Recombinant human IGF-1 LR3 for research use only
IGF-1LR3 is a modified version IGF-1 Protein
Insulin-like growth factor-1 is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9 kDa.
IGF1 mediates many of the growth-promoting effects of growth hormone.
The analog of IGF-1 known as IGF lr3 had been made to enhance and increase biological function and half-life.
IGF-1 lr3 allows for many of the growth-promoting effects of growth hormone-insulin-like growth factors, also known as IGF.
IGF1 LR3 is also known as Long R3 IGF-1 or Long Arg3.
Long Arg3 is a human recombinant non-glycosylated single polypeptide made up of 83 amino acids with a specific molecular mass of 9200 Daltons.
The unique process for manufacturing LR3 is designed to support the recombinant bio-pharmaceutical industries.
Studies show that growth hormone does not directly stimulate the incorporation of sulphate into cartilage, but instead acts upon a serum, termed 'sulfation factor,' which became known as 'somatomedin.'
IGF-1 is the first protein response of cells to the human growth hormone (HGH).
In essence, the IGF-1 production is in response to GH and then kickstarts cellular activities. One good example is hypertrophy, also known as muscle growth.
This protein increases insulin sensitivity making it the most influential growth factor found.
Increased IGF-1 causes the splitting muscle cell forming new cells in a process named hyperplasia.
The ultimate form of IGF-1 is LR3, its chemical alteration voids binding protein and increases the half-life for about 20-30 hours.
Sequence: MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIV DECCFRSCDLRRLEMYCAPLKPAKSA
Molar Mass: 9,111 Da
Synonyms: Long r3 IGF-1, LR3 IGF, IGF1 LR3, Long Arg3 IGF-1
The Sequence of IGF-1 LR3
The polypeptide Long R3 Insulin-like Growth Factor-I (IGF1 LR3) is an 83 amino acid analog of IGF-I.
Therefore the complete IGF-1 sequence save for the swap of a Glutamic acid (Glu) for the Arginine (Arg) at third position and the13 amino acid extension.
This change of sequence is to avoid binding to proteins giving IGF-1 LR3 a much longer half-life, around 20-30 hours.
This analog of IGF-1 has produced to increase the biological activity of the IGF peptide.” IGF stands for insulin-like growth factor.
Among the effects, the most positive are increased amino acid transport to cells, increased glucose transport, increased protein synthesis, and decreased protein degradation.
When IGF is active, the specific activity depends upon the tissue where it is present.
In muscle cells, protein synthesis accelerates along with amino acid absorption.
As a source of energy, IGF-1 LR3 mobilizes fat for use as energy in adipose tissue.
In lean tissue, IGF-1 LR3 prevents insulin receptor activity by transporting glucose across cell membranes.
As a result, the cells have to switch to burning off fat as a source of energy.
IGF-1 LR3 builds new muscle tissue by promoting nitrogen retention and protein synthesis resulting in hyperplasia and mitogenesis
Hyperplasia is an increase in the number of muscle cells.
Mitogenesis is the actual growth of new muscle fibres.
Thus IGF-1 LR3 not only makes muscle fibres more prominent, but it also creates more of them as well.
Therefore, IGF can change genetic capabilities in terms of muscle tissue and cell count.
IGF increases and differentiates the number and types of cells present.
IGF-1 LR3 is a synthetic analog of the naturally existing insulin growth factor (IGF) which is a 93 amino acid residue.
Modifications of the natural form occurred with the substitution of the Arg with Glu at position 3, giving a code R3, and also an extension of a 13 amino acid at the B-terminus.
Just like IGF-1, R3 has been shown to induce the development and growth of cells.
The studies on transgenic and knockout mice have shown that it can control its development and growth.
It plays a vital role as a regulator in the G1 to the S phase of the cell cycle. When applied to cardiomyocyte cultures, IGF-1 LR3 has shown a massive increase in proliferating cell nuclear antigen expression and several cyclins involved in cell progression as well as in bromodeoxyuridine (BrdU) labelling (Kajstura et al. 1994).
