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16006 Ensembl ENSG00000146678 ENSMUSG00000020429 UniProt P08833 P47876 RefSeq (mRNA) NM_001013029 NM_000596 NM_008341 RefSeq (protein) NP_000587 NP_032367 Location (UCSC) Chr 7: 45.89 – 45.89 Mb Chr 11: 7.15 – 7.15 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Insulin-like growth factor-binding protein 1 (IBP-1) also known as placental protein 12 (PP12) is a protein that in ...
Insulin-like growth factor-binding protein 7 is a protein that in humans is encoded by the IGFBP7 gene. [ 5 ] [ 6 ] [ 7 ] The major function of the protein is the regulation of availability of insulin-like growth factors (IGFs) in tissue as well as in modulating IGF binding to its receptors.
This complex system (often referred to as the IGF "axis") consists of two cell-surface receptors (IGF1R and IGF2R), two ligands (IGF-1 and IGF-2), a family of seven high-affinity IGF-binding proteins (IGFBP1 to IGFBP7), as well as associated IGFBP degrading enzymes, referred to collectively as proteases.
Approximately 98% of IGF-1 is always bound to one of six binding proteins (IGF-BP). IGFBP-3, the most abundant protein, accounts for 80% of all IGF binding.
[7] IGF-1 is a protein that in humans is encoded by the IGF1 gene. [8] [9] IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7,649 daltons. [10] In dogs, an ancient mutation in IGF1 is the primary cause of the toy phenotype. [11] IGF-1 is produced primarily by the liver.
The IGFBP3 gene (or IBP3), on human chromosome 7, is organized into four protein-coding exons with a 5th exon in the 3' untranslated region. [8] It is located adjacent to the IGFBP1 gene in tail-to-tail orientation, separated by 20 kb. [9] The encoded protein includes a 27-residue signal peptide followed by the 264-residue mature protein.
Human protein-coding gene pages: •Python code for maintaining the list •List of human protein-coding genes page 1 covers genes A1BG–EPGN •List of human protein-coding genes page 2 covers genes EPHA1–MTMR3
In vitro decidualization results in similar morphological changes to the human ESCs as well as upregulated production of decidualization markers such as IGFBP1 and prolactin. [7] Mouse models have been extensively used for the identification of the molecular factors required for and involved in decidualization. [12]