Receptor Grade IGF-1 LR3 (100mcg)

Receptor Grade IGF-1 LR3 Peptide

Receptor Grade IGF-1 LR3 peptide is a research reagent examined in studies on cellular growth, IGF receptors, and IGF binding proteins. It appears to be more powerful than rH IGF-1 and Media Grade IGF-1 LR3 due to an apparent significant improvement in its biological activity (since it exhibits a stronger affinity for the IGF receptor). This enhanced biological activity distinguishes between Receptor Grade IGF-1 LR3 and Media Grade (standard) IGF-1 LR3. Media grade IGF-1 LR3 is routinely studied in cell cultures. It is also used as a research reagent (at an economical cost) for studies where biological potency is not crucial. Receptor Grade IGF-1 LR3 should be the reagent of choice to achieve optimum results when performing any animal study and cell-based assays. Growth of mammalian cells in the presence of low concentrations of Long R3 IGF-1 appears to result in better productivity than standard concentrations of insulin and/or standard IGF-1.^[1] Researchers report that the peptide “demonstrated equivalent or better performance using two recombinant CHO cell lines.” IGF-1 LR3 may be more capable of inducing the type 1 IGF receptor, potentially promoting an elevated level of intracellular signaling, cellular proliferation, and apoptosis inhibition.

Specifications

Molecular Formula:C₉₉₀H₁₅₂₈N₂₆₂O₃₀₀S₇

Molecular Weight: 9,111 da

Sequence: MFPAMP LSSLF VNGPR TLCGA ELVDA LQFVC GDRGF YFNKP TGYGS SSRRA PQTGIV DECCFR SCDLRR LEMY CAPLK PAKSA

Receptor Grade IGF-1 LR3 Research

IGFB Binding and Biological Activity of IGF-1 LR3
The peptide appears to bring about a more pronounced impact than IGF-1 through a potential resistance in the association of IGFB.^[2] The prolonged duration of action may help mediate the same biological impact while examining smaller concentrations of the receptor. Certain IGF-1 derivatives, including the GPE derivative, comprising only the last three N-terminal amino acids of the IGF-1 protein, have been suggested to exert positive action in animal research models of neurological damage such as stroke. However, the majority of the research aimed to unravel the action of IGF-1 derivatives has been executed in cell cultures.

Insulin-Like Growth Factor Receptor Interactions
Naturally produced IGF-1 hormones interact with at least two cell surface receptors: the IGF-1 receptor (IGF-1R) and the insulin receptor.^[3] The researchers also note that “IR and IGF1R act as identical portals to the regulation of gene expression, with differences between insulin and IGF-1 effects due to a modulation of the amplitude of the signal created by the specific ligand-receptor interaction.” The IGF-1R is referred to as the “physiologic” receptor due to its potential higher affinity (approximately 100 times higher) for IGF-1 as compared to the insulin receptor. The association of IGF-1 and IGF-1R apparently leads to changes in metabolism, prevention of cell death (apoptosis), promotion of cell growth (hypertrophy), differentiation and cell division (hyperplasia), normal development, and even malignant growth. IGF-1R has been researched for its involvement in diverse types of cancer, such as prostate, breast, and lung cancer.^[4] IGF-1 also appears to stimulate insulin receptors and activate them, thereby promoting glucose uptake from the bloodstream by cells. IGF-1 displays a three-fold influence on muscle cells. At the onset, IGF-1 may promote an increase in the number of muscle cells, also known as hyperplasia. Secondly, IGF-1 appears to influence the life span of satellite cells of the skeletal muscles.^[5] Satellite cells provide nutritional support to muscle cells, thereby helping them to operate efficiently. IGF-1 may help to build muscle tissue by improving the lifespan of these cells. Finally, IGF-1 appears to promote the differentiation of myoblasts.^[6] In other words, it may encourage the commitment of stem cell progeny from non-specific pluripotent stem cells to dedicated muscle tissue. To conclude, IGF-1 may improve muscle development by enhancing the rate at which generic stem cells are transformed into muscle cells.

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References