Other effects it has on cell lines are increased cell survival, inhibition of the apoptotic pathways, culture longevity and increased recombination of protein production (Fang et al. 1997).
In another study, the application of the LR3 IGF-1 has led to an increase in the myocyte bromodeoxyuridine uptake by three to fivefold.
IGF-1 LR3 actions are blocked by the ERK and P13K labelling which completely abolished the BrdU uptake.
Furthermore, it has been shown that in myocytes, IGF-1 R3 stimulates the cardiomyocyte division in vivo (Sundgren et al. 2003).
It has also been suggested that IGF-1-Long 3R is more potent than the IGF-1 because of its low binding capacity with all known IGF binding proteins (Tomas et al. 1995).
Orally administered IGF-1 Lr3 has shown no effects on the somatotropic axis (plasma levels of IGF-1 and 2, IGFBPs). The report concludes that plasma Long-R3 increased only when administered subcutaneously.
Furthermore, LR3 lowers the levels of natural IGF-1 in rhGH, but L-R3 increased the amounts of IGF-II concentrations when administered with L-R3 subcutaneously.
The parenteral administration of the Long R3 IGF-1 decreased the growth hormone concentration but did not affect the secretory system.
The somatotropic axis is functioning is influenced by nutrition, growth hormone and Long-R3-IGF-1 (IGF1-LR3).
The Half-Life of IGF-1 LR3 and its Effects of IGF-1
IGF-1 LR3 has a considerably longer half-life than other forms, nearly 20-30 hours.
When IGF-1 is active, it has multiple effects on tissues in muscle cells.
It plays an essential role in muscle renewal. IGF-1 LR3 encourages both increases as well as the distinction of stem cells.
IGF-1 LR3 increases satellite cell activity, muscle DNA, muscle protein content, muscle weight, and cross-sectional muscle area.
The importance of IGF-1 LR3 lies in the fact that all of its apparent effects work to induce muscle growth.
These effects are enhanced when combined with weight training.
Protein creation is better, along with amino acid absorption as a source of energy.
It enhances the use of fat as energy. In lean tissue, IGF-1 LR3 prevents insulin form carrying glucose across cell membranes. As a result, the cells have to change to burning off fat as a source of energy.
IGF-1 also mimics insulin in the human body.
Perhaps the most remarkable also strong influence it has on the human body is its ability to cause hyperplasia, which is a definite splitting of cells.
Hypertrophy is what ensues during weight training; it is an increase in the size of muscle cells.
Adult humans have a fixed number of muscle cells, that can become larger with training. However, the amount of muscle cells does not increase.
But, with this preparation use, you can induce hyperplasia, which increases the number of muscle cells present in the muscle.
Research studies show that with weight training, the new cells develop faster and become stronger and denser.
IGF-1 LR3 used in clinical research
IGF-1 LR3 plays an integral part in childhood growth and continues to have resulted in adults.
It is made in the human body and is at ideal levels during puberty.
In most studies, the maximum active length for research studies IGF-1 LR3 is 50 days on also 20-40 days off.
The most common range used during clinical research is typically between 20mcg to 120mcg per day.
During puberty, IGF is the most responsible for the natural muscle growth that occurs during these few years.
There are many different things that IGF does in the human body; among the effects, the most positive are increased amino acid transport to cells, increased glucose transport, increased protein synthesis, decreased protein degradation and increased RNA synthesis.
Perhaps the most potent effect IGF has on the human body is its ability to cause hyperplasia, which is an actual splitting of cells.
In muscle cells, proteins and their cell components become stimulated.
Protein synthesis increased along with amino acid absorption. As a source of energy, IGF-1 mobilizes fat for use as energy in adipose tissue.
In lean tissue, IGF prevents insulin from transporting glucose across cell membranes. As a result, the cells have to switch to burning off fat as a source of energy.
Researchers may use IGF-1 LR3 for various cellular projects involving
- enlarged amino acid transporting cells
- increased protein production
- reduced protein degradation
- amplified glucose transporting
- augmented RNA combination