Structured Review

GE Healthcare resource rpc
Biophysical characterization of PAS#1(600)-hGH. ( A ) Mass spectrometric analysis of PAS#1(600)-hGH by ESI-MS, confirming the calculated molecular mass of 73121.65 Da as well as precisely monodisperse composition, without any indication of prematurely terminated gene products. ( B ) Hydrophobicity analysis of PASylated hGH by reverse-phase (RP) HPLC. HIC of the original recombinant hGH and its PASylated version was performed on a Resource <t>RPC</t> column using an elution gradient from 2% v/v acetonitrile, 0.065% v/v <t>TFA</t> to 80% v/v acetonitrile, 0.05% v/v TFA. Both profiles show a single homogeneous peak with slightly earlier elution of PAS#1(600)-hGH (51.8% acetonitrile) in comparison with the corresponding unfused protein (52.3% acetonitrile). ( C ) Thermal denaturation of hGH and PAS#1(600)-hGH as determined by far UV CD measurement. Thermal unfolding of a 8.2 µM protein solution in 50 mM K 2 SO 4 , 20 mM K-P i pH 7.5 was followed at a wavelength of 208 nm where maximal spectral change upon unfolding was observed and the normalized unfolded fraction, f(u), was plotted as a function of temperature. The melting temperatures ( T m ) of hGH and PAS#1(600)-hGH were 85.4°C and 88.6°C, respectively.
Resource Rpc, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins"

Article Title: PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins

Journal: Protein Engineering, Design and Selection

doi: 10.1093/protein/gzt023

Biophysical characterization of PAS#1(600)-hGH. ( A ) Mass spectrometric analysis of PAS#1(600)-hGH by ESI-MS, confirming the calculated molecular mass of 73121.65 Da as well as precisely monodisperse composition, without any indication of prematurely terminated gene products. ( B ) Hydrophobicity analysis of PASylated hGH by reverse-phase (RP) HPLC. HIC of the original recombinant hGH and its PASylated version was performed on a Resource RPC column using an elution gradient from 2% v/v acetonitrile, 0.065% v/v TFA to 80% v/v acetonitrile, 0.05% v/v TFA. Both profiles show a single homogeneous peak with slightly earlier elution of PAS#1(600)-hGH (51.8% acetonitrile) in comparison with the corresponding unfused protein (52.3% acetonitrile). ( C ) Thermal denaturation of hGH and PAS#1(600)-hGH as determined by far UV CD measurement. Thermal unfolding of a 8.2 µM protein solution in 50 mM K 2 SO 4 , 20 mM K-P i pH 7.5 was followed at a wavelength of 208 nm where maximal spectral change upon unfolding was observed and the normalized unfolded fraction, f(u), was plotted as a function of temperature. The melting temperatures ( T m ) of hGH and PAS#1(600)-hGH were 85.4°C and 88.6°C, respectively.
Figure Legend Snippet: Biophysical characterization of PAS#1(600)-hGH. ( A ) Mass spectrometric analysis of PAS#1(600)-hGH by ESI-MS, confirming the calculated molecular mass of 73121.65 Da as well as precisely monodisperse composition, without any indication of prematurely terminated gene products. ( B ) Hydrophobicity analysis of PASylated hGH by reverse-phase (RP) HPLC. HIC of the original recombinant hGH and its PASylated version was performed on a Resource RPC column using an elution gradient from 2% v/v acetonitrile, 0.065% v/v TFA to 80% v/v acetonitrile, 0.05% v/v TFA. Both profiles show a single homogeneous peak with slightly earlier elution of PAS#1(600)-hGH (51.8% acetonitrile) in comparison with the corresponding unfused protein (52.3% acetonitrile). ( C ) Thermal denaturation of hGH and PAS#1(600)-hGH as determined by far UV CD measurement. Thermal unfolding of a 8.2 µM protein solution in 50 mM K 2 SO 4 , 20 mM K-P i pH 7.5 was followed at a wavelength of 208 nm where maximal spectral change upon unfolding was observed and the normalized unfolded fraction, f(u), was plotted as a function of temperature. The melting temperatures ( T m ) of hGH and PAS#1(600)-hGH were 85.4°C and 88.6°C, respectively.

Techniques Used: Mass Spectrometry, High Performance Liquid Chromatography, Hydrophobic Interaction Chromatography, Recombinant

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Mass Spectrometry:

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Pyrolysis Gas Chromatography:

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Proliferation Assay:

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Nuclear Magnetic Resonance:

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Article Snippet: Paragraph title: NMR sample preparation ... Prior to this step, protein that underwent partial auto-proteolysis was re-purified by reversed-phase HPLC with a Resource RPC 3 mL column (GE Healthcare) equilibrated with 0.05% trifluoroacetic acid (v/v), and eluted with 80% acetonitrile and 0.05% trifluoroacetic acid (v/v).

