IGF-I R Protein, Cynomolgus (HEK293, His)

The IGF-I R protein is a receptor tyrosine kinase that mediates the effects of insulin-like growth factor 1 (IGF1) and has high affinity for IGF1. Upon ligand binding, IGF1R is activated, leading to autophosphorylation and tyrosine phosphorylation of substrates, including IRS1/2, Shc, and 14-3-3 proteins. IGF-I R Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived IGF-I R protein, expressed by HEK293 , with C-His labeled tag.

The IGF-I R protein, a receptor tyrosine kinase, serves as a mediator for the actions of insulin-like growth factor 1 (IGF1). It exhibits a high affinity for IGF1, lower affinity for IGF2, and insulin (INS). Activation of IGF1R plays a pivotal role in controlling cell growth and survival, with critical implications in tumor transformation and the survival of malignant cells. Upon ligand binding, the receptor kinase is activated, leading to autophosphorylation and the tyrosine phosphorylation of various substrates, including insulin-receptor substrates (IRS1/2), Shc, and 14-3-3 proteins. Phosphorylation of IRS proteins initiates two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. Activation of the MAPK pathway enhances cellular proliferation, while activation of the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Furthermore, IGF1R signals through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT), where phosphorylation of JAK proteins can activate STAT proteins, particularly STAT3, contributing to the transforming activity of IGF1R. Additionally, IGF1R activates JNK kinases and exerts inhibitory effects on JNK activation. When forming a hybrid receptor with INSR, IGF1R binds IGF1.

Cynomolgus

HEK293

C-6*His

G7P9I7 (E31-N908)

102130142  [NCBI]

Partial

EICGPGIDIRNDYQQLKRLENCTVIEGYLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTVDWSLILDAVSNNYIVGNKPPKECGDLCPGTMEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSACGKRACTENNECCHPECLGSCSAPDNDTACVACRHYYYAGVCVPACPPNTYRFEGWRCVDRDFCANILSAESSDSEGFVIHDGECMQECPSGFIRNGSQSMYCIPCEGPCPKVCEEEKKTKTIDSVTSAQMLQGCTIFKGNLLINIRRGNNIASELENFMGLIEVVTGYVKIRHSHALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWDHRNLTIKAGKMYFAFNPKLCVSEIYRMEEVTGTKGRQSKGDINTRNNGERASCESDVLHFTSTTTWKNRIIITWHRYRPPDYRDLISFTVYYKEAPFKNVTEYDGQDACGSNSWNMVDVDLPPNKDVEPGILLHGLKPWTQYAVYVKAVTLTMVENDHIRGAKSEILYIRTNASVPSIPLDVLSASNSSSQLIVKWNPPSLPNGNLSYYIVRWQRQPQDGYLYRHNYCSKPTIDEEVGPCCACPKTEAEKQAEKEEAEYRKVFENFLHNSIFVPRPERKRRDVMQVANTTMSSRSRNTTVADTYNITDLEELETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTGYEN

Approximately 48-58 kDa (beta subunit) & 100-115 kDa (alpha subunit) & 130-150 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.