bio spin p6 desalting columns (Bio-Rad)
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bio spin p6 desalting columns
Bio Spin P6 Desalting Columns, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 212 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/bio+spin+p6+desalting+columns/Bio-Spin+P-6+Gel+Columns/pm41747261-100-26-30
Average 94 stars, based on 212 article reviews
Bio Spin P6 Desalting Columns, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 212 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/bio+spin+p6+desalting+columns/Bio-Spin+P-6+Gel+Columns/pm41747261-100-26-30
Average 94 stars, based on 212 article reviews
bio spin p6 desalting columns - by Bioz Stars,
2026-10
94/100 stars
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Concentration Assay:Article Title: Response Factor Correction for Quantitative Determination of Homooligomeric Sso SSB Binding to ssDNA by Native Mass Spectrometry Article Snippet: The data was analyzed and fit using GraphPad Prism (San Diego, CA, v10.6) using a total site binding model that accounts for nonspecific binding as described below: A = B max × P K d ′ + P + NS × P + A 0 2 or a cooperativity model A = B max × P h K d ′ h + P h + A 0 3 where A is the change in anisotropy, P is the protein concentration, B max is the saturation point for A , K d ′ is the apparent dissociation constant, NS is the slope for any nonspecific binding between proteins in solution interacting with Sso SSB-ssDNA bound species at higher protein concentrations, A 0 is the background signal of the unbound Cy5-ssDNA, and h is the Hill coefficient. .. Protein samples were prepared in 200 mM NH 4 OAc (pH = 7.1 ± 0.1) to a concentration of 5 μM following two rounds of buffer exchange with Article Title: Response Factor Correction for Quantitative Determination of Homooligomeric Sso SSB Binding to ssDNA by Native Mass Spectrometry. Article Snippet: Native mass spectrometry (nMS) has emerged as a complementary approach for elucidating molecular parameters of biological complexes relative to solution-phase experiments.. Herein, we utilize nMS to determine the subunit binding affinities (Kd,i) of the single-stranded DNA binding protein (SSB) from Saccharolobus solfataricus (Sso) to poly dT single-stranded DNA (ssDNA) compared with the apparent Kd′ values obtained from solution-phase fluorescence anisotropy.. This work resolves conflicting previous biochemical reports on the stoichiometry and affinities of SsoSSB while also highlighting the advantages and limitations of nMS quantification. Buffer Exchange:Article Title: Response Factor Correction for Quantitative Determination of Homooligomeric Sso SSB Binding to ssDNA by Native Mass Spectrometry Article Snippet: The data was analyzed and fit using GraphPad Prism (San Diego, CA, v10.6) using a total site binding model that accounts for nonspecific binding as described below: A = B max × P K d ′ + P + NS × P + A 0 2 or a cooperativity model A = B max × P h K d ′ h + P h + A 0 3 where A is the change in anisotropy, P is the protein concentration, B max is the saturation point for A , K d ′ is the apparent dissociation constant, NS is the slope for any nonspecific binding between proteins in solution interacting with Sso SSB-ssDNA bound species at higher protein concentrations, A 0 is the background signal of the unbound Cy5-ssDNA, and h is the Hill coefficient. .. Protein samples were prepared in 200 mM NH 4 OAc (pH = 7.1 ± 0.1) to a concentration of 5 μM following two rounds of buffer exchange with Article Title: Response Factor Correction for Quantitative Determination of Homooligomeric Sso SSB Binding to ssDNA by Native Mass Spectrometry. Article Snippet: Native mass spectrometry (nMS) has emerged as a complementary approach for elucidating molecular parameters of biological complexes relative to solution-phase experiments.. Herein, we utilize nMS to determine the subunit binding affinities (Kd,i) of the single-stranded DNA binding protein (SSB) from Saccharolobus solfataricus (Sso) to poly dT single-stranded DNA (ssDNA) compared with the apparent Kd′ values obtained from solution-phase fluorescence anisotropy.. This work resolves conflicting previous biochemical reports on the stoichiometry and affinities of SsoSSB while also highlighting the advantages and limitations of nMS quantification. |