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
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Activity Assay:

Article Title: Nanoglycan Complex-Formulation Extends VEGF Retention Time in the Lung
Article Snippet: Purification of VEGF was performed according to a previously described procedure by Lee et al. , using columns of heparin Sepharose 6 Fast Flow, Resource S, and Resource RPC purchased from GE Health Sciences (# 17-0998-01, #17-1178-01, and #17-1181-01, respectively). .. The activity of the purified VEGF was determined by an endothelial cell proliferation assay, using a CellTiter 96 AQueous Cell Proliferation Assay reagent from Promega/Fisher (#PR-G5421).

Cell Culture:

Article Title: Nanoglycan Complex-Formulation Extends VEGF Retention Time in the Lung
Article Snippet: The virus was propagated, titrated, and inoculated into Sf21 cell culture for VEGF expression. .. Purification of VEGF was performed according to a previously described procedure by Lee et al. , using columns of heparin Sepharose 6 Fast Flow, Resource S, and Resource RPC purchased from GE Health Sciences (# 17-0998-01, #17-1178-01, and #17-1181-01, respectively).

Expressing:

Article Title: Nanoglycan Complex-Formulation Extends VEGF Retention Time in the Lung
Article Snippet: The expression medium containing secreted recombinant VEGF was collected for purification. .. Purification of VEGF was performed according to a previously described procedure by Lee et al. , using columns of heparin Sepharose 6 Fast Flow, Resource S, and Resource RPC purchased from GE Health Sciences (# 17-0998-01, #17-1178-01, and #17-1181-01, respectively).

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
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Article Title: Highly Efficient NMR Assignment of Intrinsically Disordered Proteins: Application to B- and T Cell Receptor Domains
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BIA-KA:

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High Performance Liquid Chromatography:

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Transfection:

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Chromatography:

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Infection:

Article Title: Molecular and Functional Characterization of a c-type lysozyme from the Asian Corn Borer, Ostrinia furnacalis
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Liquid Chromatography:

Article Title: Chromobacterium spp. mediate their anti-Plasmodium activity through secretion of the histone deacetylase inhibitor romidepsin
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Inhibition:

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Sequencing:

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Sonication:

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
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Injection:

Article Title: Molecular and Functional Characterization of a c-type lysozyme from the Asian Corn Borer, Ostrinia furnacalis
Article Snippet: Insect immunization, haemolymph collection and purification of lysozyme Fifth-instar O. furnacalis larvae were injected with 2 µl of the bacterial mixture of E. coli K12D31 and S. aureus (about 2×105 cells of each bacterial species suspended in 2 µl PBS) and kept at 26°C for 24 hours. .. The antibacterial fractions were pooled and lyophilized in the Freeze Dry System/Freezone® 4.5 (Labconco, www.labconco.com ), then resuspended in 0.1% trifluoroacetic acid buffer and applied to a Resource RPC 3 ml column (6.4 × 100 mm, Amersham Pharmacia Biotech) in the ÄKTA FPLC system (Amersham Pharmacia Biotech).

Recombinant:

Article Title: Nanoglycan Complex-Formulation Extends VEGF Retention Time in the Lung
Article Snippet: The expression medium containing secreted recombinant VEGF was collected for purification. .. Purification of VEGF was performed according to a previously described procedure by Lee et al. , using columns of heparin Sepharose 6 Fast Flow, Resource S, and Resource RPC purchased from GE Health Sciences (# 17-0998-01, #17-1178-01, and #17-1181-01, respectively).

Molecular Weight:

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA. .. SDS-PAGE analysis, HPLC/MS experiments, size exclusion chromatography, and NMR spectra confirmed the molecular weight and homogeneous purity of the protein samples.

Mutagenesis:

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: The wild type HAfp23 and mutant HAfp23-F3G fusion peptides (H1 subtype) were expressed in Escherichia coli BL21(DE3) as a fusion protein with the IgG-binding domain B1 of streptococcal protein G (GB1; Protein Data Bank code 3GB1 ) located at the N terminus and a solubility tag, GSKKKKD, at the C terminus to assist in the purification. .. The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA.

Article Title: Comprehensive Experimental and Computational Analysis of Binding Energy Hot Spots at the NF-?B Essential Modulator (NEMO)/IKK? Protein-Protein Interface
Article Snippet: Paragraph title: Proteolytic Cleavage and Purification of IKKβ Mutant Pep-tides ... We therefore purified each cleaved IKKβ peptide by reversed phase HPLC using a Resource RPC 3 ml column (GE Life Sciences), eluting with a linear gradient of 0–100% Buffer B over at least 45 minutes (Buffer A: 0.065% trifluoroacetic acid in water; Buffer B: 0.05% trifluoroacetic acid in methanol).

