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  • 产品名称:Insulin-LikeGrowthFactor1(IGF1)(AA49-118)(Active)protein(FcTag)

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  • 产品厂商:ACROBiosystems
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简单介绍:
Insulin-LikeGrowthFactor1(IGF1)(AA49-118)(Active)protein(FcTag)
详情介绍:
Characteristics This protein carries a human IgG1 Fc tag at the N-terminus. The protein has a calculated MW of 35 kDa. The protein migrates as 35 kDa under reducing (R) condition (SDS-PAGE).
Purity >98 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: Measured in a serum-free cell proliferation assay using MCF-7 human breast cancer cells. The ED50 for this effect is typically 0.5-2.5 ng/mL.
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 *****s. 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.
Molecular Weight 35 kDa
UniProt P05019
Research Area Diabetes, Metabolism, Growth Factors
Pathways RTK Signaling, Intracellular Steroid Hormone Receptor Signaling Pathway, Peptide Hormone Metabolism, Hormone Activity, Regulation of Intracellular Steroid Hormone Receptor Signaling, Regulation of Hormone Metabolic Process, Regulation of Hormone Biosynthetic Process, Stem Cell Maintenance, Glycosaminoglycan Metabolic Process, Regulation of Carbohydrate Metabolic Process, Autophagy, Smooth Muscle Cell Migration, Activated T Cell Proliferation, Positive Regulation of fat Cell Differentiation
Restrictions For Research Use only
Format Lyophilized
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.
Buffer 50 mM Tris, 100 mM Glycine, pH 7.5
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Supplier Images
SDS-PAGE (SDS) image for Insulin-Like Growth Factor 1 (IGF1) (AA 49-118) (Active) protein (Fc Tag) (ABIN2181262) Human IGF-I, Fc Tag on SDS-PAGE under reducing (R) condition. The gel was stained ove...
Binding Studies (Bind) image for Insulin-Like Growth Factor 1 (IGF1) (AA 49-118) (Active) protein (Fc Tag) (ABIN2181262) Immobilized Human IGF-I, Fc Tag (Cat# IG1-H4269) at 5 μg/mL (100 µl/well),can bind Hu...
Background publications Qin, Strong, Baylink, Mohan: "Structure-function analysis of the human insulin-like growth factor binding protein-4." in: The Journal of biological chemistry, Vol. 273, Issue 36, pp. 23509-16, 1998 (PubMed).