interferon gamma rabbit polyclonal Search Results


antibodies to ifn-γ  (Angel Biotechnology)
90
Angel Biotechnology antibodies to ifn-γ
( a ) Experimental THz spectrum of water (orange), HD-water (blue, dashed line), HD of antibody to <t>IFN</t> - γ (black), HD of antibody to IFNGR1 (red) and HD of IFN - γ (green) in the 100–240 cm − 1 spectral region. The inset shows the full amplitude of the HD-IFN - γ sample in the spectral region highlighting a prominent 217 cm − 1 mode in the spectrum. ( b ) Experimental THz spectrum of IFN - γ (cyan) and anti-IFN - γ (purple dashed line) in the 100–240 cm − 1 spectral region. ( c ) Experimental THz spectrum of water (orange), HD-water (blue, dashed line), HD of antibody to IFN - γ (black ), HD of IFN - γ (green), and HD of antibody to IFNGR1 (red) in the 40–100 cm − 1 spectral region. ( d ) The experimental THz spectrum of IFN - γ (cyan) and anti-IFN - γ (purple dashed line) in the 40–100 cm − 1 spectral region.
Antibodies To Ifn γ, supplied by Angel Biotechnology, 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


( a ) Experimental THz spectrum of water (orange), HD-water (blue, dashed line), HD of antibody to IFN - γ (black), HD of antibody to IFNGR1 (red) and HD of IFN - γ (green) in the 100–240 cm − 1 spectral region. The inset shows the full amplitude of the HD-IFN - γ sample in the spectral region highlighting a prominent 217 cm − 1 mode in the spectrum. ( b ) Experimental THz spectrum of IFN - γ (cyan) and anti-IFN - γ (purple dashed line) in the 100–240 cm − 1 spectral region. ( c ) Experimental THz spectrum of water (orange), HD-water (blue, dashed line), HD of antibody to IFN - γ (black ), HD of IFN - γ (green), and HD of antibody to IFNGR1 (red) in the 40–100 cm − 1 spectral region. ( d ) The experimental THz spectrum of IFN - γ (cyan) and anti-IFN - γ (purple dashed line) in the 40–100 cm − 1 spectral region.

Journal: Scientific Reports

Article Title: New insights into the microscopic interactions associated with the physical mechanism of action of highly diluted biologics

doi: 10.1038/s41598-021-93326-1

Figure Lengend Snippet: ( a ) Experimental THz spectrum of water (orange), HD-water (blue, dashed line), HD of antibody to IFN - γ (black), HD of antibody to IFNGR1 (red) and HD of IFN - γ (green) in the 100–240 cm − 1 spectral region. The inset shows the full amplitude of the HD-IFN - γ sample in the spectral region highlighting a prominent 217 cm − 1 mode in the spectrum. ( b ) Experimental THz spectrum of IFN - γ (cyan) and anti-IFN - γ (purple dashed line) in the 100–240 cm − 1 spectral region. ( c ) Experimental THz spectrum of water (orange), HD-water (blue, dashed line), HD of antibody to IFN - γ (black ), HD of IFN - γ (green), and HD of antibody to IFNGR1 (red) in the 40–100 cm − 1 spectral region. ( d ) The experimental THz spectrum of IFN - γ (cyan) and anti-IFN - γ (purple dashed line) in the 40–100 cm − 1 spectral region.

Article Snippet: The following reagents were used: antibodies to IFN-γ (2.5 mg/ml, Angel Biotechnology Holdings, Penicuik, U.K.), antibodies to IFN-γ receptor 1 (1 mg/ml, Abcam, cat.number Ab61179-100), IFN-γ (1 mg/ml, Prospec Protein Specialists, cat.number CYT-206), distilled water (solvent).

Techniques:

Free energy surface derived from the full correlation analyses (FCA) of the MD trajectories of the IFN - γ dimer. The C-a representation of IFN - γ illustrates the dominant motion within the minimum of the energy surfaces where regions colored in red show greater mobility and regions in blue have less mobility.

