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IGF1 LR6 2mg Vial

$57.99 $47.99

One of the most attractive compounds we recently developed is a LongR 86 amino acid IGF-1 variant or LongR86 IGF-1. The additional 3 amino acids can extend the half life beyond that of LongR3 83a.a. The IGFs constitute a family of proteins having growth hormone stimulation properties. IGF-1 variants bring about a complexity from the splicing and modifications of the IGF-1 gene.


This gives rise to various IGF-1 isoforms, particularly in skeletal muscle that are used in various biological roles. In recent developments, different IGF-1 variants are endogenously secreted according to the particular overload or damage of skeletal muscle. This indicates IGF-1 variants have the possibility to bind to IGF receptors initiating cell proliferation and gene transcription. The sequences below are the Long86 variant of IGF-1 and LongR3 IGF-1, respectively.


The top variant is 86 amino acids long and is approximately 9.35kDa. The highlighted ATG is a translational starting site. The first ATG amino acid is degraded from the GCG signaling the decap enzyme for removal of the ATG. This particular IGF-1 variant (LongR86) has the same characteristics as the LongR3, however, the polypeptide is significantly more stable, thus increasing the half life to a more realistic 20 hours.

Function

Muscle building. May induce conception of twins. Also known as insulin growth factor, its a good protagonist at targeting tissues to spur cell to cell growth or in a more autocrine cell signaling process that facilitates cell division. Best if coupled with GH or any AS. Can be taken alone. One of the most attractive compounds we recently developed is a LongR 86 amino acid IGF-1 variant or LongR86 IGF-1. The additional 3 amino acids can extend the half life beyond that of LongR3 83a.a. The IGFs constitute a family of proteins having growth hormone stimulation properties. IGF-1 variants bring about a complexity from the splicing and modifications of the IGF-1 gene. This gives rise to various IGF-1 isoforms, particularly in skeletal muscle that are used in various biological roles. In recent developments, different IGF-1 variants are endogenously secreted according to the particular overload or damage of skeletal muscle. This indicates IGF-1 variants have the possibility to bind to IGF receptors initiating cell proliferation and gene transcription. The sequences below are the Long86 variant of IGF-1 and LongR3 IGF-1, respectively. The top variant is 86 amino acids long and is approximately 9.35kDa. The highlighted ATG is a translational starting site. The first ATG amino acid is degraded from the GCG signaling the decap enzyme for removal of the ATG. This particular IGF-1 variant (LongR86) has the same characteristics as the LongR3, however, the polypeptide is significantly more stable, thus increasing the half life to a more realistic 20 hours.