. HILIC uses hydrophilic stationary phases with reversed-phase type. In hydrophobic interaction chromatography the matrix material is lightly substituted with hydrophobic groups. These groups can range from methyl, ethyl, propyl, octyl, or phenyl groups. At high salt concentrations, non-polar sidechains on the surface on proteins interact with the hydrophobic groups; that is, both types of groups are excluded by the polar solvent (hydrophobic effects are. The term hydrophobic interaction chromatography didn't appear until 1973 , but the groundwork for this separation mode was first reported in 1948 . At the time, it was well known that proteins can be precipitated using high concentrations of salts. The new twist was the observation that proteins adsorbed strongly to sorbents for which they would ordinarily have only weak affinity at salt concentrations much lower than would normally be required for precipitation. The first.
Hydrophobic Interaction Chromatography, a chemistry technique; Hic may refer to: The onomatopoeia for the sound made when hiccuping; See also. Hi-C (disambiguation Some argue that the hydrophobic interaction is mostly an entropic effect originating from the disruption of highly dynamic hydrogen bonds between molecules of liquid water by the nonpolar solute. A hydrocarbon chain or a similar nonpolar region of a large molecule is incapable of forming hydrogen bonds with water Reversed-phase chromatography (also called RPC, reverse-phase chromatography, or hydrophobic chromatography) includes any chromatographic method that uses a hydrophobic stationary phase. RPC refers to liquid (rather than gas) chromatography. Stationary phases. In the 1970s, most liquid chromatography was performed using a solid support stationary phase (also called a column) containing. Hydrophobic interaction chromatography (HIC) separates proteins according to differences in their surface hydrophobicity. HIC utilizes a reversible interaction between the proteins and the hydrophobic ligand of a HIC resin. The interaction between hydrophobic proteins and a HIC resin is greatly influenced by the running buffer Learn more about Hydrophobic Interaction Chromatography, an HPLC separation technique that separates proteins according to differences in their surface hydro..
Hydrophobic interaction chromatography (HIC) is a versatile method for the purification and separation of biomolecules by using the function of hydrophobicity. The proteins containing both hydrophilic and hydrophobic regions are applied to a HIC column under specified salt buffer conditions, which promotes the binding of the biomolecule to the HIC resin but also has a stabilizing influence on. chromatography such as. [...] gel-filtration or Size-Exclusion Chromatography (SEC), Ion Exch ange Chromatography (IEC), Hydrophobic Interaction Chromatography (HIC) and Affinity Chromatography, optek provides a wide variety of. [...
Hydrophobic Interaction Chromatography (HIC) Selection Guide. Promoting hydrophobic interactions (NH 4) 2 SO 4 Ammonium sulphate K 2 HPO 4 Potassium phosphate CH 3 COONa Sodium acetate NaCl Sodium chloride KSCN Potassium thiocyanate Cytochrome c RNAse A Lysozyme a-chymotrypsin UV absorbance Salt concentration Proteins separated in order of increasing surface hydrophobicity 2 29-0222-23 AA. Hydrophobic interaction chromatography (HIC) separates molecules based on their hydrophobicity. HIC is a useful separation technique for purifying proteins while maintaining biological activity due to the use of conditions and matrices that operate under less denaturing conditions. This section provides an overview of hydrophobic interaction chromatography with general considerations about. . The proteins are separated.
Illustration of Hydrophilic Interaction Chromatography and how it works on a particle level.HILIC is ideally suited for analysis of polar and hydrophilic com.. Hydrophobic interaction chromatography (HIC) is a widely used chromatographic technique that finds application at different stages of downstream processing. It was first described by Shepard and Tiselius in 1949 using the term salting out chromatography. The name HIC was later coined by Hjerten (1973), who was active in developing the technique. HIC is fundamentally different from other. HIC is a type of chromatography which exploits the phenomena of the interaction of hydrophobic groups with each other to prevent the interaction with the hydrophilic or polar groups. To simplify, the hydrophobic amino acids of any protein are buri.. Hydrophobic (interaction) chromatography. 3 III. DETERMINATION OF THE HYDROPHOBICITY OF BIOMOLECULES. It is well kno~vn that most proteins contain a relatively high proportion of amino acids ~dth non-polar chains (table I). Tanford , and TABLE I. Non-polar (hydrophobic) amino acids commonly found in proteins. AI anine CH 3 -R Leucine CH3x / CH-CH2-R CH 3 Isoleucine CH3-CH2-CH-R I CH 3. Analytical hydrophobic interaction chromatography (HIC), which is performed at high salt concentrations to enhance hydrophobic interactions, is an attractive assay for identifying mAbs with low hydrophobicity. However, this assay is low throughput and thus not amenable to processing the large numbers of mAbs that are commonly generated during antibody discovery. Therefore, we investigated.
