Recombinant Mouse IGF2 protein (rFc Tag)

Species

Mouse

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg4527

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Validation Data Gallery

• 

  Purity of Recombinant Mouse IGF2 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

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Product Information

• Purity: >90 %, SDS-PAGE
• Endotoxin: <0.1 EU/μg protein, LAL method
• Activity:

  Not tested

• Expression: HEK293-derived Mouse IGF2 protein Ala25-Glu91 (Accession# P09535-1) with a rabbit IgG Fc tag at the N-terminus.
• GeneID: 16002
• Accession: P09535-1
• PredictedSize: 34.6 kDa
• SDS-PAGE: 33-38 kDa, reducing (R) conditions
• Formulation: Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
• Reconstitution: Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
• Storage Conditions:
  It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
• Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Insulin-like growth factor 2 (IGF2) is a crucial protein that plays a significant role in regulating growth, particularly during normal fetal development, and is also often dysregulated during tumorigenesis. IGF2 is one of the main ligands of the type 1 IGF receptor (IGF-1R), a tyrosine kinase receptor that transmits signals upon binding with IGF-II. IGF2 is predominantly secreted via the placenta during pregnancy and, after birth, primarily by hepatocytes, with its secretion being independent of growth hormone (GH) secretion, unlike IGF-I.

References:

1. Benyoucef, S. et al. (2007). Biochem. J. 403, 603-613.
2.Frasca, F. et al. (1999). Mol. Cell. Biol. 19, 3278-3288.
3.Pandini, G. et al. (2002). J. Biol. Chem. 277, 39684-39695.
4. Vella, V. et al. (2019). Cells. 8, 1017.
5.Sciacca, L. et al.(1999). Oncogene.18, 2471-2479.