277 Results for: "hydrophobic interaction"

Supplier: Cytiva

HiScreen Butyl HP columns are prepacked with Butyl Sepharose High Performance hydrophobic interaction chromatography (HIC) resins. The columns are an excellent choice for method optimization and parameter screening.

Supplier: Cayman Chemical Company

bis-ANS is a high-affinity non-covalent extrinsic fluorescent dye used to analyze protein conformation. Its predominant interaction with proteins is through its hydrophobic phenyl and naphthyl rings.

Supplier: Prosci

NECAP2 belongs to the NECAP family. The WXXF motifs mediate binding of accessory proteins to the ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions. Adaptin ear-binding coat-associated protein 2 can interacts with AP1G1 and AP2A1 components of the adapter protein complex AP-1 and AP-2. It also interacts with the GAE domain proteins GGA1, GGA2 and GGA3.

Supplier: Bio-Rad

Bio-Beads™ SM-2 adsorbents are analytical-grade, neutral macroporous polymeric beads with a high surface area for adsorbing organics with MW <2,000 from aqueous solutions. Mechanism: Hydrophobic interaction chromatography (HIC).

Supplier: Cytiva

HiTrap Butyl HP are prepacked Butyl Sepharose High Performance columns for high-resolution hydrophobic interaction chromatography (HIC). The columns are used for small-scale protein purification as well as for screening of binding and elution conditions.

Supplier: G-Biosciences

A selection of strong chemicals to aid in the denaturation of proteins. Denaturants, or chaotropes, disrupt water interactions resulting in the solubilization of hydrophobic proteins and peptides. The chaotropes also act on all proteins to unfold them and alter their three-dimensional structure.

Supplier: Cytiva

RESOURCE ISO are prepacked SOURCE 15 ISO (isopropyl) columns for purification of proteins and peptides with hydrophobic interaction chromatography (HIC). For fast, high-resolution purifications, RESOURCE columns are excellent choice for polishing and removal of trace impurities.

Supplier: Cytiva

RESOURCE PHE are prepacked SOURCE 15 PHE (phenyl) columns for purification of proteins and peptides with hydrophobic interaction chromatography (HIC). For fast, high-resolution purifications, RESOURCE columns are excellent choice for polishing and removal of trace impurities.

Supplier: G-Biosciences

A selection of strong chemicals to aid in the denaturation of proteins. Denaturants, or chaotropes, disrupt water interactions resulting in the solubilization of hydrophobic proteins and peptides. The chaotropes also act on all proteins to unfold them and alter their three-dimensional structure.

Supplier: Chem-Impex International

Fmoc-(S)-3-amino-3-(1-naphthyl)propionic acid is a key building block in peptide synthesis, offering unique properties for drug development and research. Ideal for creating bioactive peptides, it enhances hydrophobic interactions and stability, making it essential for innovative therapeutic applications.

Supplier: Cytiva

The Capto hydrophobic interaction chromatography (HIC) selection kit has a set of five 1 ml ready-to-use HiTrap™ columns for resin screening and small-scale protein purification. The HiTrap™ Capto HIC selection kit is useful in process development or research applications.

Supplier: Cytiva

Naturally hydrophobic PVDF, ideal for a wide variety of protein-analysis applications. The family of FluroTrans® media are white, microporous solid phase supports that bind proteins tenaciously via hydrophobic interactions. FluoroTrans® membrane is optimised for N-terminal protein sequencing. FluoroTrans® W membranes are optimised for Western transfer applications. They allow for sensitive protein detection with low background and very low protein burn-through. Immobilised proteins can be visually detected with Coomassie® Blue, Amido black, Ponceau S, and colloidal gold.

Supplier: Avantor

Avantor® ACE® CN-ES combines CN polar selectivity with enhanced hydrophobicity, enabling the benefits of both interactions to be fully exploited. Extra phase stability and increased column lifetime is provided by an extended alkyl chain spacer between the silica surface and cyano group. Avantor® ACE® CN-ES is suitable for both reversed phase and normal phase separations.

Supplier: Avantor

Avantor® ACE® CN-ES combines CN polar selectivity with enhanced hydrophobicity, enabling the benefits of both interactions to be fully exploited. Extra phase stability and increased column lifetime is provided by an extended alkyl chain spacer between the silica surface and cyano group. Avantor® ACE® CN-ES is suitable for both reversed phase and normal phase separations.

Supplier: Avantor

Avantor® ACE® CN-ES combines CN polar selectivity with enhanced hydrophobicity, enabling the benefits of both interactions to be fully exploited. Extra phase stability and increased column lifetime is provided by an extended alkyl chain spacer between the silica surface and cyano group. Avantor® ACE® CN-ES is suitable for both reversed phase and normal phase separations.

