Recombinant Human LR3 IGF-I/IGF-1 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 8335-G1

R&D Systems, part of Bio-Techne
Discontinued Product
8335-G1 has been discontinued. An alternative/replacement product is available: 8335D-GMP. View all IGF-I/IGF-1 products.

Key Product Details

A synthetic analog of IGF-1 designed specifically to excel in cell culture applications

Features and Benefits
  • High Purity Is determined by SDS-PAGE (>95%) and reverse phase HPLC (>90%). This is the purest commercially available recombinant human LR3 IGF-1 (Figure 1). The high purity generates excellent performance of the protein.
  • Stability Extended half-life in culture provides cost saving and time saving benefits.
  • Low Endotoxin R&D Systems' endotoxin specification of <0.01 EU/ug of protein greatly diminishes potential non-specific effects in culture applications.
  • Lot-to-Lot Consistency Our robust manufacturing process includes stringent testing and analysis to ensure the same performance across all lots.
  • Multigram quantities are available to meet bioproduction demands.

Source

E. coli

Accession #

P05019

Conjugate

Unconjugated

Applications

Bioactivity

View all IGF-I/IGF-1 Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human IGF-I/IGF-1 protein
MFPAMPLSSLFVN Human LR3 IGF-I/IGF-1
(Gly49-Ala118 (Glu51Arg))
Accession # P05019
N-terminus C-terminus

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.01 EU per 1 μg of the protein by the LAL method.

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

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 inhibt its activity.

Scientific Data Images for Recombinant Human LR3 IGF-I/IGF-1 Protein, CF

Recombinant Human LR3 IGF-I/IGF-1 Protein Bioactivity

Recombinant Human LR3 IGF-I/IGF-1 Protein Bioactivity

Recombinant Human LR3 IGF-I/IGF-1 (Catalog # 8335-G1) 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.
Recombinant Human LR3 IGF-I/IGF-1 Protein SDS-PAGE

Recombinant Human LR3 IGF-I/IGF-1 Protein SDS-PAGE

1 μg/lane of Recombinant Human LR3 IGF-I/IGF-1 was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 7 kDa.
Recombinant Human LR3 IGF-I/IGF-1 Protein Mass Spectrometry

Recombinant Human LR3 IGF-I/IGF-1 Protein Mass Spectrometry

ESI analysis of Recombinant Human LR3 IGF-I/IGF-1 (Catalog # 8335-G1). The peak at 9112 Da corresponds to the calculated molecular mass, 9118 Da.

Formulation, Preparation and Storage

8335-G1
Formulation Lyophilized from a 0.2 μm filtered solution in phosphate buffer, pH 7.2 .
Reconstitution Reconstitute at 500 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.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: IGF-I/IGF-1

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/Insulin-like Growth Factor 1

Alternate Names

IGF-1, IGF1, IGFI, Somatomedin A, Somatomedin C

Entrez Gene IDs

3479 (Human); 16000 (Mouse); 24482 (Rat)

Gene Symbol

IGF1

UniProt

P05019

Additional IGF-I/IGF-1 Products

Product Documents for Recombinant Human LR3 IGF-I/IGF-1 Protein, CF

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