Journal: Scientific Reports

Article Title: New insights into the microscopic interactions associated with the physical mechanism of action of highly diluted biologics

doi: 10.1038/s41598-021-93326-1

Figure Lengend Snippet: Free energy surface derived from the full correlation analyses (FCA) of the MD trajectories of the IFN - γ dimer. The C-a representation of IFN - γ illustrates the dominant motion within the minimum of the energy surfaces where regions colored in red show greater mobility and regions in blue have less mobility.

Article Snippet: The following reagents were used: antibodies to IFN-γ (2.5 mg/ml, Angel Biotechnology Holdings, Penicuik, U.K.), antibodies to IFN-γ receptor 1 (1 mg/ml, Abcam, cat.number Ab61179-100), IFN-γ (1 mg/ml, Prospec Protein Specialists, cat.number CYT-206), distilled water (solvent).

Techniques: Derivative Assay

( a ) A comparison of the root mean square fluctuations (RMSF) of the dominant conformation of IFN-γ in water vs a water–ethanol solvent. ( b ) The C-a representation of the dominant conformational mode of IFN-γ in the water–ethanol solvent from the MD simulation. Regions colored in red show greater mobility and regions in blue have less mobility. ( c ) A representative root mean square deviation (RMSD) of the MD simulations carried out on IFN-γ in water vs that in the water–ethanol solvent. ( e ) The C α –C α distribution of distances in IFN-γ from the RMSD calculation from ( d ). The van Hove self-correlation function of all atoms of IFN-γ in water ( e ) and ( f ) in the water–ethanol solvent.

Journal: Scientific Reports

Article Title: New insights into the microscopic interactions associated with the physical mechanism of action of highly diluted biologics

doi: 10.1038/s41598-021-93326-1

Figure Lengend Snippet: ( a ) A comparison of the root mean square fluctuations (RMSF) of the dominant conformation of IFN-γ in water vs a water–ethanol solvent. ( b ) The C-a representation of the dominant conformational mode of IFN-γ in the water–ethanol solvent from the MD simulation. Regions colored in red show greater mobility and regions in blue have less mobility. ( c ) A representative root mean square deviation (RMSD) of the MD simulations carried out on IFN-γ in water vs that in the water–ethanol solvent. ( e ) The C α –C α distribution of distances in IFN-γ from the RMSD calculation from ( d ). The van Hove self-correlation function of all atoms of IFN-γ in water ( e ) and ( f ) in the water–ethanol solvent.

Article Snippet: The following reagents were used: antibodies to IFN-γ (2.5 mg/ml, Angel Biotechnology Holdings, Penicuik, U.K.), antibodies to IFN-γ receptor 1 (1 mg/ml, Abcam, cat.number Ab61179-100), IFN-γ (1 mg/ml, Prospec Protein Specialists, cat.number CYT-206), distilled water (solvent).

Techniques: Comparison, Solvent

( a ) The calculated MSD of IFN - γ in water (black) and in the water–ethanol mixed solvent (magenta) from the MD simulation. ( b ) The calculated self ISF of IFN - γ in water (black) and in the mixed ethanol–water solvent (magenta) from the MD simulation.

Journal: Scientific Reports

Article Title: New insights into the microscopic interactions associated with the physical mechanism of action of highly diluted biologics

doi: 10.1038/s41598-021-93326-1

Figure Lengend Snippet: ( a ) The calculated MSD of IFN - γ in water (black) and in the water–ethanol mixed solvent (magenta) from the MD simulation. ( b ) The calculated self ISF of IFN - γ in water (black) and in the mixed ethanol–water solvent (magenta) from the MD simulation.

Article Snippet: The following reagents were used: antibodies to IFN-γ (2.5 mg/ml, Angel Biotechnology Holdings, Penicuik, U.K.), antibodies to IFN-γ receptor 1 (1 mg/ml, Abcam, cat.number Ab61179-100), IFN-γ (1 mg/ml, Prospec Protein Specialists, cat.number CYT-206), distilled water (solvent).

