. (A and B) Conditioned medium contains NLRC5-inducing activity. (A) A conditioned medium from RSV-infected A549 cells (CM-RSV A549) was UV irradiated to deactivate RSV (+UV), heat inactivated (HK), or left untreated (−UV). The medium was then mixed with fresh DMEM at a 10% ratio and used to treat A549 cells. (B) Dose response of NLRC5 induction to the conditioned medium. UV-irradiated conditioned medium was mixed with fresh DMEM at various ratios (percent [vol/vol]) and used to treat A549 cells. NLRC5 induction was determined by Western blotting. The expression of viral F protein was determined to show the effect of UV irradiation or heat deactivation on infectious virions. The experiment was performed two times independently. (C) Induction of NLRC5 by recombinant interferons. A549 cells were treated with IFN-β (100 U/ml), IFN-γ (100 U/ml), and IL-28B or IL-29 (10, 30, and 100 ng/ml) for 24 h. Cells were harvested, and NLRC5 induction was detected by Western blotting. GAPDH expression was used as an internal control. (D) Time course of NLRC5 induction by recombinant IFN-β. A549 cells were treated with recombinant IFN-β at 100 U for the indicated times. NLRC5 induction was determined by immunoblotting. GAPDH was the loading control. (E) Immunodepletion of IFN-β removes NLRC5-inducing activity. Aliquots (100 μl) of UV-irradiated conditioned medium were left untreated or incubated at 4°C with anti-IFN-β (10 μg/ml and 30 μg/ml) or anti-IFN-γ (30 μg/ml) for 60 min. The immunocomplexes were removed by protein <t>A-Sepharose</t> beads. The supernatants were mixed with fresh DMEM at 5% (vol/vol) and tested on A549 cells for NLRC5-inducing activity. The results are representative of two independent experiments. GAPDH was used as a loading control. Tx, treatment. (F) Suppression of NLRC5 expression inhibits NLRC5 and MHC-I induction by IFN-β. A549 cells were transfected with scrambled control or with siNLRC5 number 1 (10, 20, or 30 nM) for 24 h. The cells were then treated with 100 U of IFN-β for 24 h. NLRC5 and MHC-I expression was determined by Western blotting. GAPDH expression was the loading control.
    Protein A Sepharose Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2270 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Thermo Fisher nab protein
    RSV promotes NLRC5 expression in A549 cells through IFN-β secretion. (A and B) Conditioned medium contains NLRC5-inducing activity. (A) A conditioned medium from RSV-infected A549 cells (CM-RSV A549) was UV irradiated to deactivate RSV (+UV), heat inactivated (HK), or left untreated (−UV). The medium was then mixed with fresh DMEM at a 10% ratio and used to treat A549 cells. (B) Dose response of NLRC5 induction to the conditioned medium. UV-irradiated conditioned medium was mixed with fresh DMEM at various ratios (percent [vol/vol]) and used to treat A549 cells. NLRC5 induction was determined by Western blotting. The expression of viral F protein was determined to show the effect of UV irradiation or heat deactivation on infectious virions. The experiment was performed two times independently. (C) Induction of NLRC5 by recombinant interferons. A549 cells were treated with IFN-β (100 U/ml), IFN-γ (100 U/ml), and IL-28B or IL-29 (10, 30, and 100 ng/ml) for 24 h. Cells were harvested, and NLRC5 induction was detected by Western blotting. GAPDH expression was used as an internal control. (D) Time course of NLRC5 induction by recombinant IFN-β. A549 cells were treated with recombinant IFN-β at 100 U for the indicated times. NLRC5 induction was determined by immunoblotting. GAPDH was the loading control. (E) Immunodepletion of IFN-β removes NLRC5-inducing activity. Aliquots (100 μl) of UV-irradiated conditioned medium were left untreated or incubated at 4°C with anti-IFN-β (10 μg/ml and 30 μg/ml) or anti-IFN-γ (30 μg/ml) for 60 min. The immunocomplexes were removed by protein <t>A-Sepharose</t> beads. The supernatants were mixed with fresh DMEM at 5% (vol/vol) and tested on A549 cells for NLRC5-inducing activity. The results are representative of two independent experiments. GAPDH was used as a loading control. Tx, treatment. (F) Suppression of NLRC5 expression inhibits NLRC5 and MHC-I induction by IFN-β. A549 cells were transfected with scrambled control or with siNLRC5 number 1 (10, 20, or 30 nM) for 24 h. The cells were then treated with 100 U of IFN-β for 24 h. NLRC5 and MHC-I expression was determined by Western blotting. GAPDH expression was the loading control.
    Nab Protein, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher sybr gold nucleic acid gel stain