Supplier: Avantor

Avantor® ACE® CN-ES combines CN polar selectivity with enhanced hydrophobicity, enabling the benefits of both interactions to be fully exploited. Extra phase stability and increased column lifetime is provided by an extended alkyl chain spacer between the silica surface and cyano group. Avantor® ACE® CN-ES is suitable for both reversed phase and normal phase separations.

Supplier: Avantor

Avantor® ACE® CN-ES combines CN polar selectivity with enhanced hydrophobicity, enabling the benefits of both interactions to be fully exploited. Extra phase stability and increased column lifetime is provided by an extended alkyl chain spacer between the silica surface and cyano group. Avantor® ACE® CN-ES is suitable for both reversed phase and normal phase separations.

Supplier: Avantor

Avantor® ACE® CN-ES combines CN polar selectivity with enhanced hydrophobicity, enabling the benefits of both interactions to be fully exploited. Extra phase stability and increased column lifetime is provided by an extended alkyl chain spacer between the silica surface and cyano group. Avantor® ACE® CN-ES is suitable for both reversed phase and normal phase separations.

Supplier: Avantor

Avantor® ACE® CN-ES combines CN polar selectivity with enhanced hydrophobicity, enabling the benefits of both interactions to be fully exploited. Extra phase stability and increased column lifetime is provided by an extended alkyl chain spacer between the silica surface and cyano group. Avantor® ACE® CN-ES is suitable for both reversed phase and normal phase separations.

Supplier: Genetex

Influenza viruses are a common and widely spread infectious agent. Like many other viruses, influenza virus are constantly undergoing mutations and thereby avoiding the immune system. The Influenza A Virus M proteins form a continuous shell on the inner side of the lipid bilayer, maintaining the structural integrity of the virus particle through hydrophobic interactions.

Supplier: Genetex

Influenza viruses are a common and widely spread infectious agent. Like many other viruses, influenza virus are constantly undergoing mutations and thereby avoiding the immune system. The Influenza A Virus M proteins form a continuous shell on the inner side of the lipid bilayer, maintaining the structural integrity of the virus particle through hydrophobic interactions.

Supplier: Anaspec

GALA is a 30 amino acid synthetic peptide with a glutamic acid-alanine-leucine-alanine (EALA) repeat. It also contains a histidine and tryptophan residue as spectroscopic probes. This peptide was designed to explore how viral fusion protein sequences interact with membranes. It was used to study the importance of the helix length, hydrophobicity, and hydrophobic moment on the formation, structure, and function of ion channels. The membrane-interacting properties of GALA have been extensively documented. Investigations with analogs of cytotoxic peptides clarify the importance of peptide charge and the role of particular amino acids or arrays of amino acids in the conformation, membrane-binding affinity, and pore-forming abilities of these toxins.
Sequence:WEAALAEALAEALAEHLAEALAEALEALAA
MW:3032.4 Da
% peak area by HPLC:95
Storage condition:-20° C

Supplier: Prosci

Endoplasmic reticulum resident protein 27, also known as ER protein 27, C12orf46 and ERP27, is an endoplasmic reticulum luminal protein which is a member of the protein disulfide isomerase family. ERP27 contains one thioredoxin domain and does not contain a CXXC active site motif. ERP27 is widely expressed in many tissues; it has highest expression in pancreas, with lower levels in spleen, lung, kidney, thymus, and bone marrow. ERP27 interacts with PDIA3 and binds somatostatin-14 via hydrophobic interactions. ERP27 may act as a protease, protein disulfide isomerase, thiol-disulfide oxidase or phospholipase.

Supplier: Prosci

Myelin Protein P0 (MPZ) is a single-pass type I membrane glycoprotein which belongs to the myelin P0 protein family. MPZ contains one Ig-like V-type (immunoglobulin-like) domain, absent in the central nervous system. MPZ is a major component of the myelin sheath in peripheral nerves. It is postulated that MPZ is a structural element in the formation and stabilisation of peripheral nerve myelin, holding its characteristic coil structure together by the interaction of its positively-charged domain with acidic lipids in the cytoplasmic face of the opposed bilayer, and by interaction between hydrophobic globular of adjacent extracellular domains. Defects in MPZ associated with Charcot-Marie-Tooth disease and Dejerine-Sottas disease.

