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Secondary Antibodies

Secondary Antibodies

Tag Antibodies

Tag Antibodies

Tag Antibodies

Tag Antibodies

Tag Antibodies

Tag Antibodies

Tag Antibodies

Secondary Antibodies

Secondary Antibodies

Secondary Antibodies

Tag Antibodies

Tag Antibodies

Tag Antibodies

Tag Antibodies

Secondary Antibodies

Secondary Antibodies

Secondary Antibodies

Secondary Antibodies

Secondary Antibodies

Secondary Antibodies

Secondary Antibodies

Loading control Antibodies

Loading control Antibodies

Loading control Antibodies

Loading control Antibodies

Staphylococcal Protein A binds strongly and specifically to the Fc region of immunoglobulin molecules, especially IgG of many species such as Human, Rabbit, Pig, etc. The product contains five high affinity binding sites that are capable of interacting with the Fc region of IgG. HRP-Protein A is produced by covalently linking HRP to Protein A, which can be used in immuno-detection such as immunoblotting (Western or Dot blot), ELISA, and immunohistochemistry.

Protein G, a cell surface protein of Group G streptococci, is a Type III Fc receptor that binds to the Fc region of IgG by a non-immune mechanism similar to that of protein A. It contains 3 IgG binding domains and is engineered to delete albumin-binding region. HRP has been covalently coupled to Protein G to produce the HRP-Protein G, which can be used in detection systems such as immunoblotting, ELISA, immunoperoxidase electron microscopy and immunohistochemistry.

Protein L is a cell surface protein expressed by Peptostreptoccocus magnus, that binds to the variable light chains (kappa chains) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins such as protein A and protein G, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. HRP-Protein L is produced by covalently linking HRP to protein L. The complex can be used in immuno-detection such as immunoblotting (western or dot blot), ELISA, and immunohistochemistry.

Monoclonal Antibodies

Monoclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni²⁺ affinity resin.
Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni²⁺ affinity resin.
Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Recombinant PreScission Protease (rPSP) from human rhinovirus (HRV 3C) is a recombinant restriction-grade protease. PSP is a highly purified recombinant 6xHis-fusion protein, which recognizes the same cleavage site as the native enzyme. It is used to cleave affinity tags from fusion proteins. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro(LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. The optimal temperature for cleavage is 4°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of Recombinant PreScission Protease, reaction time, or incubation temperature. It can be removed by Ni²⁺ affinity resin.
Recombinant PreScission Protease (rPSP) contains 217 amino acids with N-terminal His tag. A fully biologically active molecule, rPSP has a molecular mass of 24 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Molecular/Enzyme Products

Molecular/Enzyme Products

Molecular Formula : C21H18N4O4S

Molecular Formula : C21H18N4O4S

Molecular Formula : C21H18N4O4S

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies