IGF-II human

General description
Insulin-like growth factors (IGFs) are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the insulin gene family, which also contains insulin and relaxin.[1] The IGFs are similar by structure and function to insulin, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR),[2] but, IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and three intra-molecular disulfide bonds.
Application
IL-4 from mouse has been used to activate B-cells.[3] Biochem/physiol Actions
The insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro.[1] Physical form
Lyophilized with no additives.
Preparation Note
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.
Other Notes
AYRPSETLCG GELVDTLQFV CGDRGFYFSR PASRVSRRSR GIVEECCFRS CDLALLETYC ATPAKSE