Human IGF-I R / CD221 Protein, His Tag

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).

 

Molecule : IGF-I R

 

Synonyms : IGF1R,IGFR,JTK13,CD221,MGC142170,MGC142172,MGC18216

 

Format : Powder

 

Category : Bio-Markers & CD Antigens

 

Accession : NP_000866.1

 

Storage : -20℃

 

Shipping condition : Powder,RT

 

Molecular Weight : 81.0 kDa, 23.8 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

 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.

 

Buffer : PBS, pH7.4

 

Description :

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.

 

References :

(1) Jones JI, Clemmons DR., 1995, Endocr. Rev. 16 (1): 3–34.
(2) LeRoith D, et al., 1995, Endocr. Rev. 16 (2): 143–63.