Techniques: Solvent

( a ) The calculated distance dependent ( d ) absorption coefficient of water in the IFN - γ hydration shell from the MD simulation. ( b ) The calculated distance ( d ) dependent absorption coefficient of hydration shell water of IFN - γ in a water–ethanol solvent mixture. ( c ) The calculated low-frequency fluctuation spectrum of intra-protein interactions in IFN - γ from MD simulation. ( d ) The computed water-protein H-bonding spectrum of IFN - γ in water (black) and IFN - γ in the water–ethanol solvent environment (magenta).

Journal: Scientific Reports

Article Title: New insights into the microscopic interactions associated with the physical mechanism of action of highly diluted biologics

doi: 10.1038/s41598-021-93326-1

Figure Lengend Snippet: ( a ) The calculated distance dependent ( d ) absorption coefficient of water in the IFN - γ hydration shell from the MD simulation. ( b ) The calculated distance ( d ) dependent absorption coefficient of hydration shell water of IFN - γ in a water–ethanol solvent mixture. ( c ) The calculated low-frequency fluctuation spectrum of intra-protein interactions in IFN - γ from MD simulation. ( d ) The computed water-protein H-bonding spectrum of IFN - γ in water (black) and IFN - γ in the water–ethanol solvent environment (magenta).

Article Snippet: The following reagents were used: antibodies to IFN-γ (2.5 mg/ml, Angel Biotechnology Holdings, Penicuik, U.K.), antibodies to IFN-γ receptor 1 (1 mg/ml, Abcam, cat.number Ab61179-100), IFN-γ (1 mg/ml, Prospec Protein Specialists, cat.number CYT-206), distilled water (solvent).

Techniques: Solvent

( a ) 3-D representation of the structure of the IFN - γ receptor complex and ( b ) the dynamics of the principal conformational states of the individual components forming the receptor complex from the FCA of all of the individual IFN - γ receptor MD simulations.

Journal: Scientific Reports

Article Title: New insights into the microscopic interactions associated with the physical mechanism of action of highly diluted biologics

doi: 10.1038/s41598-021-93326-1

Figure Lengend Snippet: ( a ) 3-D representation of the structure of the IFN - γ receptor complex and ( b ) the dynamics of the principal conformational states of the individual components forming the receptor complex from the FCA of all of the individual IFN - γ receptor MD simulations.

Article Snippet: The following reagents were used: antibodies to IFN-γ (2.5 mg/ml, Angel Biotechnology Holdings, Penicuik, U.K.), antibodies to IFN-γ receptor 1 (1 mg/ml, Abcam, cat.number Ab61179-100), IFN-γ (1 mg/ml, Prospec Protein Specialists, cat.number CYT-206), distilled water (solvent).

Techniques:

Free energy surface derived from the FCA of the MD trajectory of ( a ) IFN-γ, ( b ) IFNGR1, and ( c ) IFNGR2 from the IFN-γ receptor complex in a mixed water–ethanol solvent. The C-a representation of each conformation illustrates the dominant motion within the minimum of the energy surfaces where regions colored in red show greater mobility and regions in blue have less mobility.

Journal: Scientific Reports

Article Title: New insights into the microscopic interactions associated with the physical mechanism of action of highly diluted biologics

doi: 10.1038/s41598-021-93326-1

Figure Lengend Snippet: Free energy surface derived from the FCA of the MD trajectory of ( a ) IFN-γ, ( b ) IFNGR1, and ( c ) IFNGR2 from the IFN-γ receptor complex in a mixed water–ethanol solvent. The C-a representation of each conformation illustrates the dominant motion within the minimum of the energy surfaces where regions colored in red show greater mobility and regions in blue have less mobility.

Article Snippet: The following reagents were used: antibodies to IFN-γ (2.5 mg/ml, Angel Biotechnology Holdings, Penicuik, U.K.), antibodies to IFN-γ receptor 1 (1 mg/ml, Abcam, cat.number Ab61179-100), IFN-γ (1 mg/ml, Prospec Protein Specialists, cat.number CYT-206), distilled water (solvent).

