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!