Flow Cytometry:

Article Title: Nanoglycan Complex-Formulation Extends VEGF Retention Time in the Lung
Article Snippet: .. Purification of VEGF was performed according to a previously described procedure by Lee et al. , using columns of heparin Sepharose 6 Fast Flow, Resource S, and Resource RPC purchased from GE Health Sciences (# 17-0998-01, #17-1178-01, and #17-1181-01, respectively). .. The purity of the prepared VEGF was greater than 95%, according to SDS PAGE and Coomassie blue staining.

Article Title: Novel Probiotic Bifidobacterium bifidum CECT 7366 Strain Active against the Pathogenic Bacterium Helicobacter pylori ▿
Article Snippet: For the inverse-phase chromatography, a Resource RPC 3-ml column (GE Healthcare) was used, working in gradient with eluent A (5% 2-propanol, 0.1% trifluoroacetic acid [TFA] in Milli-Q-filtered water) and eluent B (0.1% TFA in 2-propanol). .. Throughout the purification process, several parameters, including UV absorbance (280, 254, and 214 nm), pressure, flow rate, pH, and ionic strength, were monitored.

Article Title: Chromobacterium spp. mediate their anti-Plasmodium activity through secretion of the histone deacetylase inhibitor romidepsin
Article Snippet: .. Panama (resuspended in start buffer) using a RESOURCE RPC 3 mL (GE Healthcare Life Sciences) column under gradient elution between 2% and 85% methanol in water 0.1% TFA at a constant 2 mL/min flow rate. ..

Article Title: Molecular and Functional Characterization of a c-type lysozyme from the Asian Corn Borer, Ostrinia furnacalis
Article Snippet: The filtrate was applied to a CM-Sepharose Fast Flow column (Amersham Pharmacia Biotech, www.apbiotech.com ) and eluted with a linear gradient of 0.05–1 M NH4OAc in the same buffer at a flow rate of 1.5 ml/min. .. The antibacterial fractions were pooled and lyophilized in the Freeze Dry System/Freezone® 4.5 (Labconco, www.labconco.com ), then resuspended in 0.1% trifluoroacetic acid buffer and applied to a Resource RPC 3 ml column (6.4 × 100 mm, Amersham Pharmacia Biotech) in the ÄKTA FPLC system (Amersham Pharmacia Biotech).

Article Title: A Comparative Study of Lectin Affinity Based Plant N-Glycoproteome Profiling Using Tomato Fruit as a Model *
Article Snippet: PGC flow through and bound fractions were additionally fractionated using high pH reverse phase (hpRP) chromatography using an Akta Explorer FPLC equipped with a Frac 950 fraction collector and UV detector (GE Healthcare). .. Tryptic peptides were reconstituted in buffer A (20 m m ammonium formate, pH 9.5 in water), and loaded onto a Resource RPC 3 ml column (GE Healthcare) with 20 m m ammonium formate, pH 9.5 as buffer A and 80% acetonitrile (ACN)/20 m m ammonium formate as buffer B.

Article Title: Characterization of antimicrobial substance from Lactobacillus salivarius KL-D4 and its application as biopreservative for creamy filling
Article Snippet: .. The bacteriocin separation was achieved using a Resource RPC 3 ml column (Amersham Bioscience, Sweden) at the flow rate of 1 ml/min. ..

Article Title: PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins
Article Snippet: Reverse-Phase HPLC The purified protein solution in PBS was adjusted to 2% v/v acetonitrile, 0.065% v/v trifluoroacetic acid (TFA) and 1 ml was applied to a Resource RPC 1 ml column (GE Healthcare) equilibrated with buffer A (2% v/v acetonitrile, 0.065% v/v TFA). .. For elution, a 0–100% gradient of buffer B (80% v/v acetonitrile, 0.05% v/v TFA) was applied over 20-bed volumes at a flow rate of 2 ml/min while monitoring protein elution at both 280 and 225 nm (PAS only absorbs in the peptide backbone region due to the absence of aromatic side chains).

Article Title: Highly Efficient NMR Assignment of Intrinsically Disordered Proteins: Application to B- and T Cell Receptor Domains
Article Snippet: .. The flow-through, containing the purified cleaved protein, was collected and filtered through a 0.2 µm syringe filter and loaded onto a RESOURCE RPC 3 ml column (Amersham Bioscience) connected to an FPLC system (ÄKTA Prime). ..

Labeling:

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: The 15 N isotope labeling was achieved by supplementing M9 minimal medium with 15 NH4 Cl , and natural abundance proteins were prepared by growing the E. coli in LB medium. .. The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA.

