649 Results for: "ion exchange ion exchange chromatography"

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Aladdin Scientific

CHAPS is a non-denaturing, zwitterionic detergent derived from cholic acid. CHAPS is often used as a detergent in the solubilization and purification of membrane proteins for several advantageous reasons. CHAPS detergent is non-denaturing to membrane proteins, can solubilize proteins, disaggregate protein-protein interactions and is electrically neutral. CHAPS is also useful in ion exchange chromatography and isoelectric focusing as it is zwitterionic and does not exhibit a net charge between pH 2 to 12.

Supplier: MP Biomedicals

Peroxidase-conjugated goat IgG fraction to rabbit IgG (whole molecule) is the lyophilized powder of horseradish peroxidase (HRP)-conjugated goat IgG fraction to rabbit IgG (whole molecule) and buffer salts. Anti-Human IgG is developed in goat using IgG from pooled normal human serum as the immunogen. Whole antiserum is fractionated and then further purified by ion exchange chromatography to provide the IgG fraction of antiserum. This fraction is essentially free of other goat serum proteins.

Specificity for human IgG is determined by immunoelectrophoresis (IEP) versus purified human IgA, IgG, IgM, Bence Jones kappa, and Bence Jones lambda myeloma proteins. Identity and purity of the antibody is established by immunoelectrophoresis (IEP), prior to conjugation. Electrophoresis of the antibody preparation followed by diffusion versus anti-goat IgG and anti-goat whole serum result in single arcs of precipitation in the gamma region.

Peroxidase-conjugated goat IgG fraction to rabbit IgG (whole molecule) product is suitable for use as a reagent in enzyme immunoassays (EIA), cell and tissue staining (for light microscopy), cell and tissue labeling (for electron microscopy), and blot immunostaining. Note: F(ab')2 fragments are recommended for staining of cells or tissues which contain Fc receptors. Affinity purified antibodies or their fragments are recommended to avoid non-specific binding from inherent antibodies of host animals.

Antibody and highly purified HRP (Rz>3.0) are conjugated under defined conditions to obtain optimally labeled product. Conjugated protein is purified by salt fractionation. The product is dialyzed into 0.02M sodium phosphate, 0.14M sodium chloride, pH 7.3, adjusted to standard titer, filtered through a 0.22 µm filter, vialed and lyophilized.

The total protein is measured using the Biuret procedure with bovine albumin as the standard. To ensure that the product titer falls within the required range, antibody titer is standardized by microtiter plate ELISA with rabbit IgG. The product is tested for purity and specificity at final concentration by immunoelectrophoresis. The antibody is predominantly goat IgG; no trace of albumin is detected.

Supplier: Avantor

Avantor® Hichrom Anion/S columns are based on 10 µm silica with quaternary ammonium ion-exchange groups.

Supplier: Thermo Scientific

Fast ion-exchange separation and protein purification is possible using the Thermo Scientific™ ProSwift ion exchange (IEX) columns.

Supplier: Thermo Scientific

Fast ion-exchange separation and protein purification is possible using the Thermo Scientific™ ProSwift ion exchange (IEX) columns.

Supplier: Thermo Scientific

Fast ion-exchange separation and protein purification is possible using the Thermo Scientific™ ProSwift ion exchange (IEX) columns.

Supplier: Sepax Technologies

Proteomix ion-exchange phases have been innovatively developed for achieving high ion-exchange capacity, a breakthrough technology for non-porous resins.

Supplier: AVANTOR PERFORMANCE MATERIAL LLC

Disposable polypropylene columns are prepacked with selective reversed phase, polar, and ion exchange organosilanes bonded to 40 µm, 60 Å, and 275 Å silica gel absorbents and size exclusion gels.

Supplier: Cytiva

HiTrap Capto MMC is prepacked with Capto MMC, a multimodal BioProcess ion exchange resin. The multimodal functionality gives a different selectivity compared with traditional ion exchangers and it binds proteins at high or low ionic strength.

Supplier: Ace Glass

Unit is designed for metal recovery using ion-exchange resins such as amborane.