    RSV promotes NLRC5 expression in A549 cells through IFN-β secretion. (A and B) Conditioned medium contains NLRC5-inducing activity. (A) A conditioned medium from RSV-infected A549 cells (CM-RSV A549) was UV irradiated to deactivate RSV (+UV), heat inactivated (HK), or left untreated (−UV). The medium was then mixed with fresh DMEM at a 10% ratio and used to treat A549 cells. (B) Dose response of NLRC5 induction to the conditioned medium. UV-irradiated conditioned medium was mixed with fresh DMEM at various ratios (percent [vol/vol]) and used to treat A549 cells. NLRC5 induction was determined by Western blotting. The expression of viral F protein was determined to show the effect of UV irradiation or heat deactivation on infectious virions. The experiment was performed two times independently. (C) Induction of NLRC5 by recombinant interferons. A549 cells were treated with IFN-β (100 U/ml), IFN-γ (100 U/ml), and IL-28B or IL-29 (10, 30, and 100 ng/ml) for 24 h. Cells were harvested, and NLRC5 induction was detected by Western blotting. GAPDH expression was used as an internal control. (D) Time course of NLRC5 induction by recombinant IFN-β. A549 cells were treated with recombinant IFN-β at 100 U for the indicated times. NLRC5 induction was determined by immunoblotting. GAPDH was the loading control. (E) Immunodepletion of IFN-β removes NLRC5-inducing activity. Aliquots (100 μl) of UV-irradiated conditioned medium were left untreated or incubated at 4°C with anti-IFN-β (10 μg/ml and 30 μg/ml) or anti-IFN-γ (30 μg/ml) for 60 min. The immunocomplexes were removed by protein <t>A-Sepharose</t> beads. The supernatants were mixed with fresh DMEM at 5% (vol/vol) and tested on A549 cells for NLRC5-inducing activity. The results are representative of two independent experiments. GAPDH was used as a loading control. Tx, treatment. (F) Suppression of NLRC5 expression inhibits NLRC5 and MHC-I induction by IFN-β. A549 cells were transfected with scrambled control or with siNLRC5 number 1 (10, 20, or 30 nM) for 24 h. The cells were then treated with 100 U of IFN-β for 24 h. NLRC5 and MHC-I expression was determined by Western blotting. GAPDH expression was the loading control.
    Sybr Gold Nucleic Acid Gel Stain, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2937 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Agilent technologies 1100 series lc msd trap vl mass spectrometer
    RSV promotes NLRC5 expression in A549 cells through IFN-β secretion. (A and B) Conditioned medium contains NLRC5-inducing activity. (A) A conditioned medium from RSV-infected A549 cells (CM-RSV A549) was UV irradiated to deactivate RSV (+UV), heat inactivated (HK), or left untreated (−UV). The medium was then mixed with fresh DMEM at a 10% ratio and used to treat A549 cells. (B) Dose response of NLRC5 induction to the conditioned medium. UV-irradiated conditioned medium was mixed with fresh DMEM at various ratios (percent [vol/vol]) and used to treat A549 cells. NLRC5 induction was determined by Western blotting. The expression of viral F protein was determined to show the effect of UV irradiation or heat deactivation on infectious virions. The experiment was performed two times independently. (C) Induction of NLRC5 by recombinant interferons. A549 cells were treated with IFN-β (100 U/ml), IFN-γ (100 U/ml), and IL-28B or IL-29 (10, 30, and 100 ng/ml) for 24 h. Cells were harvested, and NLRC5 induction was detected by Western blotting. GAPDH expression was used as an internal control. (D) Time course of NLRC5 induction by recombinant IFN-β. A549 cells were treated with recombinant IFN-β at 100 U for the indicated times. NLRC5 induction was determined by immunoblotting. GAPDH was the loading control. (E) Immunodepletion of IFN-β removes NLRC5-inducing activity. Aliquots (100 μl) of UV-irradiated conditioned medium were left untreated or incubated at 4°C with anti-IFN-β (10 μg/ml and 30 μg/ml) or anti-IFN-γ (30 μg/ml) for 60 min. The immunocomplexes were removed by protein <t>A-Sepharose</t> beads. The supernatants were mixed with fresh DMEM at 5% (vol/vol) and tested on A549 cells for NLRC5-inducing activity. The results are representative of two independent experiments. GAPDH was used as a loading control. Tx, treatment. (F) Suppression of NLRC5 expression inhibits NLRC5 and MHC-I induction by IFN-β. A549 cells were transfected with scrambled control or with siNLRC5 number 1 (10, 20, or 30 nM) for 24 h. The cells were then treated with 100 U of IFN-β for 24 h. NLRC5 and MHC-I expression was determined by Western blotting. GAPDH expression was the loading control.
    1100 Series Lc Msd Trap Vl Mass Spectrometer, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 99/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher protein l chromatography
    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over <t>protein</t> L or protein A columns, and single Fab fragments or Fc fragments were collected,
    Protein L Chromatography, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pcr  (Qiagen)
    99
    Qiagen pcr
    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over <t>protein</t> L or protein A columns, and single Fab fragments or Fc fragments were collected,
