Katalognummer: 209 - 100-191-AF
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 20 µg
100-191-AF
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-α is an acid-stable molecule that signals through IFN-α/βR, which is also used by IFN-β. Both IFNs have similar anti-viral activity and regulate expression of MHC class I antigens. IFN-α contains four highly conserved cysteine residues that form two disulfide bonds, one of which is necessary for biological activity. PeproTech’s Recombinant Human IFN-β is a 20.0 kDa protein containing 166 amino acid residues.
100-191S-AF
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-α is an acid-stable molecule that signals through IFN-α/βR, which is also used by IFN-β. Both IFNs have similar anti-viral activity and regulate expression of MHC class I antigens. IFN-α contains four highly conserved cysteine residues that form two disulfide bonds, one of which is necessary for biological activity. PeproTech’s Recombinant Human IFN-β is a 20.0 kDa protein containing 166 amino acid residues.
IHUIFNBRAFLY5UG
Human IFN-beta Recombinant Protein (Animal Free) Lyophilized
100-187-AF
Neuregulin/Heregulin is a family of structurally-related polypeptide growth factors derived from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). To date, there are over 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms releases soluble growth factors. HRG1-β1 contains an Ig domain and an EGF-like domain; the latter is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. This binding induces erb3 and erb4 heterodimerization with erb2, stimulating intrinsic kinase activity that leads to tyrosine phosphorylation. Although HRG1-β1's biological effects are still unclear, it has been found to promote motility and invasiveness of breast cancer cells, which may also involve up-regulation of expression and function of the autocrine motility-promoting factor (AMF). Recombinant Human Heregulinβ-1 (HRG1-B1) is a 7.5 kDa polypeptide consisting of only the EGF domain of heregulinβ-1 (65 amino acid residues).
100-187S-AF
Neuregulin/Heregulin is a family of structurally-related polypeptide growth factors derived from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). To date, there are over 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms releases soluble growth factors. HRG1-β1 contains an Ig domain and an EGF-like domain; the latter is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. This binding induces erb3 and erb4 heterodimerization with erb2, stimulating intrinsic kinase activity that leads to tyrosine phosphorylation. Although HRG1-β1's biological effects are still unclear, it has been found to promote motility and invasiveness of breast cancer cells, which may also involve up-regulation of expression and function of the autocrine motility-promoting factor (AMF). Recombinant Human Heregulinβ-1 (HRG1-B1) is a 7.5 kDa polypeptide consisting of only the EGF domain of heregulinβ-1 (65 amino acid residues).
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