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Long R3 IGF-1, Buy Long R3 IGF-1

Shuttles nutrients directly into cells and muscles for maximum results:

- Anabolic Peptide;
- Builds muscle mass, promotes fat loss;
- Increased protein synthesis;
- IGF mobilizes fat for use as energy in adipose tissue;
- Causes hyperplasia, the increase of more muscle cells;
- At a genetic level it has the potential to alter an individuals capacity to build superior muscle density and size;
- Possesses the ability to rehabilitate damaged cartilage.

IGF-1 is a growth-promoting polypeptide that is essential for normal growth and development. Long R3 IGF-1 is an 83 amino acid analog of IGF-1 encapsulating the complete human IGF-1 sequence with the substition of an Arg(R) for the Glu(E) at position three, hence R3, and a 13 amino acid extension peptide at the N terminus. This analog of IGF-1 has been produced with the purpose of increasing the biological activity of the IGF peptide.

Long R3 IGF-1 is significantly more potent than IGF-1. The enhanced potency is due to the decreased binding of Long R3 IGF-1 to all known IGF binding proteins. These binding proteins normally inhibit the biological actions of IGF?s. (FM Tomas, SE Knowles, CS Chandler, GL Francis, PC Owens, and FJ Ballard 1995).

Long R3 IGF-1 is an excellent additive for cellular culture. It is adaptable to many cell varieties and has good effects for promoting growth, these two functions are generally incompatible, as other cytokines do not have these two functions. This growth factor binds to IGF-I receptors to stimulate cell growth in serum-free media, but, unlike insulin, it is made exclusively for use in cell culture. It promotes cell proliferation, increases cell survival, inhibits intracellular apoptotic pathways, extends culture longevity, eases transition to serum-free media and increases recombinant protein production. The major advantage for Long R3 IGF-1 is that it binds with high affinity to IGF-1 receptors and in many cell types potently stimulates proliferation and increases culture viability and specific recombinant protein production. Another advantage is that it binds with very low affinity to IGF-binding proteins, making it more biologically active than native IGF and allowing easier study of the IGF-1 receptor and its actions.

Long R3 IGF-1 has many functions, such as it can increase the protein synthesis, increase the RNA synthesis, promote fat metabolism, sugar transport, and so on, thus IGF-1 increases the efficacy of the nutrient intake.

IGF-1, as the name implies, is an extremely anabolic peptide that has insulin-like actions (i.e. It shuttles nutrients, specifically amino acids and glucose, into the muscle cells where they can then be synthesized into new muscle tissue). To test the hypothesis that IGF increases protein synthesis, the effects of IGF-1 have been studied with burn injuries, a significant catabolic inducing event. Burn injury is associated with substantial whole-body protein loss, reflecting mainly a catabolic response in skeletal muscle. The anabolic effects of IGF-1 after burn reflect inhibited protein breakdown and stimulated protein synthesis in skeletal muscle and that this response is caused by a direct effect of IGF-1 on muscle tissue. (CH Fang, BG Li, JJ Wang, JE Fischer, and PO Hasselgren 1997). (see also the below graphs for illustrations on IGF-1?s ability to inhibit protein breakdown).

Long R3 IGF-1 has a positive role in promoting muscle tissue, increased nitrogen retention, and increased food conversion i.e. the body utilizes nutrients more efficiently, Long R3 IGF-1is also significantly more biologically active than its IGF-1 counterpart as the following study suggests: Administration of IGF-I over a 14-day period to growing female rats via s.c. implanted osmotic pumps led to an increased body weight gain, an improved N retention and a greater food conversion efficiency. The effects were dose-dependent, with the highest daily dose tested, 278 micrograms/day, producing 18-26% increases in these measurements. LR3IGF-I, a variant of human IGF-I that contains an amino terminal extension peptide as well as glutamate-3 replaced by arginine and exhibits very weak binding to IGF-binding proteins, was substantially more potent than the natural growth factor, in the 44 micrograms/day of this peptide produced similar effects to the high IGF-I dose. (FM Tomas, SE Knowles, CS Chandler, GL Francis, PC Owens, and FJ Ballard 1995).

The amazing capabilities of Long R3 IGF-1 are enhanced with the addition of Growth Hormone (GH). (S R Kupfer, L E Underwood, R C Baxter, and D R Clemmons 1993).
During puberty IGF is responsible for the natural muscle growth that occurs during these 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.

When IGF is active it behaves differently in different types of tissues. In muscle cells, proteins and associated cell components are stimulated. Protein synthesis is increased along with amino acid absorption. As a source of energy, IGF 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.

IGF also mimic?s insulin in the human body. It makes muscles more sensitive to insulin?s effects, so if you are a person that currently uses insulin you can lower your dosage by a decent margin to achieve the same effects, and as mentioned IGF will keep the insulin from making you fat.

Perhaps the most interesting and potent effect IGF has on the human body is its ability to cause hyperplasia, which is an actual splitting of cells. Hypertrophy is what occurs during weight training and steroid use, it is simply an increase in the size of muscle cells. After puberty you have a set number of muscle cells, and all you are able to do is increase the size of these muscle cells, you don?t actually gain more. But, with IGF use you are able to induce hyperplasia which actually increases the number of muscle cells present in the tissue. IGF can actually change a research subjects genetic capabilities in terms of muscle tissue and cell count. IGF proliferates and differentiates the number of types of cells present. At a genetic level it has the potential to alter a research subjects capacity to build superior muscle density and size.

IGF-1 also has the therapeutic benefit of being able to rehabilitate damaged cartilage. Researchers investigated the effects of exogenous local Insulin like growth factor-I (IGF-I) on the repair of full-thickness articular cartilage defects in immature rabbits. These researchers concluded that repair of full-thickness immature cartilage defects can be enhanced by recombinant IGF-I. (Tuncel M, Halici M, Canoz O, Yildirim Turk C, Oner M, Ozturk F, Kabak S. 2005).

Long R3 IGF-1 has many functions, such as it can increase the protein synthesis, increase the RNA synthesis, promote fat metabolism, cause hyperplasia, repair damaged cartilage, increase nutrient uptake, and so forth. We are only in the beginning research stages of unlocking the potential of this extremely potent recombinant peptide!