Results for Other Proteins ( 64690 )
Recombinant Human IFN-beta (Legacy Tebubio ref. 167300-02BC). Proteins of this family play an important role in inducing non-specific resistance against a broad range of viral infections. They also affect cell proliferation and modulate immune responses. Produced by peripheral blood leukocytes and lymphoblastoid cells, IFN-alpha is an acid-stable molecule that signals through IFN-alpha/betaR, which is also used by IFN-beta. Both IFNs have similar anti-viral activity and regulate expression of MHC class I antigens. IFN-alpha contains four highly conserved cysteine residues that form two disulfide bonds, one of which is necessary for biological activity. PeproTech's Recombinant Human IFN-beta is a 20.0 kDa protein containing 166 amino acid residues. Due to glycosylation, IFN-beta has an approximate MW of 22.3 kDa based on SDS-PAGE gel and Mass Spectrometry. *Human IFN-beta (Catalog Number 300-02BC) has replaced Human IFN-beta (Catalog Number 300-02B)
Recombinant Human IFN-beta (Legacy Tebubio ref. 167300-02BC). Proteins of this family play an important role in inducing non-specific resistance against a broad range of viral infections. They also affect cell proliferation and modulate immune responses. Produced by peripheral blood leukocytes and lymphoblastoid cells, IFN-alpha is an acid-stable molecule that signals through IFN-alpha/betaR, which is also used by IFN-beta. Both IFNs have similar anti-viral activity and regulate expression of MHC class I antigens. IFN-alpha contains four highly conserved cysteine residues that form two disulfide bonds, one of which is necessary for biological activity. PeproTech's Recombinant Human IFN-beta is a 20.0 kDa protein containing 166 amino acid residues. Due to glycosylation, IFN-beta has an approximate MW of 22.3 kDa based on SDS-PAGE gel and Mass Spectrometry. *Human IFN-beta (Catalog Number 300-02BC) has replaced Human IFN-beta (Catalog Number 300-02B)
Recombinant Human IFN-omega (Legacy Tebubio ref. 167300-02J). IFN-omega is a type I interferon that can be induced by virus-infected leukocytes. Members of the type I interferon family, which includes IFN-alpha, IFN-beta, and IFN-omega, signal through the IFNAR-1/IFNAR-2 receptor complex, and exert antiviral and antiproliferative activities. IFN-omega exhibits about 75% sequence homology with IFN-alpha, and contains two conserved disulfide bonds that are necessary for full biological activity. Recombinant Human IFN-omega is a 19.9 kDa protein consisting of 172 amino acid residues.
Recombinant Human IFN-omega (Legacy Tebubio ref. 167300-02J). IFN-omega is a type I interferon that can be induced by virus-infected leukocytes. Members of the type I interferon family, which includes IFN-alpha, IFN-beta, and IFN-omega, signal through the IFNAR-1/IFNAR-2 receptor complex, and exert antiviral and antiproliferative activities. IFN-omega exhibits about 75% sequence homology with IFN-alpha, and contains two conserved disulfide bonds that are necessary for full biological activity. Recombinant Human IFN-omega is a 19.9 kDa protein consisting of 172 amino acid residues.
Recombinant Human IFN-lambda2 (Legacy Tebubio ref. 167300-02K). IFN-lambda1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the IL-10 family and interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN-lambdaR1 subunit (also called CRF2-12) and IL-10R2 subunit (also called CRF2-14). Signaling through this receptor system induces antiviral defenses similar to, but distinct from, than that of type I interferons. Recombinant Human IFN-lambda2 is a 19.6 kDa protein containing 174 amino acid residues.
Recombinant Human IFN-lambda2 (Legacy Tebubio ref. 167300-02K). IFN-lambda1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the IL-10 family and interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN-lambdaR1 subunit (also called CRF2-12) and IL-10R2 subunit (also called CRF2-14). Signaling through this receptor system induces antiviral defenses similar to, but distinct from, than that of type I interferons. Recombinant Human IFN-lambda2 is a 19.6 kDa protein containing 174 amino acid residues.
Recombinant Human IFN-lambda1 (Legacy Tebubio ref. 167300-02L). IFN-lambda1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the IL-10 family and the interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN-lambdaR1 subunit (also called CRF2-12) and IL-10R2 subunit (also called CRF2-14). Signaling through this receptor system induces antiviral defenses similar to, but distinct from, that of type I interferons. Recombinant Human IFN-lambda1 is a 19.8 kDa protein containing 178 amino acid residues.
Recombinant Human IFN-lambda1 (Legacy Tebubio ref. 167300-02L). IFN-lambda1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the IL-10 family and the interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN-lambdaR1 subunit (also called CRF2-12) and IL-10R2 subunit (also called CRF2-14). Signaling through this receptor system induces antiviral defenses similar to, but distinct from, that of type I interferons. Recombinant Human IFN-lambda1 is a 19.8 kDa protein containing 178 amino acid residues.
Recombinant Human GM-CSF (Legacy Tebubio ref. 167300-03). GM-CSF is a hematopoietic growth factor that stimulates the development of neutrophils and macrophages, and promotes the proliferation and development of early erythroid megakaryocytic and eosinophilic progenitor cells. It is produced in endothelial cells, monocytes, fibroblasts and T-lymphocytes. GM-CSF inhibits neutrophil migration and enhances the functional activity of the mature end-cells. The human and murine molecules are species-specific and exhibit no cross-species reactivity. Recombinant Human GM-CSF is a 14.6 kDa globular protein consisting of 128 amino acids, containing two intramolecular disulfide bonds and two potential N-linked glycosylation sites.