描述：
Human GROα, GROβ (MIP-2α), and GROγ (MIP-2β) are products of three distinct, non-allelic
human genes. GROβ and GROγ share 90% and 86% amino acid (aa) sequence homology,
respectively, with GROα. All three human GROs are members of the alpha (C-X-C) subfamily
of chemokines and are thought to be the homologs of the murine KC, and MIP-2.The three
GRO cDNAs encode 107 aa precursor proteins from which the N-terminal 34 aa residues are
cleaved to generate the mature GROs. There are no potential N-linked glycosylation sites in the
aa sequences. GRO expression is inducible by serum, PDGF and/or by a variety of inflammatory
mediators, such as IL-1 and TNF, in monocytes, fibroblasts, melanocytes and epithelial cells. In
certain tumor cell lines, GRO is expressed constitutively.Similarly to other alpha chemokines,
the three GRO proteins are potent neutrophil attractants and activators. In addition, these
chemokines are also active toward basophils. All three GROs can bind with high affinity to
CXCR2. The 69 aa variant of human GROβ is approximately 3 times more active than the 73
aa variant (R&D Systems, Catalog # 276-GB) in inducing myeloperoxidase release from
cytochalasin B treated neurotrophils.
原厂资料：
Human GROα, GROβ (MIP-2α), and GROγ (MIP-2β) are products of three distinct, non-allelic
human genes. GROβ and GROγ share 90% and 86% amino acid (aa) sequence homology,
respectively, with GROα. All three human GROs are members of the alpha (C-X-C) subfamily
of chemokines and are thought to be the homologs of the murine KC, and MIP-2.The three
GRO cDNAs encode 107 aa precursor proteins from which the N-terminal 34 aa residues are
cleaved to generate the mature GROs. There are no potential N-linked glycosylation sites in the
aa sequences. GRO expression is inducible by serum, PDGF and/or by a variety of inflammatory
mediators, such as IL-1 and TNF, in monocytes, fibroblasts, melanocytes and epithelial cells. In
certain tumor cell lines, GRO is expressed constitutively.Similarly to other alpha chemokines,
the three GRO proteins are potent neutrophil attractants and activators. In addition, these
chemokines are also active toward basophils. All three GROs can bind with high affinity to
CXCR2. The 69 aa variant of human GROβ is approximately 3 times more active than the 73
aa variant (R&D Systems, Catalog # 276-GB) in inducing myeloperoxidase release from
cytochalasin B treated neurotrophils.
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