Purification:

Article Title: Nanoglycan Complex-Formulation Extends VEGF Retention Time in the Lung
Article Snippet: .. Purification of VEGF was performed according to a previously described procedure by Lee et al. , using columns of heparin Sepharose 6 Fast Flow, Resource S, and Resource RPC purchased from GE Health Sciences (# 17-0998-01, #17-1178-01, and #17-1181-01, respectively). .. The purity of the prepared VEGF was greater than 95%, according to SDS PAGE and Coomassie blue staining.

Article Title: Novel Probiotic Bifidobacterium bifidum CECT 7366 Strain Active against the Pathogenic Bacterium Helicobacter pylori ▿
Article Snippet: Paragraph title: Purification of the substance(s) of interest by cationic-exchange chromatography followed by inverse-phase chromatography. ... For the inverse-phase chromatography, a Resource RPC 3-ml column (GE Healthcare) was used, working in gradient with eluent A (5% 2-propanol, 0.1% trifluoroacetic acid [TFA] in Milli-Q-filtered water) and eluent B (0.1% TFA in 2-propanol).

Article Title: Differential Flap Dynamics in Wild-type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR Relaxation
Article Snippet: For NMR sample preparation, the purified protein was dialyzed against 20 mM formic acid at pH 2.7. .. Prior to this step, protein that underwent partial auto-proteolysis was re-purified by reversed-phase HPLC with a Resource RPC 3 mL column (GE Healthcare) equilibrated with 0.05% trifluoroacetic acid (v/v), and eluted with 80% acetonitrile and 0.05% trifluoroacetic acid (v/v).

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: Further purification was achieved by size exclusion chromatography through a Superdex 75 26/600 PG (GE Healthcare) in the presence of 25 m m Tris, pH 7.4. .. The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA.

Article Title: Molecular and Functional Characterization of a c-type lysozyme from the Asian Corn Borer, Ostrinia furnacalis
Article Snippet: Paragraph title: Insect immunization, haemolymph collection and purification of lysozyme ... The antibacterial fractions were pooled and lyophilized in the Freeze Dry System/Freezone® 4.5 (Labconco, www.labconco.com ), then resuspended in 0.1% trifluoroacetic acid buffer and applied to a Resource RPC 3 ml column (6.4 × 100 mm, Amersham Pharmacia Biotech) in the ÄKTA FPLC system (Amersham Pharmacia Biotech).

Article Title: A Cocoa Peptide Protects Caenorhabditis elegans from Oxidative Stress and ?-Amyloid Peptide Toxicity
Article Snippet: Paragraph title: Peptide purification ... Peptides were loaded in a Resource RPC 3 mL column (GE Healthcare, Amersham Bioscience AB, Barcelona, Spain) and eluted with a linear gradient of acetonitrile with 0.1% TFA.

Article Title: PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins
Article Snippet: .. Reverse-Phase HPLC The purified protein solution in PBS was adjusted to 2% v/v acetonitrile, 0.065% v/v trifluoroacetic acid (TFA) and 1 ml was applied to a Resource RPC 1 ml column (GE Healthcare) equilibrated with buffer A (2% v/v acetonitrile, 0.065% v/v TFA). .. For elution, a 0–100% gradient of buffer B (80% v/v acetonitrile, 0.05% v/v TFA) was applied over 20-bed volumes at a flow rate of 2 ml/min while monitoring protein elution at both 280 and 225 nm (PAS only absorbs in the peptide backbone region due to the absence of aromatic side chains).

Article Title: Highly Efficient NMR Assignment of Intrinsically Disordered Proteins: Application to B- and T Cell Receptor Domains
Article Snippet: .. The flow-through, containing the purified cleaved protein, was collected and filtered through a 0.2 µm syringe filter and loaded onto a RESOURCE RPC 3 ml column (Amersham Bioscience) connected to an FPLC system (ÄKTA Prime). ..

Article Title: Comprehensive Experimental and Computational Analysis of Binding Energy Hot Spots at the NF-?B Essential Modulator (NEMO)/IKK? Protein-Protein Interface
Article Snippet: .. We therefore purified each cleaved IKKβ peptide by reversed phase HPLC using a Resource RPC 3 ml column (GE Life Sciences), eluting with a linear gradient of 0–100% Buffer B over at least 45 minutes (Buffer A: 0.065% trifluoroacetic acid in water; Buffer B: 0.05% trifluoroacetic acid in methanol). .. The steepness of the gradient was adjusted for each mutant to achieve baseline separation of the IKKβ peptide from the cleaved MBP.

Protein Purification:

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: Protein purification closely followed the previously published protocol for the HAfp23 influenza fusion domain ( ). .. The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA.

