Description
Human IGF-I R / CD221 Protein, His Tag (MALS verified) | IGR-H5229-1mg| Gentaur Distribution US, UK & Europe
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.
Source: Human IGF-I R, His Tag (IGR-H5229) is expressed from human 293 cells (HEK293). It contains AA Glu 31 - Asn 932 (Accession # P08069-1).
Format: Powder.
Tag: C-10×His.
Expression System: HEK293.
Expression Region: Glu 31 - Asn 932.
Conjugate: Unconjugated.
Molecular Weight: 104.8 kDa.
Characteristics: This protein carries a polyhistidine tag at the C-terminus. This protein contains a furin convertase cleavage site, 737-RKRR-740, and will be partially processed into N (α chain) and C-terminal fragment (partial β chain) with calculated MW of 81.0 kDa and 23.8 kDa respectively. The protein migrates as 35-45 kDa (partial β chain), 110-120 kDa (α chain) and 130 kDa (α chain & partial β chain) under reducing (R) condition (SDS-PAGE) due to glycosylation.
Purity: 90%.
Buffer: PBS, pH7.4.
Storage Conditions: -20℃.
Shipping Conditions: RT