Measured by its ability to inhibit the biological activity of IGFII on MCF7 human breast adenocarcinoma cells (Karey, K.P. et al. (1988) Cancer Research 48:4083.). The ED50 for this effect is typically 0.02-0.1 μg/mL in the presence of 14 ng/mL human IGFII.

IGFBP-2 Protein, Rhesus, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 32.8 kDa and the accession number is XP_001087071.1.

Rhesus

HEK293 Cells

insulin-like growth factor binding protein 2, 36kDa

A DNA sequence encoding the rhesus IGFBP2 (XP_001087071.1) (Met1-Gln324) was expressed, fused with a polyhistidine tag at the C-terminus. Predicted N terminal: Glu 38

> 67 % as determined by SDS-PAGE

A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.

It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.

IGFBP-2, also known as IGFBP2, is an insulin-like growth factor-binding protein (IGFBP). IGFBPs prolong the half-life of the IGFs, control bioavailability, activity, and distribution of insulin-like growth factor (IGF) through high-affinity IGFBP/IGF complexes. Six high-affinity IGF-binding proteins (IGFBP-1 to -6) have been identified. The six IGFBPs are structurally related but encoded by distinct genes. IGFBPs have a high affinity for IGFs. Some members of the IGFBP family have been consistently shown to inhibit IGF actions by preventing them from gaining access to the IGF receptors, while others potentiate IGF actions by facilitating the ligand-receptor interaction. IGFBP-2 is overexpressed in many malignancies and is often correlated with an increasingly malignant status of the tumor, pointing to the potential involvement of IGFBP-2 in tumorigenesis. It contains 1 IGFBP N-terminal domain and 1 thyroglobulin type-1 domain. It inhibits IGF-mediated growth and developmental rates.