Software:

Article Title: Characterization of antimicrobial substance from Lactobacillus salivarius KL-D4 and its application as biopreservative for creamy filling
Article Snippet: Reverse-phase HPLC This process was performed using the Breeze 2 System (Walter, USA), including a binary pump: model 1525 (Walter, USA), a 6 port injector: model 7725 (Rheodyn, USA), a UV/visible detector: model 2489 (Walter, USA) and a computer with the Breeze software installed. .. The bacteriocin separation was achieved using a Resource RPC 3 ml column (Amersham Bioscience, Sweden) at the flow rate of 1 ml/min.

Fast Protein Liquid Chromatography:

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: Cells were lysed by sonication, and proteins were purified from lysate by histidine affinity chromatography using a HisTrap HP column (GE Healthcare) on Aktä PrimePlus and Aktä Purifier FPLC systems. .. The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA.

Article Title: Chromobacterium spp. mediate their anti-Plasmodium activity through secretion of the histone deacetylase inhibitor romidepsin
Article Snippet: Reverse-phase FPLC was conducted on the n -butanol extract of C. sp . .. Panama (resuspended in start buffer) using a RESOURCE RPC 3 mL (GE Healthcare Life Sciences) column under gradient elution between 2% and 85% methanol in water 0.1% TFA at a constant 2 mL/min flow rate.

Article Title: Molecular and Functional Characterization of a c-type lysozyme from the Asian Corn Borer, Ostrinia furnacalis
Article Snippet: .. The antibacterial fractions were pooled and lyophilized in the Freeze Dry System/Freezone® 4.5 (Labconco, www.labconco.com ), then resuspended in 0.1% trifluoroacetic acid buffer and applied to a Resource RPC 3 ml column (6.4 × 100 mm, Amersham Pharmacia Biotech) in the ÄKTA FPLC system (Amersham Pharmacia Biotech). ..

Article Title: A Comparative Study of Lectin Affinity Based Plant N-Glycoproteome Profiling Using Tomato Fruit as a Model *
Article Snippet: PGC flow through and bound fractions were additionally fractionated using high pH reverse phase (hpRP) chromatography using an Akta Explorer FPLC equipped with a Frac 950 fraction collector and UV detector (GE Healthcare). .. Tryptic peptides were reconstituted in buffer A (20 m m ammonium formate, pH 9.5 in water), and loaded onto a Resource RPC 3 ml column (GE Healthcare) with 20 m m ammonium formate, pH 9.5 as buffer A and 80% acetonitrile (ACN)/20 m m ammonium formate as buffer B.

Article Title: Dietary Fibers and Protective Lactobacilli Drive Burrata Cheese Microbiome
Article Snippet: .. The peptide profiles of the pH 4.6-soluble fractions were determined by reverse-phase (RP) chromatography with a Resource RPC 3-ml column using an Äkta fast protein liquid chromatography (FPLC) system (GE Healthcare Biosciences). .. Concentrations of total and individual free amino acids (FAA) in the pH 4.6-soluble extract were determined using the Biochrom 30 amino acid analyzer (Biochrom LTD, Cambridge Science Park, England) as previously described ( ).

Article Title: A Cocoa Peptide Protects Caenorhabditis elegans from Oxidative Stress and ?-Amyloid Peptide Toxicity
Article Snippet: Hydrolyzed “Barquillo” (protease-treated) samples underwent FPLC using a Hi-Prep 16/10 Phenyl FF column (GE Healthcare, Amersham Biosciences AB). .. Peptides were loaded in a Resource RPC 3 mL column (GE Healthcare, Amersham Bioscience AB, Barcelona, Spain) and eluted with a linear gradient of acetonitrile with 0.1% TFA.

Article Title: Highly Efficient NMR Assignment of Intrinsically Disordered Proteins: Application to B- and T Cell Receptor Domains
Article Snippet: .. The flow-through, containing the purified cleaved protein, was collected and filtered through a 0.2 µm syringe filter and loaded onto a RESOURCE RPC 3 ml column (Amersham Bioscience) connected to an FPLC system (ÄKTA Prime). ..

Reversed-phase Chromatography:

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: .. The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA. ..

Peptide Fractionation:

Article Title: A Comparative Study of Lectin Affinity Based Plant N-Glycoproteome Profiling Using Tomato Fruit as a Model *
Article Snippet: Paragraph title: Peptide Fractionation for Shotgun Proteomics ... Tryptic peptides were reconstituted in buffer A (20 m m ammonium formate, pH 9.5 in water), and loaded onto a Resource RPC 3 ml column (GE Healthcare) with 20 m m ammonium formate, pH 9.5 as buffer A and 80% acetonitrile (ACN)/20 m m ammonium formate as buffer B.

