IGF-1 1mg

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Buy IGF-1,  Insulin-Like Growth Factor 1

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IGF-1 1mg

Insulin-like growth factor 1 (IGF-1), also called somatomedin C, is a protein that in humans is encoded by the IGF1 gene. 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. IGF-1 is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin is used for the treatment of growth failure. Therapeutic administration with neurotrophic proteins (IGF I) is associated with potential reversal of degeneration of spinal cord motor neuron axons in certain peripheral neuropathies. IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges.


 

The Mitogenic Polypeptide Growth Factor That is IGF-1

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. The liver predominantly produces iGFs, 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. 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), but, IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions, generates mature IGFs. Recombinant human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds.


 

Insulin-Like Growth Factor-1

IGF-1


Sequence:
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECC
FRSCDLRRLEMYCAPLKPAKSA
Molar Mass: 7,649 daltons
Synonyms: Somatomedin C, IGF-1, IGF1, Insulin-Like Growth Factor-1

IGF-1 (Insulin-Like Growth Factor-1)

 


 

IGF-1 Muscle Growth and Fat Loss

Insulin-like growth factor I, also known as mechano growth factor, somatomedin-C, IGF-I and IGF1, is a secreted protein which belongs to the insulin family. The insulin family, comprised of insulin, relaxin, insulin-like growth factors I and II ( IGF-I and IGF-II ) and possibly the beta-subunit of 7S nerve growth factor, represents a group of structurally related polypeptides whose biological functions have diverged. The IGFs, or somatomedins, constitute a class of polypeptides that have a key role in pre-adolescent mammalian growth. IGF-I expression is regulated by growth hormone and mediates postnatal growth, while IGF-II appears to be induced by placental lactogen during prenatal development. IGF-1 is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin is used for the treatment of growth failure.

Therapeutic administration with neurotrophic proteins (IGF I) is associated with potential reversal of degeneration of spinal cord motor neuron axons in certain peripheral neuropathies. IGF1 / IGF-I may be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. IGF1 / IGF-I 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. Defects in IGF1 / IGF-I are the cause of insulin-like growth factor I deficiency (IGF1 deficiency) which is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation.

References
Dull T.J. et al., 1984, Nature. 310:777-81.
Bell G.I. et al., 1984, Nature. 310:775-7.
Cooke R.M. et al., 1991, Biochemistry 30:5484-91.
Sandberg-Nordqvist A.-C . et al., 1992, Brain Res. Mol. Brain Res. 12: 275 - 7.