Supplier: Prosci

NR0B2 is an unusual orphan receptor that contains a putative ligand-binding domain but lacks a conventional DNA-binding domain. It is a member of the nuclear hormone receptor family, a group of transcription factors regulated by small hydrophobic hormones, a subset of which do not have known ligands and are referred to as orphan nuclear receptors. The protein has been shown to interact with retinoid and thyroid hormone receptors, inhibiting their ligand-dependent transcriptional activation. In addition, interaction with estrogen receptors has been demonstrated, leading to inhibition of function. Studies suggest that the protein represses nuclear hormone receptor-mediated transactivation via two separate steps: competition with coactivators and the direct effects of its transcriptional repressor function.The protein encoded by this gene is an unusual orphan receptor that contains a putative ligand-binding domain but lacks a conventional DNA-binding domain. The gene product is a member of the nuclear hormone receptor family, a group of transcription factors regulated by small hydrophobic hormones, a subset of which do not have known ligands and are referred to as orphan nuclear receptors. The protein has been shown to interact with retinoid and thyroid hormone receptors, inhibiting their ligand-dependent transcriptional activation. In addition, interaction with estrogen receptors has been demonstrated, leading to inhibition of function. Studies suggest that the protein represses nuclear hormone receptor-mediated transactivation via two separate steps: competition with coactivators and the direct effects of its transcriptional repressor function. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Prosci

Karyopherin Subunit alpha-2 (KPNA2) belongs to the importin alpha family. KPNA2 is widely expressed in many tissues and contains an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. KPNA2 interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V(D)J recombination. KPNA2 functions in nuclear protein importantly as an adapter protein for nuclear receptor KPNB1.

Supplier: Prosci

NR0B2 is an unusual orphan receptor that contains a putative ligand-binding domain but lacks a conventional DNA-binding domain. It is a member of the nuclear hormone receptor family, a group of transcription factors regulated by small hydrophobic hormones, a subset of which do not have known ligands and are referred to as orphan nuclear receptors. The protein has been shown to interact with retinoid and thyroid hormone receptors, inhibiting their ligand-dependent transcriptional activation. In addition, interaction with estrogen receptors has been demonstrated, leading to inhibition of function. Studies suggest that the protein represses nuclear hormone receptor-mediated transactivation via two separate steps: competition with coactivators and the direct effects of its transcriptional repressor function. The protein encoded by this gene is an unusual orphan receptor that contains a putative ligand-binding domain but lacks a conventional DNA-binding domain. The gene product is a member of the nuclear hormone receptor family, a group of transcription factors regulated by small hydrophobic hormones, a subset of which do not have known ligands and are referred to as orphan nuclear receptors. The protein has been shown to interact with retinoid and thyroid hormone receptors, inhibiting their ligand-dependent transcriptional activation. In addition, interaction with estrogen receptors has been demonstrated, leading to inhibition of function. Studies suggest that the protein represses nuclear hormone receptor-mediated transactivation via two separate steps: competition with coactivators and the direct effects of its transcriptional repressor function. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Genetex

Influenza A and B are the two types of influenza viruses that cause epidemic human disease. Influenza type C infections cause a mild respiratory illness and are not thought to cause epidemics. Influenza A viruses are further categorized into subtypes on the basis of two surface antigens: hemagglutinin (H) and neuraminidase (N). Strains are also described by geographic origin, strain number and year of isolation. This protein forms a continuous shell on the inner side of the lipid bilayer. Maintains the structural integrity of the virus particle through hydrophobic interactions. Also mediates the encapsidation of RNA nucleoprotein cores into the membrane envelope.

Supplier: Genetex

Influenza A and B are the two types of influenza viruses that cause epidemic human disease. Influenza type C infections cause a mild respiratory illness and are not thought to cause epidemics. Influenza A viruses are further categorized into subtypes on the basis of two surface antigens: hemagglutinin (H) and neuraminidase (N). Strains are also described by geographic origin, strain number and year of isolation. This protein forms a continuous shell on the inner side of the lipid bilayer. Maintains the structural integrity of the virus particle through hydrophobic interactions. Also mediates the encapsidation of RNA nucleoprotein cores into the membrane envelope.

Supplier: MP Biomedicals

Guanidine Hydrochloride is a protein denaturant and thus having an important role in molecular weight determinations.
Guanidine Hydrochloride is a strong chaotropic agent useful for the denaturation and subsequent refolding of proteins. This strong denaturant can solubilize insoluble or denatured proteins such as inclusion bodies. This can be used as the first step in refolding proteins or enzymes into their active form. Urea and dithiothreitol (DTT) may also be necessary. Guanidine HCl is used in the isolation of RNA to dissociate the nucleoprotein into its nucleic acid and protein moieties. It is an inhibitor of RNase. Highly concentrated (6 - 8 M) Guanidine HCl solutions are used to denature native globular proteins. It apparently disrupts hydrogen bonds which hold the protein in its unique structure. However, there also is evidence suggesting that guanidine hydrocholoride may disrupt hydrophobic interactions by promoting the solubility of hydrophobic residues in aqueous solutions.