Affinity Purification:

Article Title: Comprehensive Experimental and Computational Analysis of Binding Energy Hot Spots at the NF-?B Essential Modulator (NEMO)/IKK? Protein-Protein Interface
Article Snippet: Passage of the cleaved samples over a Ni/NTA affinity purification column was not successful in separating the His-tag containing IKKβ peptide from the cleaved MPB fusion partner, because under all conditions attempted significant amounts of MBP also bound to the column and co-eluted with the cleaved IKKβ peptide upon application of an imidazole gradient. .. We therefore purified each cleaved IKKβ peptide by reversed phase HPLC using a Resource RPC 3 ml column (GE Life Sciences), eluting with a linear gradient of 0–100% Buffer B over at least 45 minutes (Buffer A: 0.065% trifluoroacetic acid in water; Buffer B: 0.05% trifluoroacetic acid in methanol).

Plasmid Preparation:

Article Title: Nanoglycan Complex-Formulation Extends VEGF Retention Time in the Lung
Article Snippet: Briefly, VEGF cDNA was inserted into a Gateway vector, pDEST8 (#11804-010), through a LR recombination reaction using the Gateway LR Clonase II enzyme mix (#11791-20). .. Purification of VEGF was performed according to a previously described procedure by Lee et al. , using columns of heparin Sepharose 6 Fast Flow, Resource S, and Resource RPC purchased from GE Health Sciences (# 17-0998-01, #17-1178-01, and #17-1181-01, respectively).

Solubility:

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: The wild type HAfp23 and mutant HAfp23-F3G fusion peptides (H1 subtype) were expressed in Escherichia coli BL21(DE3) as a fusion protein with the IgG-binding domain B1 of streptococcal protein G (GB1; Protein Data Bank code 3GB1 ) located at the N terminus and a solubility tag, GSKKKKD, at the C terminus to assist in the purification. .. The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA.

Affinity Chromatography:

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: Cells were lysed by sonication, and proteins were purified from lysate by histidine affinity chromatography using a HisTrap HP column (GE Healthcare) on Aktä PrimePlus and Aktä Purifier FPLC systems. .. The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA.

Sample Prep:

Article Title: Differential Flap Dynamics in Wild-type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR Relaxation
Article Snippet: Paragraph title: NMR sample preparation ... Prior to this step, protein that underwent partial auto-proteolysis was re-purified by reversed-phase HPLC with a Resource RPC 3 mL column (GE Healthcare) equilibrated with 0.05% trifluoroacetic acid (v/v), and eluted with 80% acetonitrile and 0.05% trifluoroacetic acid (v/v).

Size-exclusion Chromatography:

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: Further purification was achieved by size exclusion chromatography through a Superdex 75 26/600 PG (GE Healthcare) in the presence of 25 m m Tris, pH 7.4. .. The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA.

Incubation:

Article Title: Highly Efficient NMR Assignment of Intrinsically Disordered Proteins: Application to B- and T Cell Receptor Domains
Article Snippet: For protein elution, one-hour incubation with four times the gel column volume of buffer A (with 250 mM imidazole) was used. .. The flow-through, containing the purified cleaved protein, was collected and filtered through a 0.2 µm syringe filter and loaded onto a RESOURCE RPC 3 ml column (Amersham Bioscience) connected to an FPLC system (ÄKTA Prime).

Concentration Assay:

Article Title: Dietary Fibers and Protective Lactobacilli Drive Burrata Cheese Microbiome
Article Snippet: Paragraph title: Assessment of proteolysis and concentration of free amino acids. ... The peptide profiles of the pH 4.6-soluble fractions were determined by reverse-phase (RP) chromatography with a Resource RPC 3-ml column using an Äkta fast protein liquid chromatography (FPLC) system (GE Healthcare Biosciences).

Article Title: Comprehensive Experimental and Computational Analysis of Binding Energy Hot Spots at the NF-?B Essential Modulator (NEMO)/IKK? Protein-Protein Interface
Article Snippet: Following cleavage, samples were treated with PMSF (final concentration 1 mM, freshly prepared from 100 mM stock solutions stored frozen in 100% isopropanol) on ice for at least 1 hour. .. We therefore purified each cleaved IKKβ peptide by reversed phase HPLC using a Resource RPC 3 ml column (GE Life Sciences), eluting with a linear gradient of 0–100% Buffer B over at least 45 minutes (Buffer A: 0.065% trifluoroacetic acid in water; Buffer B: 0.05% trifluoroacetic acid in methanol).

BAC Assay:

Article Title: Nanoglycan Complex-Formulation Extends VEGF Retention Time in the Lung
Article Snippet: The pBac-VEGF was subsequently transfected into Sf21 insect cells (#11497-013) to generate recombinant baculovirus, Bac-VEGF. .. Purification of VEGF was performed according to a previously described procedure by Lee et al. , using columns of heparin Sepharose 6 Fast Flow, Resource S, and Resource RPC purchased from GE Health Sciences (# 17-0998-01, #17-1178-01, and #17-1181-01, respectively).