    Pcr, supplied by Qiagen, used in various techniques. Bioz Stars score: 99/100, based on 35685 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher spin purification kit
    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over <t>protein</t> L or protein A columns, and single Fab fragments or Fc fragments were collected,
    Spin Purification Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher revertaid h minus first strand cdna synthesis kit
    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over <t>protein</t> L or protein A columns, and single Fab fragments or Fc fragments were collected,
    Revertaid H Minus First Strand Cdna Synthesis Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 9555 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    STATA Corporation stata version 13 1
    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over <t>protein</t> L or protein A columns, and single Fab fragments or Fc fragments were collected,
    Stata Version 13 1, supplied by STATA Corporation, used in various techniques. Bioz Stars score: 93/100, based on 2819 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Delsys 16 channel trigno wireless system
    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over <t>protein</t> L or protein A columns, and single Fab fragments or Fc fragments were collected,
    16 Channel Trigno Wireless System, supplied by Delsys, used in various techniques. Bioz Stars score: 91/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Agilent technologies 5975c vl msd
    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over <t>protein</t> L or protein A columns, and single Fab fragments or Fc fragments were collected,
    5975c Vl Msd, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 88/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare akta fplc system
    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over <t>protein</t> L or protein A columns, and single Fab fragments or Fc fragments were collected,
    Akta Fplc System, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 6156 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher antibody library
    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over <t>protein</t> L or protein A columns, and single Fab fragments or Fc fragments were collected,
    Antibody Library, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    DiaSorin anti hcv
    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over <t>protein</t> L or protein A columns, and single Fab fragments or Fc fragments were collected,
    Anti Hcv, supplied by DiaSorin, used in various techniques. Bioz Stars score: 92/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    RSV promotes NLRC5 expression in A549 cells through IFN-β secretion. (A and B) Conditioned medium contains NLRC5-inducing activity. (A) A conditioned medium from RSV-infected A549 cells (CM-RSV A549) was UV irradiated to deactivate RSV (+UV), heat inactivated (HK), or left untreated (−UV). The medium was then mixed with fresh DMEM at a 10% ratio and used to treat A549 cells. (B) Dose response of NLRC5 induction to the conditioned medium. UV-irradiated conditioned medium was mixed with fresh DMEM at various ratios (percent [vol/vol]) and used to treat A549 cells. NLRC5 induction was determined by Western blotting. The expression of viral F protein was determined to show the effect of UV irradiation or heat deactivation on infectious virions. The experiment was performed two times independently. (C) Induction of NLRC5 by recombinant interferons. A549 cells were treated with IFN-β (100 U/ml), IFN-γ (100 U/ml), and IL-28B or IL-29 (10, 30, and 100 ng/ml) for 24 h. Cells were harvested, and NLRC5 induction was detected by Western blotting. GAPDH expression was used as an internal control. (D) Time course of NLRC5 induction by recombinant IFN-β. A549 cells were treated with recombinant IFN-β at 100 U for the indicated times. NLRC5 induction was determined by immunoblotting. GAPDH was the loading control. (E) Immunodepletion of IFN-β removes NLRC5-inducing activity. Aliquots (100 μl) of UV-irradiated conditioned medium were left untreated or incubated at 4°C with anti-IFN-β (10 μg/ml and 30 μg/ml) or anti-IFN-γ (30 μg/ml) for 60 min. The immunocomplexes were removed by protein A-Sepharose beads. The supernatants were mixed with fresh DMEM at 5% (vol/vol) and tested on A549 cells for NLRC5-inducing activity. The results are representative of two independent experiments. GAPDH was used as a loading control. Tx, treatment. (F) Suppression of NLRC5 expression inhibits NLRC5 and MHC-I induction by IFN-β. A549 cells were transfected with scrambled control or with siNLRC5 number 1 (10, 20, or 30 nM) for 24 h. The cells were then treated with 100 U of IFN-β for 24 h. NLRC5 and MHC-I expression was determined by Western blotting. GAPDH expression was the loading control.

