Affinity Columns(without media),12ml(1.5*8)

Affinity column empty column

Affinity chromatography is a chromatographic technique designed to take advantage of the specific affinity between biomolecules.

Such as antigens and antibodies, protein A and some antibodies, recombinant proteins and some metal ions, have a specific affinity, under certain conditions can be tightly combined into a complex, and this combination is reversible, change the conditions can be separated from each other.

When one side of a pair of molecules that can be bound (called a ligand) is bound to an inert carrier to make it solid, and the other side flows through the carrier with the mobile phase, the two sides are combined as a whole. They are then managed to dissociate them to obtain a specific substance that has a specific ability to bind to the ligand.

The affinity chromatography columns offered by Solarbio Biochem are specially designed for laboratory purification of antibodies, recombinant proteins or other molecules in small batches for further scientific research.

Affinity chromatography column The column used for the empty column is polypropylene plastic, this engineering material has been proven through a large number of applications with clean non-toxic, non-binding to biomolecules and low solubility advantages.

The sieve plate used in the empty column of affinity chromatography column is made of pure UHWMPE as raw material and processed by a unique process, which has hydrophilic properties. The screen plate is placed at the upper and lower ends of the filler matrix during loading to block the leakage of expensive matrix.

Hydrophilic sieve plate adopts the leading hydrophilic UHWMPE production technology, which can guarantee the flow rate of 1-2 ml/min or 1-2 drops/second when using gravity method. At the same time, compared with other suppliers, the sieve plate does not adsorb proteins due to the introduction of hydrophilic groups. In addition, the hydrophilic sieve plate is not easy to form bubbles during use, and the bubbles will reduce the flow rate and the liquid will not pass through the matrix evenly.

The empty column of the affinity chromatography column can be equipped with a syringe, a column pushing rod and a connecting tube, which is convenient for the filling of the column and the matching of the peristaltic pump and other equipment.

Empty affinity chromatography column for antibody purification

Staphylococcus aureus Protein A(SPA) can bind to Fc fragments of serum IgG molecules of human and A variety of mammals, and the affinity order of binding is pig, dog, rabbit, human, monkey, mouse, mouse and cow.

SPA, in addition to IgG, can also be combined with a small amount of IgM and IgA in serum, SPA bacteria on various types of immunoglobulin adsorption rate: IgG is 90% to 98%, IgM is 2% to 30%, IgA is 1.5% to 20%.

Purified antibodies generally use Protein A as the purified ligand, but can also use Protein G,Protein L, or allogeneic antibodies as the ligand.

Empty affinity Chromatography column for small molecule extraction

(Taking aflatoxin M1 extraction as an example)

Aflatoxin M1 was extracted when the sample passed the immunoaffinity column. The affinity column contains aflatoxin M1-specific monoclonal antibodies that are cross-linked to the solid support. When the sample passes through the affinity column, the antibodies selectively bind to aflatoxin M1(antigen) to form an antibody-antigen complex. Wash the column with water to remove the impurities in the column, and then elute aflatoxin M1 adsorbed on the column with eluent to collect the eluent. The content of aflatoxin M1 in eluent was determined by high performance liquid chromatograph with fluorescence detector.

Affinity Chromatography column Empty column for recombinant protein purification

In recent years, with the rapid development of biotechnology, especially genetic engineering technology, recombinant protein expression and purification are becoming easier and easier. The common expression strategy of recombinant protein is to fuse the protein with the affinity label and purify the target protein with the affinity label in one step. This method does not require knowledge of the biochemical properties or physiological activity of the protein, and can selectively bind to ligands on the chromatographic matrix through labeled recombinant fusion proteins, allowing the purification of any protein. This method differs from conventional chromatography in that there is no need to develop specific ligands and methods for different proteins. Under mild conditions to protect the structural and functional integrity of the protein, the recombinant protein can be purified from the crude extract by one-step affinity chromatography with a purity of more than 90%.

Affinity labeling has become a common method for purification of recombinant proteins in the post-genomics era. Affinity labeling systems generally have the following characteristics: (a) one-step adsorption and purification; (b) little effect on tertiary structure and biological activity; (c) can be conveniently and specifically removed to produce natural proteins; (d) The analysis of recombinant proteins in the purification process is simple and accurate; (e) Suitable for a large number of different proteins. However, no label is perfect and can only be screened according to actual needs. The following table is part of the labels and purification scheme.

Note：Product information may be optimized and upgraded. Please refer to the actual label information for accuracy.

Remark：These protocols are for reference only. Solarbio does not independently validate these methods.

Note：

1. The products are all for scientific research use only. Do not use it for medical, clinical diagnosis or treatment, food and cosmetics, etc. Do not store them in ordinary residential areas.

2. For your safety and health, please wear laboratory clothes, disposable gloves and masks.

3. The experimental results may be affected by many factors, after-sale service is limited to the product itself and does not involve other compensation.