Staining:

Article Title: Nanoglycan Complex-Formulation Extends VEGF Retention Time in the Lung
Article Snippet: Purification of VEGF was performed according to a previously described procedure by Lee et al. , using columns of heparin Sepharose 6 Fast Flow, Resource S, and Resource RPC purchased from GE Health Sciences (# 17-0998-01, #17-1178-01, and #17-1181-01, respectively). .. The purity of the prepared VEGF was greater than 95%, according to SDS PAGE and Coomassie blue staining.

Article Title: Dietary Fibers and Protective Lactobacilli Drive Burrata Cheese Microbiome
Article Snippet: Gels were stained by the method described by Blakesley and Boezi ( ) with Coomassie brilliant blue G250, and the color background was faded by continuous washing in distilled water. .. The peptide profiles of the pH 4.6-soluble fractions were determined by reverse-phase (RP) chromatography with a Resource RPC 3-ml column using an Äkta fast protein liquid chromatography (FPLC) system (GE Healthcare Biosciences).

Article Title: Highly Efficient NMR Assignment of Intrinsically Disordered Proteins: Application to B- and T Cell Receptor Domains
Article Snippet: The flow-through, containing the purified cleaved protein, was collected and filtered through a 0.2 µm syringe filter and loaded onto a RESOURCE RPC 3 ml column (Amersham Bioscience) connected to an FPLC system (ÄKTA Prime). .. To verify purity of the protein, SimplyBlue Coomassie (Invitrogen) staining of NuPAGE Novex 12% Bis-Tris Mini Gels (Invitrogen) was performed.

SDS Page:

Article Title: Nanoglycan Complex-Formulation Extends VEGF Retention Time in the Lung
Article Snippet: Purification of VEGF was performed according to a previously described procedure by Lee et al. , using columns of heparin Sepharose 6 Fast Flow, Resource S, and Resource RPC purchased from GE Health Sciences (# 17-0998-01, #17-1178-01, and #17-1181-01, respectively). .. The purity of the prepared VEGF was greater than 95%, according to SDS PAGE and Coomassie blue staining.

Article Title: The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature *
Article Snippet: The GB1 portion was removed by Factor Xa proteolytic cleavage, separated by reverse phase chromatography on a Resource RPC 3-ml column (GE Healthcare), and eluted using an acetonitrile gradient in 0.1% TFA. .. SDS-PAGE analysis, HPLC/MS experiments, size exclusion chromatography, and NMR spectra confirmed the molecular weight and homogeneous purity of the protein samples.

Article Title: Comprehensive Experimental and Computational Analysis of Binding Energy Hot Spots at the NF-?B Essential Modulator (NEMO)/IKK? Protein-Protein Interface
Article Snippet: Successful cleavage of each IKKβ mutant was confirmed by SDS-PAGE ( ). .. We therefore purified each cleaved IKKβ peptide by reversed phase HPLC using a Resource RPC 3 ml column (GE Life Sciences), eluting with a linear gradient of 0–100% Buffer B over at least 45 minutes (Buffer A: 0.065% trifluoroacetic acid in water; Buffer B: 0.05% trifluoroacetic acid in methanol).

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  • 97
    GE Healthcare resource rpc column
    Elution profile from the Resource <t>RPC</t> column on <t>HPLC.</t> The peak corresponding to VDRBP is marked with an arrow. The acetonitrile gradient is also shown.
    Resource Rpc Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 97/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/resource rpc column/product/GE Healthcare
    Average 97 stars, based on 15 article reviews
    Price from $9.99 to $1999.99
    resource rpc column - by Bioz Stars, 2020-02
    97/100 stars
      Buy from Supplier

    94
    GE Healthcare resource rpc
    Biophysical characterization of PAS#1(600)-hGH. ( A ) Mass spectrometric analysis of PAS#1(600)-hGH by ESI-MS, confirming the calculated molecular mass of 73121.65 Da as well as precisely monodisperse composition, without any indication of prematurely terminated gene products. ( B ) Hydrophobicity analysis of PASylated hGH by reverse-phase (RP) HPLC. HIC of the original recombinant hGH and its PASylated version was performed on a Resource <t>RPC</t> column using an elution gradient from 2% v/v acetonitrile, 0.065% v/v <t>TFA</t> to 80% v/v acetonitrile, 0.05% v/v TFA. Both profiles show a single homogeneous peak with slightly earlier elution of PAS#1(600)-hGH (51.8% acetonitrile) in comparison with the corresponding unfused protein (52.3% acetonitrile). ( C ) Thermal denaturation of hGH and PAS#1(600)-hGH as determined by far UV CD measurement. Thermal unfolding of a 8.2 µM protein solution in 50 mM K 2 SO 4 , 20 mM K-P i pH 7.5 was followed at a wavelength of 208 nm where maximal spectral change upon unfolding was observed and the normalized unfolded fraction, f(u), was plotted as a function of temperature. The melting temperatures ( T m ) of hGH and PAS#1(600)-hGH were 85.4°C and 88.6°C, respectively.
    Resource Rpc, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/resource rpc/product/GE Healthcare
    Average 94 stars, based on 16 article reviews
    Price from $9.99 to $1999.99
    resource rpc - by Bioz Stars, 2020-02
    94/100 stars
      Buy from Supplier

