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Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Monoclonal Antibodies

Monoclonal Antibodies

Protein L is a cell surface protein from Peptostreptoccocus magnus that binds to the variable light chains (kappa chain) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins, such as protein A and protein G, which bind to the Fc region of immunoglobulins, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L.

Protein L is a cell surface protein from Peptostreptoccocus magnus that binds to the variable light chains (kappa chain) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins, such as protein A and protein G, which bind to the Fc region of immunoglobulins, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L.

Protein L is a cell surface protein from Peptostreptoccocus magnus that binds to the variable light chains (kappa chain) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins, such as protein A and protein G, which bind to the Fc region of immunoglobulins, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L.

Protein L is a cell surface protein from Peptostreptoccocus magnus that binds to the variable light chains (kappa chain) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins, such as protein A and protein G, which bind to the Fc region of immunoglobulins, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L.

Monoclonal Antibodies

Monoclonal Antibodies

Monoclonal Antibodies

Monoclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Monoclonal Antibodies

Monoclonal Antibodies

Monoclonal Antibodies

Monoclonal Antibodies

Monoclonal Antibodies

Monoclonal Antibodies

Polyclonal Antibodies

Polyclonal Antibodies

Monoclonal Antibodies

Monoclonal Antibodies

At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.

At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.

Interferon-Alpha 2a (IFN-Alpha 2a), Human produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2a shares 99.4% , 98.8% aa sequence identity with IFN-alpha 2b and 2c respectively. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-Alpha 2a (IFN-Alpha 2a), Human produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2a shares 99.4% , 98.8% aa sequence identity with IFN-alpha 2b and 2c respectively. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-Alpha 2a (IFN-Alpha 2a), Human produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2a shares 99.4% , 98.8% aa sequence identity with IFN-alpha 2b and 2c respectively. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-Alpha 2b (IFN-Alpha 2b) produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2b shares 99.4% aa sequence identity with both IFN-alpha 2a and 2c. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-Alpha 2b (IFN-Alpha 2b) produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2b shares 99.4% aa sequence identity with both IFN-alpha 2a and 2c. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-Alpha 2b (IFN-Alpha 2b) produced by leukocytes is a member of Interferon family. IFN-alpha is mainly involved in innate immune response against a broad range of viral infections. IFN-alpha 2 has three acid stable forms (a,b,c) signaling through IFNAR2. IFN-alpha 2b shares 99.4% aa sequence identity with both IFN-alpha 2a and 2c. IFN-alpha contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity.

Interferon-beta (IFN-β), acting via STAT1 and STAT2, is known to upregulate and downregulate a wide variety of genes, most of which are involved in the antiviral immune response. It is a member of Type I IFNs, which include IFN-α, -β, τ, and –ω. IFN-β plays an important role in inducing non-specific resistance against a broad range of viral infections. It also affects cell proliferation and modulates immune responses.

Interferon-beta (IFN-β), acting via STAT1 and STAT2, is known to upregulate and downregulate a wide variety of genes, most of which are involved in the antiviral immune response. It is a member of Type I IFNs, which include IFN-α, -β, τ, and –ω. IFN-β plays an important role in inducing non-specific resistance against a broad range of viral infections. It also affects cell proliferation and modulates immune responses.

IFN-gamma Receptor II, also known as IFNGR2 and IFNGT1, is a transmembrane protein belonging to the type II cytokine receptor family. IFNGR2 is a non-ligand-binding beta chain of the IFN-gamma receptor. It is an integral part of the IFN-gamma signaling transduction pathway and is likely to interact with GAF, JAK1 and JAK2. Defects in IFNGR2 are a cause of autosomal recessive Mendelian susceptibility to mycobacterial disease (MSMD), also known as familial disseminated atypical mycobacterial infection.

IFN-gamma Receptor II, also known as IFNGR2 and IFNGT1, is a transmembrane protein belonging to the type II cytokine receptor family. IFNGR2 is a non-ligand-binding beta chain of the IFN-gamma receptor. It is an integral part of the IFN-gamma signaling transduction pathway and is likely to interact with GAF, JAK1 and JAK2. Defects in IFNGR2 are a cause of autosomal recessive Mendelian susceptibility to mycobacterial disease (MSMD), also known as familial disseminated atypical mycobacterial infection.