Hydrophobic Interaction Chromatography (HIC) is a widely-used technique for separation and purification of proteins and peptides. HIC sorts biomolecules by degree of their surface hydrophobicity. Samples are adsorbed to the resin at relatively high salt concentrations and eluted by applying a decreasing salt gradient. The mild conditions used in HIC separation of peptides and proteins. . ISBN 91-970490-4-2. Many biotechnologists began their careers in chromatography reading Gel Filt-ration: Theory and Practice. First published in 1966, this monograph has had over 250,000 copies printed in five languages. It was soon followed by another helpful monograph from Amersham Pharmacia Biotech on ion exchange. About 15 years ago, Affinity. Hydrophobic interaction chromatography-high performance liquid chromatography (HIC-HPLC) is a powerful analytical method used for the separation of molecular variants of therapeutic proteins. The method has been employed for monitoring various post-translational modifications, including proteolytic fragments and domain misfolding in etanercept (Enbrel®); tryptophan oxidation, aspartic acid. Hydrophobic interaction chromatography (HIC) is a powerful technique used for purification of biomolecules on both the analytical and preparative scale. This chapter presents an overview of the basic principles of HIC and the different proposed theories for the retention mechanisms as well as the main parameters to consider for the optimization of this chromatographic technique. Additionally.
Hydrophobic Interaction Chromatography Hydrophobic Interaction Chromatography. Hydrophobic Interaction Chromatography (HIC) is a powerful tool for the process... Applications. HIC is an excellent complement to ion exchange and size exclusion chromatography, particularly when... TOYOPEARL HIC Resins.. This video reviews the concept of hydrophobic interaction column chromatography. In Lab 6 of the Amgen Biotech Experience curriculum, column chromatography. Here, previously published data for hydrophobic interaction chromatography and the formation of high molecular weight species are studied. Unsurprisingly, aromatic sidechain content of complementarity-determining regions (CDRs), underpins much of the variability in hydrophobic interaction chromatography data. However, this is not reflected in nonpolar solvent accessible surface enrichment at. Hydrophobic interaction chromatography (HIC) is used to separate molecules based on the differences of their surface hydrophobicity. This technology is widely used in chromatographic purification. It is orthogonal to other techniques like ion exchange or affinity. Hydrophobic interaction chromatography commonly requires high salt concentration for efficient binding of the target protein. Hydrophobic interaction chromatography (HIC) is a chromatographic technique for the purification and analysis of proteins. The separation is based on the interaction of hydrophobic regions of the proteins with a weakly hydrophobic stationary phase. The analytes are therefore separated according to the degree of their surface polarity. Proteins with high surface hydrophobicity are more strongly.
Hydrophobic interaction chromatography.Hydrophobic interactions between proteins and the chromatographic matrix can beHydrophobic molecules in the mobile phase tend to adsorb to the relatively hydrophobic stationary phase.Hydrophilic molecules which disrupts hydrophobic interactions), or changes in pH..In general, Hydrophobic Interaction Chromatography (HIC) is. Hydrophobic interaction chromatography of thrombin forms and preforms, using a polymeric phenyl column. A linear gradient of 2-0 M sodium chloride (5-20 min), in a 25 mM Tris-HCl buffer, pH 8.0, was used for elution. The flow-rate was 1 mL/min and detection was carried out by measuring the absorbance at 280 nm. (A) water blank, (B) α. Hydrophobic interaction chromatography. In the first experiment, 4 mg of IgG4-A were loaded to the phenyl-Sepharose (low-substituted) in 1 M AS, 10 mM phosphate, pH 6.0, which resulted in complete binding. Elution was initiated by decreasing AS concentration to 0.75 M AS in 10 mM phosphate, pH 6.0, resulting in elution of only a fraction of the protein applied (16%, first column) and the. Hydrophobic interaction chromatography (1) 1. Hydrophobic interaction chromatography 2. Alternatives • Gel filtration chromatography • Ion exchange chromatography • Reverse phase chromatography Why HIC? • Different basis of separation • Weaker interactions → Less structural damage → Maintain high activity 3. tainano.com 4. → Purpose → Principle of HIC → Advantages of using.