    Image Search Results


    Elution profile from the Resource RPC column on HPLC. The peak corresponding to VDRBP is marked with an arrow. The acetonitrile gradient is also shown.

    Journal: Bulletin of the Korean Chemical Society

    Article Title: Recombinant Expression, Isotope Labeling and Purification of the Vitamin D Receptor Binding Peptide

    doi: 10.5012/bkcs.2011.32.12.4337

    Figure Lengend Snippet: Elution profile from the Resource RPC column on HPLC. The peak corresponding to VDRBP is marked with an arrow. The acetonitrile gradient is also shown.

    Article Snippet: Following the cleavage, the entire reaction mixture was loaded onto a Resource RPC column in 1 mL aliquots on HP1100 HPLC system.

    Techniques: High Performance Liquid Chromatography

    Biophysical characterization of PAS#1(600)-hGH. ( A ) Mass spectrometric analysis of PAS#1(600)-hGH by ESI-MS, confirming the calculated molecular mass of 73121.65 Da as well as precisely monodisperse composition, without any indication of prematurely terminated gene products. ( B ) Hydrophobicity analysis of PASylated hGH by reverse-phase (RP) HPLC. HIC of the original recombinant hGH and its PASylated version was performed on a Resource RPC column using an elution gradient from 2% v/v acetonitrile, 0.065% v/v TFA to 80% v/v acetonitrile, 0.05% v/v TFA. Both profiles show a single homogeneous peak with slightly earlier elution of PAS#1(600)-hGH (51.8% acetonitrile) in comparison with the corresponding unfused protein (52.3% acetonitrile). ( C ) Thermal denaturation of hGH and PAS#1(600)-hGH as determined by far UV CD measurement. Thermal unfolding of a 8.2 µM protein solution in 50 mM K 2 SO 4 , 20 mM K-P i pH 7.5 was followed at a wavelength of 208 nm where maximal spectral change upon unfolding was observed and the normalized unfolded fraction, f(u), was plotted as a function of temperature. The melting temperatures ( T m ) of hGH and PAS#1(600)-hGH were 85.4°C and 88.6°C, respectively.

    Journal: Protein Engineering, Design and Selection

    Article Title: PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins

    doi: 10.1093/protein/gzt023

    Figure Lengend Snippet: Biophysical characterization of PAS#1(600)-hGH. ( A ) Mass spectrometric analysis of PAS#1(600)-hGH by ESI-MS, confirming the calculated molecular mass of 73121.65 Da as well as precisely monodisperse composition, without any indication of prematurely terminated gene products. ( B ) Hydrophobicity analysis of PASylated hGH by reverse-phase (RP) HPLC. HIC of the original recombinant hGH and its PASylated version was performed on a Resource RPC column using an elution gradient from 2% v/v acetonitrile, 0.065% v/v TFA to 80% v/v acetonitrile, 0.05% v/v TFA. Both profiles show a single homogeneous peak with slightly earlier elution of PAS#1(600)-hGH (51.8% acetonitrile) in comparison with the corresponding unfused protein (52.3% acetonitrile). ( C ) Thermal denaturation of hGH and PAS#1(600)-hGH as determined by far UV CD measurement. Thermal unfolding of a 8.2 µM protein solution in 50 mM K 2 SO 4 , 20 mM K-P i pH 7.5 was followed at a wavelength of 208 nm where maximal spectral change upon unfolding was observed and the normalized unfolded fraction, f(u), was plotted as a function of temperature. The melting temperatures ( T m ) of hGH and PAS#1(600)-hGH were 85.4°C and 88.6°C, respectively.

    Article Snippet: Reverse-Phase HPLC The purified protein solution in PBS was adjusted to 2% v/v acetonitrile, 0.065% v/v trifluoroacetic acid (TFA) and 1 ml was applied to a Resource RPC 1 ml column (GE Healthcare) equilibrated with buffer A (2% v/v acetonitrile, 0.065% v/v TFA).

    Techniques: Mass Spectrometry, High Performance Liquid Chromatography, Hydrophobic Interaction Chromatography, Recombinant