Techniques: Derivative Assay, Solvent

( a ) The calculated MSD and ( b ) the self ISF from the MD simulation of the IFN - γ receptor complex in water (black) and in a mixed ethanol–water solvent (magenta). The inset in ( b ) shows the plot of the non-Gaussian parameter (α 2 (t)) of the cytokine complex in the two different solvent environments. The van Hove self-correlation function of the IFN - γ complex in (c ) water and ( d ) a water–ethanol mixed solvent from MD simulation. ( e ) A representative RMSD of the IFN - γ receptor complex in water (black line) vs that in the water–ethanol solvent (magenta line). In each of the individual MD simulations carried out on the IFN - γ receptor complex in the water–ethanol solvent, we observed a similar transition in the RMSD. ( f ) The distribution of the C-α distances from the computation of the root mean square deviation of atom distances in the receptor complex from ( e ).

Journal: Scientific Reports

Article Title: New insights into the microscopic interactions associated with the physical mechanism of action of highly diluted biologics

doi: 10.1038/s41598-021-93326-1

Figure Lengend Snippet: ( a ) The calculated MSD and ( b ) the self ISF from the MD simulation of the IFN - γ receptor complex in water (black) and in a mixed ethanol–water solvent (magenta). The inset in ( b ) shows the plot of the non-Gaussian parameter (α 2 (t)) of the cytokine complex in the two different solvent environments. The van Hove self-correlation function of the IFN - γ complex in (c ) water and ( d ) a water–ethanol mixed solvent from MD simulation. ( e ) A representative RMSD of the IFN - γ receptor complex in water (black line) vs that in the water–ethanol solvent (magenta line). In each of the individual MD simulations carried out on the IFN - γ receptor complex in the water–ethanol solvent, we observed a similar transition in the RMSD. ( f ) The distribution of the C-α distances from the computation of the root mean square deviation of atom distances in the receptor complex from ( e ).

Article Snippet: The following reagents were used: antibodies to IFN-γ (2.5 mg/ml, Angel Biotechnology Holdings, Penicuik, U.K.), antibodies to IFN-γ receptor 1 (1 mg/ml, Abcam, cat.number Ab61179-100), IFN-γ (1 mg/ml, Prospec Protein Specialists, cat.number CYT-206), distilled water (solvent).

Techniques: Solvent

( a ) The calculated protein-water H-bonding spectrum of the IFN - γ complex from the MD simulation in water (black line) and in the water–ethanol solvent (pink line). The 3-D representation of the IFN - γ complex in ( b ) water and ( c ) in the water–ethanol solvent where the strain propagation from the force distribution analysis (FDA) is represented as colored links. The force between IFN - γ and IFNGR1 is depicted by red links, the force between IFN - γ and IFNGR2 by orange links, and the force between IFNGR1 and IFNGR2 is represented by green links in the 3-D structure. ( d ) The low-frequency vibrational spectrum of the displacement of the correlated cluster of amino acids identified from the FDA of the complex in water (black line with black circles) and in the ethanol–water mixed solvent (pink line with pink squares).

Journal: Scientific Reports

Article Title: New insights into the microscopic interactions associated with the physical mechanism of action of highly diluted biologics

doi: 10.1038/s41598-021-93326-1

Figure Lengend Snippet: ( a ) The calculated protein-water H-bonding spectrum of the IFN - γ complex from the MD simulation in water (black line) and in the water–ethanol solvent (pink line). The 3-D representation of the IFN - γ complex in ( b ) water and ( c ) in the water–ethanol solvent where the strain propagation from the force distribution analysis (FDA) is represented as colored links. The force between IFN - γ and IFNGR1 is depicted by red links, the force between IFN - γ and IFNGR2 by orange links, and the force between IFNGR1 and IFNGR2 is represented by green links in the 3-D structure. ( d ) The low-frequency vibrational spectrum of the displacement of the correlated cluster of amino acids identified from the FDA of the complex in water (black line with black circles) and in the ethanol–water mixed solvent (pink line with pink squares).

Article Snippet: The following reagents were used: antibodies to IFN-γ (2.5 mg/ml, Angel Biotechnology Holdings, Penicuik, U.K.), antibodies to IFN-γ receptor 1 (1 mg/ml, Abcam, cat.number Ab61179-100), IFN-γ (1 mg/ml, Prospec Protein Specialists, cat.number CYT-206), distilled water (solvent).

Techniques: Solvent