Hydrophobic interaction chromatography (HIC) Principles of HIC Main stages in HIC HIC Parameters for development optimization : ligand, salt concentration, etc Troubleshooting Example 28. Unexpected results 29 The ideal HIC separation: target protein is well resolved by gradient elution Target protein is eluted early in the gradient. Poor resolution. Repeat the separation at a higher salt. .
Hydrophobic Interaction Chromatography, HIC, Media, Reverse Phase Chromatography, RPC. What is Reverse Phase Chromatography. Reverse phase chromatography (RPC) is a chromatographic technique used in the purification and analysis of biomolecules such as proteins, peptides, and oligonucleotides. It gives a high-resolution separation and is ideal for the peptide mapping and purity checking. RPC. Hydrophobic Interaction Chromatography Market Data Breakdown with Revenue and Forecast Analysis 2020-2027. Fort Collins, Colorado: The Hydrophobic Interaction Chromatography Market report offers a detailed summary of the key factors, opportunities, challenges, current market trends, and methodologies that are affecting the global market. It enables the user to examine and discover longer-term. Hydrophobic interaction chromatography (HIC) In this method the adsorbents prepared as column material for the ligand binding in affinity chromatography are used. HIC technique is based on hydrophobic interactions between side chains bound to chromatography matrix [22, 23]. Pseudoaffinity chromatography . Some compounds as anthraquinone dyes, and azo-dyes can be used as ligands because of.
Hydrophobic interaction chromatography also proved an effective one-step purification procedure of LPS as was shown with a crude preparation from S-form S. typhimurium. Lipopolysaccharide (LPS) is a prominent essential amphi- phile in the outer membrane of Gram-negative bacteria. LPS from various bacteria is constructed according to a uniform principle [l]. The hydrophilic chain is composed of. We have shown that arginine reduces non-specific protein binding in gel permeation chromatography and facilitates elution of antibodies from Protein-A columns. Here we hav The effects of arginine on protein binding and elution in hydrophobic interaction and ion-exchange chromatography Protein Expr Purif. 2007 Jul;54(1):110-6. doi: 10 .1016/j. Hydrophobic Interaction Chromatography of Proteins, Nucleic Acids, Viruses, and Cells on Noncharged Amphiphilic Gels. Stellan Hjertén. Institute of Biochemistry, University of Uppsala, Biomedical Center, Uppsala, Sweden. Search for more papers by this author. Stellan Hjertén. Institute of Biochemistry, University of Uppsala, Biomedical Center, Uppsala, Sweden . Search for more papers by this. POROS Benzyl Hydrophobic Interaction Chromatography (HIC) Resin is a bioprocess high-performance resin engineered for improved impurity removal during large-scale downstream purification of biomolecules. This unique resin provides high resolution and capacity while maintaining excellent pressure flow characteristics, helping increase productivity. POROS Benzyl HIC Resin is designed on the well. In addition to characterizing heterogeneity, Hydrophobic Interaction Chromatography (HIC) is an assay that is often used to quantify the hydrophobicity of an antibody to assess downstream risks. Earlier studies have shown that retention times in this assay can be correlated to amino-acid or atomic propensities weighted by the surface areas obtained from protein 3-dimensional structures. The.
Hydrophobic Interaction Chromatography of Proteins and mAbs. Importance of Silica Particle Strength for Sub-2 µm SEC Columns. KB: Ferrules recommended for GC self-tightening column nut. LC Method Translation - the Dwell Volume. Minimize spectroscopy workflow disruptions. Minimizing Metals for Best HILIC Results . More than just a drink: Analyzing the elemental composition of beer. Multi. Hydrophobic Interaction Chromatography - Introduction • HIC is a powerful technique for separation and purification of bio molecules. • This technique was initially termed as Salting Out. • HIC is widely used for Protein purification, isolating protein complexes and studying protein folding and unfolding. www.technologyinscience.blogspot.com 4. Hydrophobic Interaction.
Hydrophobic interaction chromatography is a well-established method to purify proteins according to their surface charge and hydrophobicity. Chromatography matrices that provide a hydrophobic surface are used for separation. This method does not require any affinity tags to be fused to the protein to be purified. Therefore it is suitable for the purification of both native and recombinant. hydrophobic interaction chromatography (HIC) using Capto™ resins Downstream processes for biomolecule purification are becoming more complex. Challenges include increasing titers from upstream cell culture, greater diversity of target molecules, and a need for better productivity. HIC has characteristics designed to solve these challenges (1). Modern HIC resins are needed to meet the demands. Many translated example sentences containing hydrophobic interaction chromatography - French-English dictionary and search engine for French translations Hydrophobic interaction chromatography involves the separation of protein molecules owing to the differential interaction of these molecules with hydrophobic sites on the surface of a solid support. In the separation process, hydrophobic patches on the protein interact with hydrophobic molecules (e.g. alkyl residues) immobilized on the hydrophilic solid phase surface (agarose). Introduction.
