
Katalognummer: 223 - 11-443
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 0.1 mg
| Storage and shipping | Lyophilized Protein should be stored at -20°C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20°C or -70°C. Avoid repeated freeze-thaw cycles. |
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11-425
The Insulin-like Growth Factor 1 Receptor (IGF1) is also known as CD221, JTK13. and is a transmembrane receptor that is activated by IGF-1 and by the related growth factor IGF-2. It belongs to the large class of tyrosine kinase receptors. This receptor mediates the effects of IGF-1, which is a polypeptide protein hormone similar in molecular structure to insulin. IGF1R is make up of two alpha subunits and two beta subunits ,the Both the α and β subunits are synthesized from a single mRNA precursor. The precursor is then glycosylated, proteolytically cleaved, and crosslinked by cysteine bonds to form a functional transmembrane αβ chain.The α chains are located extracellularly while the β subunit spans the membrane and are responsible for intracellular signal transduction upon ligand stimulation. IGF1R have a binding site for ATP, which is used to provide the phosphates for autophosphorylation. There is a 60% homology between IGF1R and the insulin receptor. In response to ligand binding, the α chains induce the tyrosine autophosphorylation of the β chains. This event triggers a cascade of intracellular signaling that, while somewhat cell type specific, often promotes cell survival and cell proliferation.
11-444
The Insulin-like Growth Factor 1 Receptor (IGF1) is also known as CD221, JTK13. and is a transmembrane receptor that is activated by IGF-1 and by the related growth factor IGF-2. It belongs to the large class of tyrosine kinase receptors. This receptor mediates the effects of IGF-1, which is a polypeptide protein hormone similar in molecular structure to insulin. IGF1R is make up of two alpha subunits and two beta subunits ,the Both the α and β subunits are synthesized from a single mRNA precursor. The precursor is then glycosylated, proteolytically cleaved, and crosslinked by cysteine bonds to form a functional transmembrane αβ chain.The α chains are located extracellularly while the β subunit spans the membrane and are responsible for intracellular signal transduction upon ligand stimulation. IGF1R have a binding site for ATP, which is used to provide the phosphates for autophosphorylation. There is a 60% homology between IGF1R and the insulin receptor. In response to ligand binding, the α chains induce the tyrosine autophosphorylation of the β chains. This event triggers a cascade of intracellular signaling that, while somewhat cell type specific, often promotes cell survival and cell proliferation.
40-155-05mg
The IGFs are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar by structure and function to insulin, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but, IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds.
91-022
Insulin-like growth factor I (IGF1) belongs to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGFs are generated by proteolytic processing of inactive precursor protein containing N-terminal and C-terminal propeptide regions. Mature human IGF-I consisting of 70 amino acids with 94% identity with mouse IGF1 and exhibits cross-species activity. IGF1 binds IGF-1R, IGF-2R, and the insulin receptor and plays a key role in cell cycle progression, cell proliferation and tumor progression. IGF1 expression is regulated by growth hormone.
40-440-001mg
The IGFs are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar by structure and function to insulin, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but, IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant murine IGF-I is a 7.6 kDa globular protein containing amino acids including 3 intra-molecular disulfide bonds.

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