Cambridge IGF-1 LR3

1,600 د.إ

GF-1 LR3 (insulin-like growth factor-1 long arginine 3) is a synthetic, modified construct of insulin-like growth factor-1. Because IGF-1 LR3 does not bind to IGF-1 binding proteins very well, it remains active up to 120 times longer than standard IGF-1. This results in improved half-life for the peptide and thus increased activity. IGF-1 LR3 enhances cell division and growth, boosts fat metabolism, and increases muscle repair and hypertrophy by inhibiting myostatin. Recent research suggests that IGF-1 LR3 may also be useful in improving lactation among mothers with young offspring.

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Description

Human IGF-1 LR3, insulin-like growth factor long arginine 3, protein is a synthetic form of IGF-1 with an N-terminal protein extension that improves potency and metabolic stability. IGF-1 LR3 is often used in the maintenance of human pluripotent stem cells1

Highly pure and bioactive 9 kDa IGR-1 LR3 protein monomer, animal-free (AF) and carrier-protein free (CF)

IGF-1 LR3 activity is determined using the Promega serum response element luciferase reporter assay (*) in transfected MCF-7 cells. EC50 = 12.0 ng/ml (1.3 nM).

Cells are treated in triplicate with a serial dilution of IGF-1 LR3 for 4 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. Data from Qk041 lot #104315.

IGF-1 LR3 migrates as a single band at 10 kDa in non-reducing (NR) conditions and upon reduction (R).  No contaminating protein bands are visible.

Purified recombinant protein (3 µg) was resolved using 18% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250.  Data from Qk041 batch #104315.

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