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Your Position: Start > Protein > IGF-I > IG1-H82Q6

Biotinylated Human IGF-I Protein, His,Avitag™ (SPR verified)

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  • Synonym
    IGF-I,IGF1A,somatomedin C,MGF
  • Source
    Biotinylated Human IGF-I, His,Avitag(IG1-H82Q6) is expressed from human 293 cells (HEK293). It contains AA Gly 49 - Ala 118 (Accession # P05019-1).
    Predicted N-terminus: His
  • Molecular Characterization
    IGF-I Structure

    This protein carries a polyhistidine tag at the N-terminus, followed by an Avi tag (Avitag™).

    The protein has a calculated MW of 11.2 kDa. The protein migrates as 14 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Labeling
    Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.
  • Protein Ratio
    Passed as determined by the HABA assay / binding ELISA.
  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >90% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
IGF-I SDS-PAGE

Biotinylated Human IGF-I, His,Avitag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90%.

Bioactivity-SPR
 IGF-I SPR

Human IGF-I R, His Tag (Cat. No. IGR-H5229) immobilized on CM5 Chip can bind Biotinylated Human IGF-I, His,Avitag (Cat. No. IG1-H82Q6) with an affinity constant of 68 nM as determined in a SPR assay (Biacore 8K) (QC tested).

Bioactivity-Bioactivity CELL BASE
 IGF-I CELL

Biotinylated Human IGF-I Protein, His,Avitag™ (SPR verified) (Cat.No. IG1-H82Q6) stimulates the proliferation of Human IGF-1 R (Luc) HEK293 Reporter Cell. The EC50 for this effect is 0.1746 µg/mL. (Routinely tested)

  • Background
    Insulin-like growth factor 1 (IGF-1) is also known as somatomedin C, IGF1A, IGFI, sulfation factor, and is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin is used for the treatment of growth failure. IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7649 daltons. IGF-1 is produced primarily by the liver as an endocrine hormone as well as in target tissues in a paracrine/autocrine fashion. IGF-1 binds to at least two cell surface receptors: the Insulin-like growth factor 1 receptor, abbreviated as "IGF1R", and the insulin receptor. The IGF-1 receptor seems to be the "physiologic" receptor - it binds IGF-1 at significantly higher affinity than the IGF-1 that is bound to the insulin receptor. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase - meaning it signals by causing the addition of a phosphate molecule on particular tyrosines. Its primary action is mediated by binding to its specific receptor IGF1R, present on many cell types in many tissues. Binding to the IGF1R, a receptor tyrosine kinase, initiates intracellular signaling; IGF-1 is one of the most potent natural activators of the AKT signaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death. Insulin-like growth factor 1 has been shown to bind and interact with all the IGF-1 Binding Proteins (IGFBPs), of which there are six (IGFBP1-6). Specific references are provided for interactions with IGFBP3, IGFBP4 and IGFBP7.
  • Clinical and Translational Updates

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  • Number of Drugs in Clinical Trials:3 Details
  • Latest Research Phase:Phase 2 Clinical

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