What is IGF-1 LR3 (Insuline Growth Factor) ?
IGF-1 LR3 (Insuline Growth Factor) Product Genuine on Generic Gensci
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
.