    Journal: Journal of Virology

    Article Title: Respiratory Syncytial Virus Infection Upregulates NLRC5 and Major Histocompatibility Complex Class I Expression through RIG-I Induction in Airway Epithelial Cells

    doi: 10.1128/JVI.00349-15

    Figure Lengend Snippet: RSV promotes NLRC5 expression in A549 cells through IFN-β secretion. (A and B) Conditioned medium contains NLRC5-inducing activity. (A) A conditioned medium from RSV-infected A549 cells (CM-RSV A549) was UV irradiated to deactivate RSV (+UV), heat inactivated (HK), or left untreated (−UV). The medium was then mixed with fresh DMEM at a 10% ratio and used to treat A549 cells. (B) Dose response of NLRC5 induction to the conditioned medium. UV-irradiated conditioned medium was mixed with fresh DMEM at various ratios (percent [vol/vol]) and used to treat A549 cells. NLRC5 induction was determined by Western blotting. The expression of viral F protein was determined to show the effect of UV irradiation or heat deactivation on infectious virions. The experiment was performed two times independently. (C) Induction of NLRC5 by recombinant interferons. A549 cells were treated with IFN-β (100 U/ml), IFN-γ (100 U/ml), and IL-28B or IL-29 (10, 30, and 100 ng/ml) for 24 h. Cells were harvested, and NLRC5 induction was detected by Western blotting. GAPDH expression was used as an internal control. (D) Time course of NLRC5 induction by recombinant IFN-β. A549 cells were treated with recombinant IFN-β at 100 U for the indicated times. NLRC5 induction was determined by immunoblotting. GAPDH was the loading control. (E) Immunodepletion of IFN-β removes NLRC5-inducing activity. Aliquots (100 μl) of UV-irradiated conditioned medium were left untreated or incubated at 4°C with anti-IFN-β (10 μg/ml and 30 μg/ml) or anti-IFN-γ (30 μg/ml) for 60 min. The immunocomplexes were removed by protein A-Sepharose beads. The supernatants were mixed with fresh DMEM at 5% (vol/vol) and tested on A549 cells for NLRC5-inducing activity. The results are representative of two independent experiments. GAPDH was used as a loading control. Tx, treatment. (F) Suppression of NLRC5 expression inhibits NLRC5 and MHC-I induction by IFN-β. A549 cells were transfected with scrambled control or with siNLRC5 number 1 (10, 20, or 30 nM) for 24 h. The cells were then treated with 100 U of IFN-β for 24 h. NLRC5 and MHC-I expression was determined by Western blotting. GAPDH expression was the loading control.

