Recombinant Human IGF-I R/IGF1R Protein

重组人IGF-I R/IGF1R蛋白 | 重组人胰岛素样生长因子1受体蛋白

CD221 antigen | CD221 | EC 2.7.10 | EC 2.7.10.1 | IGF1R | IGF-1R | IGF-I R | IGF-I receptor | IGFIR | IGF-IR | IGFR | insulin-like growth factor 1 receptor | Insulin-like growth factor I receptor | JTK13 | MGC142170 | MGC142172 | MGC18216 | soluble IGF1R

rp176705-10μg

10μg

无载体

≥90%(SDS-PAGE)

The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. Post-translational: Autophosphorylated on tyrosine residues in response to ligand binding (PubMed:11694888, PubMed:18501599, PubMed:19041240). Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit (PubMed:11694888, PubMed:18501599, PubMed:19041240). Autophosphorylation occurs in a sequential manner; Tyr-1165 is predominantly phosphorylated first, followed by phosphorylation of Tyr-1161 and Tyr-1166 (PubMed:11694888, PubMed:18501599, PubMed:19041240). While every single phosphorylation increases kinase activity, all three tyrosine residues in the kinase activation loop (Tyr-1165, Tyr-1161 and Tyr-1166) have to be phosphorylated for optimal activity (PubMed:11694888, PubMed:18501599, PubMed:19041240). Can be autophosphorylated at additional tyrosine residues (in vitro (PubMed:11694888, PubMed:18501599, PubMed:19041240). Autophosphorylated is followed by phosphorylation of juxtamembrane tyrosines and C-terminal serines (PubMed:11694888, PubMed:18501599, PubMed:19041240). May also be phosphorylated at Tyr-1161 and Tyr-1166 by mTORC2 (PubMed:26584640). Phosphorylation of Tyr-980 is required for IRS1- and SHC1-binding (PubMed:7541045). Phosphorylation of Ser-1278 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-1282 (By similarity). Dephosphorylated by PTPN1. Polyubiquitinated at Lys-1168 and Lys-1171 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome. Ubiquitination is facilitated by pre-existing phosphorylation. Sumoylated with SUMO1. Controlled by regulated intramembrane proteolysis (RIP). Undergoes metalloprotease-dependent constitutive ectodomain shedding to produce a membrane-anchored 52 kDa C-Terminal fragment which is further processed by presenilin gamma-secretase to yield an intracellular 50 kDa fragment.

重组表达

31.0 kDa

N-His

34.2 kDa, under reducing conditions

E. coli Accession #: P08069 | E. coli

人(Human)

1101-1367 aa

MHHHHHHNPVLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKEEMEPGFREVSFYYSEENKLPEPEELDLEPENMESVPLDPSASSSSLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNERALPLPQSSTC​

No

Yes