Recombinant Human LR3 IGF-I GMP Protein, CF

Animal-Free.
  
  • Purity
    >95%, by SDS-PAGE with silver staining.
  • Endotoxin Level
    <0.01 EU per 1 μg of the protein by the LAL method.
  • Activity
    Measured in a serum-free cell proliferation assay using MCF‑7 human breast cancer cells. Karey, K.P. et al. (1988) Cancer Research 48:4083. The ED50 for this effect is 0.3-1.5 ng/mL. IGFBP-3 does not inhibit its activity.
  • Source
    E. coli-derived
    MFPAMPLSSLFVN Human  LR3 IGF-I
    (Gly49-Ala118 (Glu51Arg))
    Accession # P05019
    N-terminus C-terminus
    Produced using non-animal reagents in an animal-free laboratory. Manufactured and tested under cGMP guidelines.
  • Accession #
  • N-terminal Sequence
    Analysis

    Met-Phe-Pro-Ala-Met-Pro-Leu-Ser-Ser-Leu

  • Predicted Molecular Mass
    9 kDa
  • SDS-PAGE
    7 kDa, reducing conditions
8335-GMP
 
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100-200 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • A minimum of 12 months when stored at ≤ -20 °C as supplied. Refer to lot specific COA for the Use by Date.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Data Images

GMP-grade Recombinant Human LR3 IGF-I (Catalog # 8335-GMP) stimulates cell proliferation in a serum-free assay using the MCF-7 human breast cancer cell line. The ED50 for this effect is 0.3-1.5 ng/mL.

1 μg/lane of GMP-grade Recombinant Human LR3 IGF-I (Catalog # 8335-GMP) was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 9 kDa.

Mass Spectrometry

MALDI-TOF analysis of GMP-grade Recombinant Human LR3 IGF-I (Catalog # 8335-GMP). The major peak at 9114 corresponds to the calculated molecular mass, 9118 Da. The minor peak at 9321 is a matrix-associated artifact of the MALDI-TOF.

Background: IGF-I
Insulin-like Growth Factor I (IGF-I), also known as Somatomedin C, is the dominant effector of Growth Hormone (GH) and is structurally homologous to Proinsulin. Human IGF-I is synthesized as two precursor isoforms with N- and alternative C‑terminal propeptides (1). These isoforms are differentially expressed by various tissues (1). The 7.6 kDa mature IGF‑I is identical between isoforms and is generated by proteolytic removal of the N- and C-terminal regions. Mature human IGF-I shares 94% and 96% amino acid (aa) sequence identity with the mouse and rat orthologs, respectively (2). GH stimulates the production of IGF-I in most tissues (3). Hepatocytes produce circulating IGF-I, while local IGF-I is produced by many other tissues in which it has paracrine effects (1). IGF-I induces the proliferation, migration, and differentiation of a wide variety of cell types during development and postnatally (4, 5). IGF-I regulates glucose, fatty acid, and protein metabolism, steroid hormone activity, and cartilage and bone metabolism (6-11). It plays an important role in muscle regeneration and tumor progression (1, 12, 13). IGF-I binds IGF-I R, IGF-II R, and the Insulin Receptor, although its effects are mediated primarily by IGF-I R (14). IGF-I also binds with strong affinity to IGF binding proteins (IGFBPs), which regulate the availability and biological activities of IGF-I (15, 16).

Long R3 IGF-I (LR3 IGF-I) is a 9.2 kDa synthetic analog of IGF-I that is generated by modifying the aa sequence for mature human IGF-I. These modifications include the substitution of an Arg for Glu at position 3 of the mature IGF-1 sequence and the addition of a thirteen aa N-terminal extension, which is derived from methionyl porcine Growth Hormone (17). These aa changes generate a protein that is still capable of binding to IGF-I and Insulin receptors, but shows considerably lower affinity binding to IGFBPs compared to wild-type IGF-I (17, 18). As a result, LR3 IGF-I has an increased half-life and displays increased biological potency compared to IGF-I (17-22).

  • References:
    1. Philippou, A. et al. (2007) In Vivo 21:45.
    2. Sandberg-Nordqvist, A.C. et al. (1992) Brain Res. Mol. Brain Res. 12:275.
    3. Berryman, D.E. et al. (2013) Nat. Rev. Endocrinol. 9:346.
    4. Guvakova, M.A. (2007) Int. J. Biochem. Cell Biol. 39:890.
    5. Sadagurski, M. and M.F. White (2013) Endocrinol. Metab. Clin. North Am. 42:127.
    6. Clemmons, D.R. (2006) Curr. Opin. Pharmacol. 6:620.
    7. Bluher, S. et al. (2005) Best Pract. Res. Clin. Endocrinol. Metab. 19:577.
    8. Garcia-Segura, L.M. et al. (2006) Neuroendocrinology 84:275.
    9. Malemud, C.J. (2007) Clin. Chim. Acta 375:10.
    10. Ling, P.R. et al. (1995) Am. J. Clin. Nutr. 61:116.
    11. Sheng, M.H. et al. (2014) J. Bone Metab. 21:41.
    12. Samani, A.A. et al. (2007) Endocrine Rev. 28:20.
    13. Gallagher, E.J. et al. (2010) Endocr. Pract. 16:864.
    14. LeRoith, D. and S. Yakar (2007) Nat. Clin. Pract. Endocrinol. Metab. 3:302.
    15. Denley, A. et al. (2005) Cytokine Growth Factor Rev. 16:421.
    16. Duan, C. and Q. Xu (2005) Gen. Comp. Endocrinol. 142:44.
    17. Francis, G.L. et al. (1992) J. Mol. Endocrinol. 8:213.
    18. Voorhamme, D. and C.A. Yandell (2006) Mol. Biotechnol. 34:201.
    19. Tomas, F.M. et al. (1993) Biochem. J. 291:781.
    20. Tomas, F.M. et al. (1996) J. Endocrinol. 150:77.
    21. Tomas, F.M. et al. (1997) J. Endocrinol. 155:377.
    22. von der Thüsen, J.H. et al. (2011) Am. J. Pathol. 178:924.
  • Long Name:
    Insulin-like Growth Factor I
  • Entrez Gene IDs:
    3479 (Human); 16000 (Mouse); 24482 (Rat)
  • Alternate Names:
    IBP1; IGF1; IGF-1; IGF1A; IGFI; IGF-I; IGF-IA; IGF-IB; insulin-like growth factor 1 (somatomedin C); insulin-like growth factor 1; insulin-like growth factor I; insulin-like growth factor IA; insulin-like growth factor IB; Mechano growth factor; MGF; Somatomedin A; Somatomedin C; somatomedin-C

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