Protein Interactions in Hydrophobic Charge Induction Chromatography (HCIC) Sanchayita Ghose. Purification Process Development, Amgen Inc., 1201 Amgen Court West, Seattle, Washington 98119 . Search for more papers by this author. Brian Hubbard. Purification Process Development, Amgen Inc., 1201 Amgen Court West, Seattle, Washington 98119. Search for more papers by this author. Steven M. Cramer. Welcome to Bio Basic Asia Pacific Pte Ltd; Tel: +65 6928 9042 | email@example.com Figure 1 - Hydrophobic interaction chromatography performed on plasmid solutions after 2.5M ammonium sulphate precipitation. Elution was isocratic with 1.5M ammonium sulphate in 10 mM Tris-HCl (pH.
ion-exchange chromatography (IEC) or hydrophobic interaction chromatography (HIC). To suﬃciently characterize the phase behavior of the protein and to meet the 'Time to Market' demands, high-throughput (HT) systems are the method of choice. Here, robot- based pipetting platforms are used to parallelize experiments in microliter scale to enable high-throughput screenings (HTS). Due to the. Hydrophobic interaction chromatography is a biological recognition process corresponding to a two‐dimensional lock‐and‐key model, that is, the dynamic pairing of a 2D key (protein) with its complementary 2D 'lock' (alkyl lattice). Proteins are adsorbed to hydrophobic agaroses as metastable states of adsorption-desorption hysteresis, indicating energetically that a local energy.
Hydrophobic interaction chromatography (HIC) is a powerful tool for the process purification of biomolecules. The technique utilizes the accessible hydrophobic regions located on protein surfaces and their interactions with a weakly hydrophobic stationary phase. HIC is an excellent complement to ion exchange and size exclusion chromatography particularly when protein isoforms exist or when. Hydrophobic interaction chromatography (HIC) is a commonly used technique that exploits these hydrophobic features of proteins as a basis for their separation even in complex biological mixtures (Queiroz et al., J Biotechnol 87:143-159, 2001; Eisenberg and McLachlan, Nature 319:199-203, 1986). In general, the conditions under which HIC is used are relatively mild and protein friendly. Hydrophobic interaction chromatography (HIC) is a rapid growing bioseparation technique, which separates biomolecules, such as therapeutic proteins and antibodys, based on the reversible hydrophobic interaction between immobilized hydrophobic ligands on chromatographic resin spheres and non-polar regions of solute molecule. In this review, the fundamental concepts of HIC and the factors that. Hydrophobic Interaction Chromatography. Hydrophobic interaction chromatography (HIC) is based on non-polar interactions that are induced by high salt mobile phases. Stationary phases are similar to reversed phase chromatography (RPC) but the density of functional groups is lower. A weakly non-polar stationary phase is used with an aqueous mobile phase containing a high concentration of a. InTech-Hydrophobic_interaction_chromatography_fundamentals_and_applications_in_biomedical_engineering.pdf. 26382.pdf. Content uploaded by Andrea Mahn. Author content. All content in this area was.
238000004191 hydrophobic interaction chromatography Methods 0.000 title claims abstract description 73 229920001184 polypeptide Polymers 0.000 claims abstract description 13 Hydrophobic interaction chromatography (HIC) occupies a unique niche as a polishing step in many monoclonal antibody (mAb) purification processes.1,2 This mode of chromatography is particularly useful for aggregate removal, and it provides good clearance of other process-related impurities such as host cell pro - tein (HCP), leached Protein A and endogenous viruses.3-6 HIC is based on. The present invention relates to a process for purifying polyethylene glycols (PEGs) which utilizes hydrophobic interaction chromatography (HIC) to separate the PEGs based on their size and on their end-group functionality. The purified PEGs can be used to modify biologically active molecules and improve overall production of such molecules A high‐throughput screen (HTS) was developed to evaluate the selectivity of various hydrophobic interaction chromatography (HIC) resins for separating a mAb from aggregate species. Prior to the resin screen, the solubility of the protein was assessed to determine the allowable HIC operating region by examining 384 combinations of pH, salt, and protein concentration. The resin screen then.