    Article Snippet: After removal of the antibody with protein A-Sepharose beads (Pierce), the supernatants were mixed with complete DMEM (5% [vol/vol]) and used to treat A549 cells.

    Techniques: Expressing, Activity Assay, Infection, Irradiation, Western Blot, Recombinant, Incubation, Transfection

    (A) SDS-PAGE analysis of fibrinogen and non-cross-linked and cross-linked fibrin. Gel was stained with Coomassie blue. Positions corresponding to α, β, and γ chains of fibrin are marked. Lane 1, molecular weight markers; lane 2, fibrinogen; lane 3, non-cross-linked fibrin; lane 4, cross-linked fibrin. Protein bands with an apparent molecular mass around 97 kDa are the cross-linked γ chains. (B) Specificity of MH-1 SCA. Binding of MH-1 SCA to fibrinogen and fibrin immobilized on an ELISA plate was monitored with protein L-HRP. The initial rate of color development by measuring the absorbance change at 405 nm with time was used as an indication of MH-1 SCA specificity to the different antigens. ▴, fibrinogen; ▪, non-cross-linked fibrin; •, cross-linked fibrin.

    Journal: Applied and Environmental Microbiology

    Article Title: Functional Production and Characterization of a Fibrin-Specific Single-Chain Antibody Fragment from Bacillus subtilis: Effects of Molecular Chaperones and a Wall-Bound Protease on Antibody Fragment Production

    doi: 10.1128/AEM.68.7.3261-3269.2002

    Figure Lengend Snippet: (A) SDS-PAGE analysis of fibrinogen and non-cross-linked and cross-linked fibrin. Gel was stained with Coomassie blue. Positions corresponding to α, β, and γ chains of fibrin are marked. Lane 1, molecular weight markers; lane 2, fibrinogen; lane 3, non-cross-linked fibrin; lane 4, cross-linked fibrin. Protein bands with an apparent molecular mass around 97 kDa are the cross-linked γ chains. (B) Specificity of MH-1 SCA. Binding of MH-1 SCA to fibrinogen and fibrin immobilized on an ELISA plate was monitored with protein L-HRP. The initial rate of color development by measuring the absorbance change at 405 nm with time was used as an indication of MH-1 SCA specificity to the different antigens. ▴, fibrinogen; ▪, non-cross-linked fibrin; •, cross-linked fibrin.

    Article Snippet: MH-1 SCA in the filtrate was affinity purified using protein L-agarose (Pierce) according to the manufacturer's instructions.

    Techniques: SDS Page, Staining, Molecular Weight, Binding Assay, Enzyme-linked Immunosorbent Assay

    Importance of inactivation of wall-bound protease gene in MH-1 SCA production. Cells were cultured in super-rich medium for 6 h. Culture supernatants were trichloroacetic acid precipitated, and proteins were analyzed on an 11% polyacrylamide gel containing SDS. Amounts of samples loaded were normalized to cell density. (A) Coomassie blue-stained gel; (B) Western blot using protein L-HRP as the probing agent. Lane 1, molecular weight markers; lane 2, WB800HM[pWB980, pEPP] (this served as the negative control); lane 3, WB700NHM[pMH1, pEPP]; lane 4, WB800HM[pMH1, pEPP]. Shown are the positions of intact (∗) and degraded (•) MH-1 SCA fragments, respectively.

