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Human IGF-I LR3 recombinant Protein
Human Insulin-like Growth Factor-I Long R3, recombinant
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Proteins Synonyms: Long R3 IGF-I, Somatamedin C, IGF-IA. Source: E. coli Biological Activity: ≥ 1.0 x 105 units/mg (rat L6); ≥ 5.0 x 105 units/mg (mouse FDC-P1) Purity: ≥ 98 % (SDS-PAGE, HPLC) Physical state: Lyophilized Manufacturer: |
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Active Bioscience
Product Details
Synonyms
Long R3 IGF-I, Somatamedin C, IGF-IA.
Description of Human IGF-I LR3
Recombinant Human IGF-I LR3 is a 9.1 kDa, single, nonglycosylated polypeptide chain containing 83 amino acid residues. The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissues in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. IGF-I LR3 is a recombinant analog of human IGF-I comprised of the complete IGF-I sequence, with an Arginine substitution for the third position Glutamic acid, and a 13 amino acid length N terminus peptide extension. Specifically engineered for higher biological potencysin vitro, IGF-I LR3 has an increased half-life and a binding aversion to native proteins within the body that make it ideal for both research and large-scale culturing.
Application
Recombinant Human IGF-I LR3 may increase cell growth and productivity in cell culture using CHO, ES, NK, HSC, MSC, fibroblast, hybridomas and many other cell types with a Type I IGF receptor. Typical working concentrations are between 10µg/L and 100 µg/L. 50µg/L is a good starting concentration. Some cells might need sequential adaptation (25/75; 50/50; 75/25; 0/100). Adaptation usually works best if started when cells are in mid-logarithmic growth phase and at ≥ 90% viability.
Biological Activity
The ED50 of ≤ 10.0 ng/ml was determined by its ability to stimulate the proliferation of rat-L6 myoblast cell line. It corresponds to a specific activity of ≥ 1.0 x 105 units/mg. In mouse FDC-P1 cells it shows a ED50 of ≤ 2.0 ng/ml corresponding to a specific activity of ≥ 5.0 x 105 units/mg.
Reconstitution
We recommend a quick spin followed by reconstitution in 100mM acetic acid or water to a concentration of 1.0 mg/ml. Do not vortex. Mix thoroughly to ensure complete dissolving of IGF-I LR3. We recommend keeping working aliquots at the highest practical concentration and if possible to use for example LoBind Eppendorf tubes for the preparation of working aliquots to prevent protein absorption.
Stability
The lyophilized protein is stable at room temperature for up to 1 month, and unopened at 2°C -8°C until expiry date. Reconstituted protein is stable for at least 12 months when stored in working aliquots at 2°C-8°C or at -18°C to -24°C. Do not store below -24°C. Please avoid repeated freeze-thaw cycles.
Amino Acid Sequence
MFPAMPLSSL FVNGPRTLCG AELVDALQFV CGDRGFYFNK PTGYGSSSRR APQTGIVDEC CFRSCDLRRL EMYCAPLKPA KSA
Shipped at room temperature
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
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