Mechano-Growth Factor (MGF) is an alternative name for the Insulin-like Growth Factor-1Eb (IGF-1Eb), an isoform of IGF-1. It has been studied for its potential in remodeling muscles, cellular survival, and cellular proliferation.^[1] New studies on this specific isoform highlight its potential for activating satellite cells in skeletal muscle, suggesting that this particular isoform may also activate satellite cells in skeletal muscle, protect neurons, and help overcome muscle mass loss.^[2] The principal function of MGF is its possible efficacy in reparating severe muscle wear and tear. Further, its concentration appears to correspond with skeletal muscle growth and differentiation found in rodent models.

Specifications

Other Known Titles: Frag 176-191

Molecular Formula: C₇₈H₁₂₅N₂₃O₂₃S₂

Molecular Weight: 1817.1 g/mol

Sequence: Tyr-Leu-Arg-Ile-Val-Gin-Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys-Gly-Phe

Follistatin-344 is a synthetic, full-sized version of a naturally occurring protein bearing the same name. Follistatin-344 occurs in two isomers, varying based on their gene splicing. Follistatin may exist endogenously in two distinct variants, referred to as FST 317 and FST 344. The variants are distinguished by their composition: FST 317 comprises 288 amino acids, whereas FST 344 comprises 315 amino acids. The numerical part of their names reflects the number of amino acids in the precursor molecules from which they are synthesized, with the precursor to FST 317 having 317 amino acids and that to FST 344 having 344 amino acids. It appears that FST 344 is the more commonly occurring form across various tissues. On the other hand, the FST 317 variant likely represents a minor fraction, potentially comprising under 5% of the total mRNA transcript related to Follistatin. Thus, Follistatin-344 appears to be the main constituent. Researchers suggest that its primary role may be to counteract the action of the Tumor Growth Factor-beta (TGF-beta) family. The TGF-beta family comprises Myostatin, Activin, and Follicle Stimulating Growth Hormone (FSH). Follistatin-344 appears to stimulate the Insulin/IGF-1 pathway, and the reported immense potential of the peptide has been published in Follistatin-344 research.

Specifications

Other Known Titles: Pralmorelin

Molecular Formula: C₄₅H₅₅N₉O₆

Molecular Weight: 817.9 g/mol

Sequence: H-D-Ala-D-2-Nal-Ala-Trp-D-Phe-Lys-NH2

Vilon (or Lyslglutamic Acid) is a peptide with apparent immunomodulatory and anti-aging bioregulation potential. It is a short peptide with just two amino acids in length. Scientific research suggests it may potentially act to regulate the vascular system and encourage hemostasis. Its functions may be more widespread, with studies indicating its possible influence in reducing the prevalence and growth of spontaneous tumors. Advocate researchers like Dr. Vladimir Anisimov believe that the peptide may become more widespread in contemporary research within the context of geroprotection.

PTD-DBM stands for Protein Transduction Domain-fused Disheveled Binding Motif. It is a synthetic peptide which has been studied within a wide range of research areas, including tissue damage and hair follicle development. Researchers have focused on the peptide specifically within the context of follicle development, suggested it may exert stimulating action through interaction with the endogenous proteins linked to follicle damage called CXXC5.^[1] It was discovered by Professor Kang-Yell Choi and his team of researchers at the Yonsei University in South Korea. The researchers studied the mechanism of hair follicle loss, and suggested that the cellular pathway Wnt/β-catenin may be crucial for follicle development.

The Wnt/β-catenin pathway is often studied in the context of tissue development and regeneration, Wnt proteins are a family of secreted signaling molecules that bind to cell surface receptors to trigger a cascade of intracellular events. β-catenin is a protein that normally resides in the cytoplasm of cells. Upon activation of the Wnt pathway, β-catenin is thought to accumulate in the cell and translocate to the nucleus, where it may activate the transcription of specific target genes involved in cell growth and differentiation. The activation of β-catenin may have a role in supporting and even increasing hair follicle development and possibly initiating the anagen phase, which represents the growth stage of hair follicles, as observed in murine models.

It has been hypothesized that PTD-DBM may interfere with the binding of CXXC5 and Dishevelled (Dvl) proteins by acting as a competitor. Specifically the peptide might inhibit the interaction between CXXC5 and Dishevelled (Dvl) proteins by binding to the PDZ domain of Dvl, thus interfering with CXXC5’s inhibitory actions on Wnt/β‐catenin signaling. Such a disruption might support the Wnt/β-catenin signaling pathway, thereby possibly promoting the onset of the anagen phase. Data from such murine studies suggests elevated expression levels of β-catenin, alkaline phosphatase (ALP), and proliferating cell nuclear antigen (PCNA), which are markers linked to cellular proliferation and hair follicle functionality.

Thymosin Alpha-1, also known as TA1 or Tα1, is a naturally occurring peptide fragment that was discovered in 1972 and researched for its potential action within the context of studies relating to cystic fibrosis, infection (e.g., tuberculosis, cytomegalovirus), respiratory disorders, chronic hepatitis, and cancer. It is also referred to as Thymalfasin when synthetically developed. Originally, research on Thymosin Alpha-1 centered around its potential role in immune modulation. It is hypothesized that it might increase levels of Major Histocompatibility Complex (MHC) class I molecules and boost cytokine production, key components of the immune system that may enhance immune responses.^[1][2] There is also a possibility that it might improve the activity of natural killer cells, which target virus-infected cells and tumors. Furthermore, it might enhance the expression of specific markers on T cells that are considered critical for their identification and function in the immune system, indicating a significant role in immune regulation. Thymosin Alpha-1 is also thought to possibly increase the presence of high-affinity interleukin-2 receptors on cell surfaces, potentially leading to the vigorous activation and proliferation of T lymphocytes, elements of immune response. There is speculation that it may affect both T-helper and cytotoxic T-cell populations, deemed essential for eliminating infected cells. Additionally, it might prompt the differentiation of thymocytes—precursor cells in the thymus—and peripheral blood lymphocytes into mature immune cells, increase natural killer cell numbers, and promote cytokine-driven inflammatory responses. Research also explores its potential role in enhancing macrophage efficiency—cells that engulf and digest pathogens—and in regulating the activity of alpha thrombin, a protein involved in blood clotting, highlighting its broad potential on immune function.

Modified GRF (1-29), or Mod GRF (1-29), is a synthetic peptide analog of growth hormone-releasing hormone (GHRH). It was first developed in the 1980s when studies indicated that the first 29 amino acids of GHRH may possess all of the biological roles associated with the full-length 44 residue protein.^[1] The initially designed peptide, known as GRF (1-29), is the shortest segment of GHRH, and appears to possess all the properties of the full-length hormone. A truncated synthetic form of GHRH known as Sermorelin, or GRF 1-29, also has 29 amino acids. Modified GRF (1-29) undergoes alteration to include four substituted amino groups in its chain.^[2] The intention behind these amino modifications is to protect the peptide from both oxidation and degradation during manufacture. The modification also appears to increase the binding affinity to GHRH receptors. Modified GRF (1-29) is also known as Mod GRF, or Tetra-substituted GRF (1-29). The latter name clarifies that the modified peptide differs from GRF (1-29) as a result of changes in four of its amino acids. Modified GRF (1-29) is structurally identical to CJC-1295 without DAC.