    Journal: Applied and Environmental Microbiology

    Article Title: Functional Production and Characterization of a Fibrin-Specific Single-Chain Antibody Fragment from Bacillus subtilis: Effects of Molecular Chaperones and a Wall-Bound Protease on Antibody Fragment Production

    doi: 10.1128/AEM.68.7.3261-3269.2002

    Figure Lengend Snippet: Importance of inactivation of wall-bound protease gene in MH-1 SCA production. Cells were cultured in super-rich medium for 6 h. Culture supernatants were trichloroacetic acid precipitated, and proteins were analyzed on an 11% polyacrylamide gel containing SDS. Amounts of samples loaded were normalized to cell density. (A) Coomassie blue-stained gel; (B) Western blot using protein L-HRP as the probing agent. Lane 1, molecular weight markers; lane 2, WB800HM[pWB980, pEPP] (this served as the negative control); lane 3, WB700NHM[pMH1, pEPP]; lane 4, WB800HM[pMH1, pEPP]. Shown are the positions of intact (∗) and degraded (•) MH-1 SCA fragments, respectively.

    Article Snippet: MH-1 SCA in the filtrate was affinity purified using protein L-agarose (Pierce) according to the manufacturer's instructions.

    Techniques: Cell Culture, Staining, Western Blot, Molecular Weight, Negative Control

    Purification of MH-1 SCA by protein L-agarose. Proteins were separated on a 12% polyacrylamide gel containing SDS and stained by Coomassie blue. Lane 1, molecular weight markers; lane 2, culture supernatant; lane 3, flow-through; lane 4, wash; lanes 5 and 6, eluates. Samples in lanes 2 to 4 were concentrated by trichloroacetic acid precipitation.

    Journal: Applied and Environmental Microbiology

    Article Title: Functional Production and Characterization of a Fibrin-Specific Single-Chain Antibody Fragment from Bacillus subtilis: Effects of Molecular Chaperones and a Wall-Bound Protease on Antibody Fragment Production

    doi: 10.1128/AEM.68.7.3261-3269.2002

    Figure Lengend Snippet: Purification of MH-1 SCA by protein L-agarose. Proteins were separated on a 12% polyacrylamide gel containing SDS and stained by Coomassie blue. Lane 1, molecular weight markers; lane 2, culture supernatant; lane 3, flow-through; lane 4, wash; lanes 5 and 6, eluates. Samples in lanes 2 to 4 were concentrated by trichloroacetic acid precipitation.

    Article Snippet: MH-1 SCA in the filtrate was affinity purified using protein L-agarose (Pierce) according to the manufacturer's instructions.

    Techniques: Purification, Staining, Molecular Weight, Flow Cytometry, TCA Precipitation

    CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over protein L or protein A columns, and single Fab fragments or Fc fragments were collected,

    Journal:

    Article Title: Fc-dependent expression of CD137 on human NK cells: insights into "agonistic" effects of anti-CD137 monoclonal antibodies

    doi: 10.1182/blood-2007-11-122465

    Figure Lengend Snippet: CD137 expression on NK cells is induced in an Fc-dependent fashion. GG mAb was digested into separate Fab and Fc fragments using papain. Digests were passed over protein L or protein A columns, and single Fab fragments or Fc fragments were collected,

    Article Snippet: Fab and Fc fragments from GG, CTM, and huIgG1 were generated by papain digestion followed by protein A and protein L chromatography using an ImmunoPure Fab Preparation kit (Pierce, Rockford, IL) according to the manufacturer's instructions.

    Techniques: Expressing