Hydrophobic Interaction Chromatography: Steps 1-3 1.Add bacterial lysate to column matrix in high salt buffer 2.Wash less hydrophobic proteins from column in low salt buffer 3.Elute GFP from column with no salt buffe Hydrophobic interaction chromatography (HIC) is a powerful technique for both analytical and preparative separations of bio-molecules. The technique takes advantage of the hydrophobic areas located on the surface of proteins. HIC is an excellent complement to size exclusion and ion exchange chromatography in difficult sepa- rations, particularly those in which the impurities are of similar. The global hydrophobic interaction chromatography resin market research report offers a summary of key players dominating the global market including several aspects such as their financial summary, business strategy, and most recent developments. **Note: The Values marked with $$ is confidential data. To know more about CAGR figures send mail so that our business development executive can get. Chromatography; General Laboratory Accessories; Laboratory Filtration; Liquid Preparation & Management; Molecular Biology ; Protein Analysis; Training; Special Offers. Special Offers and Discount Codes; New Lab Start-Up; Returns; Financing and Leasing; 60% Complete. Hydrophobic interaction columns. Shop; Chromatography products; Prepacked chromatography columns; Hydrophobic interaction columns. Hydrophobic Interaction Chromatography Market size reached US$ 291.3 Mn in 2017 and US$ 418.2 Mn by 2026, at a CAGR of 10.72 % during forecast period.. Hydrophobic Interaction Chromatography Market is segmented into products and services, sample type, and end-user, and region
Renata Muca, Wojciech Piątkowski and Dorota Antos, Altering efficiency of hydrophobic interaction chromatography by combined salt and temperature effects, Journal of Chromatography A, 10.1016/j.chroma.2009.04.046, 1216, 50, (8712-8721), (2009). Crossref . Jie Chen, Ting Yang. The Global Hydrophobic Interaction Chromatography Market is projected to grow at a healthy growth rate from 2018 to 2022 according to new research. The study focuses on market trends, leading. Hydrophobic Interaction Liquid Chromatography: Sorting Through the Hype December 12, 2014 by Karen Thorson chromatography industry, I have seen tremendous improvements in daily laboratory workflow through the years, in many cases, due to revolutionary products developed to save time and money for the researcher and provide more accurate and reproducible results day after day 238000004191 hydrophobic interaction chromatography Methods 0.000 title claims abstract description 64; 229920001184 polypeptides Polymers 0.000 claims abstract description 129; 239000000463 materials Substances 0.000 claims abstract description 7 Hydrophobic Interaction Chromatography (HIC) is a powerful tool for the process purification of biomolecules. The technique utilizes the accessible hydrophobic regions located on protein surfaces and their interactions with a weakly hydrophobic stationary phase. Proteins and other molecules with hydrophobic surfaces are attracted to the hydrophobic ligands of HIC resins by employing an aqueous.
Jennissen H (2005) Hydrophobic interaction chromatography: harnessing multi-valent protein-surface interactions for purification procedures. Methods Mol Biol 305:81-99 PubMed Google Scholar. 17. Ibrahim-Granet O, Bertrand O (1996) Separation of proteases: old and new approaches. J Chromatogr B-Biomed Appl 684:239-263 PubMed CrossRef Google Scholar. 18. Hofmeister F (1888) Zur lohre von der. So pH dependency in hydrophobic interaction chromatography could also be the result of pH dependent changes of ion properties from the salt solution. The possibility that pH dependent ion hydration or ion association in highly concentrated salt solutions may influence the dynamic protein binding capacity onto HIC resins was investigated. In buffer solutions commonly used in HIC e.g. sodium. Beschreibung in Englisch: Hydrophobic Interaction Chromatography. Andere Bedeutungen von HIC Neben Hydrophobe Interaktion Chromatographie hat HIC andere Bedeutungen. Sie sind auf der linken Seite unten aufgeführt. Bitte scrollen Sie nach unten und klicken Sie, um jeden von ihnen zu sehen. Für alle Bedeutungen von HIC klicken Sie bitte auf Mehr. Wenn Sie unsere englische Version besuchen. Hydrophobic interaction chromatography yielded preparations which were sufficiently pure for use in radioimmunoassays. By radioimmunoassay, the best antigens among the glycoproteins were moderately hydrophobic JAG III and the JAG IV complex. They had large amounts of antibody directed toward them in patients with schistosomiasis japonica and exhibited little reactivity with S. mansoni. The. Hydrophobic interaction chromatography (HIC) is an invaluable tool for . separating protein variants based on subtle differences in hydrophobicity. Unlike reversed-phase chromatography, which is performed under denaturing conditions, HIC is performed in aqueous eluents containing just salt and buffer, which keeps the protein in its native state. That's what makes the latest addition to the.
Introduction to hydrophobic interaction chromatography. Downstream processes for biomolecule purification are becoming more complex. Challenges include increasing titers from upstream cell culture, greater diversity of target molecules, and a need for better productivity. HIC has characteristics designed to solve these challenges (1). Modern HIC resins are needed to meet the demands of higher. We recently demonstrated that hydrophobic interaction chromatography (HIC) utilizing a MS-compatible salt can provide high resolution separation of intact proteins for top-down proteomics. Herein, we have developed a novel 3DLC strategy by coupling HIC with ion exchange chromatography (IEC) and reverse phase chromatography (RPC) for intact protein separation. We demonstrated that a 3D (IEC-HIC. Many translated example sentences containing hydrophobic interaction chromatography - Chinese-English dictionary and search engine for Chinese translations Hydrophobic interaction chromatography (HIC) represent one of the most widely used methods in enzyme purification. The expertise of Creative Enzymes on high-quality HIC will support your research demands. Hydrophobic interactions have a great importance in the biological systems. They are the dominant force in protein folding and structure stabilization, besides, it plays important roles in. Hydrophobic interaction chromatography resins: Capto Phenyl (high sub) Capto Phenyl ImpRes; Capto Butyl ImpRes; The growing need for deeper process understanding With the increased molecular diversity and drive for higher productivity, the challenge of getting deeper understanding for sources of variability and set mitigation strategies grows. Over the past decade, using a quality by design.
Hydrophobic interaction chromatography Substances are separated on the basis of their varying strengths of hydrophobic interactions with hydrophobic groups attached to an uncharged matrix. This technique is usually performed in the presence of moderately high concentrations of salts in the adsorption buffer (these salts promote adsorption and may have a stabilizing influence on protein. Great Separation! Highly recommended Product: PROTEIN KW-803 Application Area: Last step purification/buffer exchange of membrane proteins Rating: 5.0 The Fast and easy-to-use KW803 column has a high-quality performance making it possible to produce very pure protein
Hydrophobic Interaction Chromatography (HIC) Width Length Description Matrix (mm I.D.) (mm) Part Number BioSuite ™ Phenyl 10 µm HIC polymer 7.5 mm 75 mm 186002159 BioSuite™ Phenyl 13 µm HIC polymer 21.5 mm 150 mm 186002160 The separation of proteins and peptides based upon hydrophobic characteristics is a powerful chromatographic technique. However, some proteins denature at elevated. Automated Hydrophobic Interaction Chromatography Column Selection for Use in Protein Purification Article doi: 10.3791/3060. September 21st, 2011 • Usage Statistics. Patrick J. M. Murphy 1, Orrin J. Stone 2, Michelle E. Anderson 1. 1. In hydrophobic interaction chromatography (HIC), which is widely used for protein separation, a mildly hydrophobic stationary phase is employed with an aqueous salt solution as the mobile phase, and the magnitude of retention is modulated by the concentration of the salt. Retention is governed by the hydrophobic effect, which is attributed to the strongly ordered structure and high cohesive.
Hydrophobic interaction chromatography media, Butyl Sepharose™ HP Lieferant: Cytiva. Sepharose™ 17-5432-02EA 693 EUR. 17-5432-02. Hydrophobic interaction chromatography media, Butyl Sepharose™ HP. Proteinaufbereitungsmedien. Butyl Sepharose™ HP media is particularly well suited for intermediate purification and polishing steps providing high resolution due to the small particle size. Hydrophobic interaction chromatography (HIC) is commonly used to separate protein monomer and aggregate species in the purification of protein therapeutics. Despite being used frequently, the HIC separation mechanism is quite complex and not well understood. In this paper, we examined the separation of a monomer and aggregate protein mixture using Phenyl Sepharose FF La chromatographie à interaction hydrophile (HILIC) est une technique de chromatographie qui permet la séparation de petites molécules polaires. Elle requiert l'utilisation d'une phase mobile constituée d'un solvant organique miscible dans l'eau, souvent l'acétonitrile, et d'un tampon aqueux.La séparation est le résultat d'un partage ou une adsorption de l'analyte dans une couche. Hydrophobic Interaction Chromatography of mAbs and ADCs. Hydrophobic Interaction Chromatography of mAbs and ADCs.