protein

Fish (denis) IGF-I

MBS400008

0.01 mg

155 USD

Recombinant Protein

Fish (denis) IGF-I

IGF-I

Fish gilthead seabream (Sparus aurata) IGF-I

insulin-like growth factor I; Insulin-like growth factor I; insulin-like growth factor I; IGF-IA; IGF-IB; MGF; insulin-like growth factor IA; insulin-like growth factor IB; mechano growth factor; somatomedin-C; insulin-like growth factor 1 (somatomedin C); Mechano growth factor; MGF; Somatomedin-C

IGF1; IGF1; IGFI; IGF-I; IGF1A; IBP1; IGF-I; MGF

IGF1_HUMAN

E Coli

137

The sequence of the first ten N-terminal amino acids was determined and was found to be Met-Ser-Pro-Glu-Thr-Leu-Cys-Gly-Ala-Glu.

Greater than 98.0% as determined by:. (a) Analysis by reducing and non-reducing SDS-PAGE gel. (b) Gel-filtration chromatography under non denaturing conditions.

White lyophilized (freeze-dried) powder.

Lyophilized gsIGF-I although stable at room temperature for several weeks, should be stored desiccated below -18 degree C. Upon reconstitution at > 0.1 gsIGF-I mg/ml and up to 2 2 mg/ml and filter sterilization gsIGF-I can be stored at +4 degree C

Solubility: It is recommended to reconstitute the lyophilized gsIGF-I in sterile 0.4% NaHCO3 adjusted, not less than 100ug/ml, which can then be further diluted to other aqueous solutions. Protein Content: Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.60 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences. Dimers and Aggregates: The purified gsIGF-I consists of > 97% monomers as determined by gel-filtration chromatography.

Endotoxin: Less than 0.1 ng/ug (IEU/ug) of Gilthead Seabream IGF-I. Formulation: The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3. Biological Activity: Binding assays of the 125I-gsIGF-I to gilthead seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude gilthead seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF-I was about fourfold lower than that of gsIGF-I. Recombinant gsIGF-I exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF-1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF-I receptor in these cells. In contrast, the activities of gsIGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant gsIGF-I is biologically active.

Growth hormone and prolactin family; Hormones, Cytokines and Growth Factors

Gilthead seabream (Sparus aurata) insulin-like growth factor-I (gsIGF-I) cDNA coding the mature protein was expressed in Escherichia coli. The expressed protein contained within the inclusion-body pellet was solubilized and purified to over 98% purity, as a monomeric methionyl-gsIGF-I. Amino acid composition and N-terminal sequence confirmed the identity to be the predicted protein. For reference see Fine et al., J Endocrinol. 1997 53:139-150.

184834

AAA52789.1

P05019

17,762 Da

AMPK Signaling Pathway (989139); AMPK Signaling Pathway (992181); Adipogenesis Pathway (198832); Aldosterone-regulated Sodium Reabsorption Pathway (130626); Aldosterone-regulated Sodium Reabsorption Pathway (130590); Apoptosis Pathway (198797); Cardiac Progenitor Differentiation Pathway (712094); Dilated Cardiomyopathy Pathway (121494); Dilated Cardiomyopathy Pathway (121285); Endochondral Ossification Pathway (198812)

The protein encoded by this gene is similar to insulin in function and structure and is a member of a family of proteins involved in mediating growth and development. The encoded protein is processed from a precursor, bound by a specific receptor, and secreted. Defects in this gene are a cause of insulin-like growth factor I deficiency. Several transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Mar 2009]

IGF1: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. Defects in IGF1 are the cause of insulin-like growth factor I deficiency (IGF1 deficiency). IGF1 deficiency is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation. Belongs to the insulin family. 3 isoforms of the human protein are produced by alternative splicing. Protein type: Motility/polarity/chemotaxis; Secreted, signal peptide; Secreted. Chromosomal Location of Human Ortholog: 12q23.2. Cellular Component: insulin-like growth factor binding protein complex; extracellular space; plasma membrane; extracellular region. Molecular Function: integrin binding; insulin-like growth factor receptor binding; protein binding; growth factor activity; hormone activity; insulin receptor binding. Biological Process: muscle development; positive regulation of transcription, DNA-dependent; chondroitin sulfate proteoglycan biosynthetic process; glycolate metabolic process; exocrine pancreas development; water homeostasis; positive regulation of glucose import; positive regulation of fibroblast proliferation; proteoglycan biosynthetic process; inner ear development; positive regulation of DNA binding; muscle hypertrophy; platelet activation; positive regulation of mitosis; positive regulation of protein import into nucleus, translocation; regulation of establishment and/or maintenance of cell polarity; positive regulation of phosphoinositide 3-kinase cascade; cell activation; positive regulation of peptidyl-tyrosine phosphorylation; insulin-like growth factor receptor signaling pathway; branching morphogenesis of a tube; regulation of gene expression; response to heat; positive regulation of transcription from RNA polymerase II promoter; alveolus development; positive regulation of epithelial cell proliferation; negative regulation of apoptosis; positive regulation of insulin-like growth factor receptor signaling pathway; myoblast proliferation; positive regulation of smooth muscle cell proliferation; positive regulation of glycogen biosynthetic process; signal transduction; positive regulation of smooth muscle cell migration; positive regulation of activated T cell proliferation; negative regulation of cell proliferation; glial cell differentiation; platelet degranulation; mammary gland development; positive regulation of MAPKKK cascade; positive regulation of cell proliferation; DNA replication; skeletal development; positive regulation of granule cell precursor proliferation; phosphoinositide-mediated signaling; multicellular organism growth; myotube cell development; regulation of multicellular organism growth; satellite cell compartment self-renewal involved in skeletal muscle regeneration; myoblast differentiation; positive regulation of osteoblast differentiation; positive regulation of protein kinase B signaling cascade; cell proliferation; cellular protein metabolic process; positive regulation of tyrosine phosphorylation of Stat5 protein; Ras protein signal transduction; positive regulation of glycolysis; blood vessel remodeling; positive regulation of Ras protein signal transduction; blood coagulation; cell motility; positive regulation of DNA replication. Disease: Insulin-like Growth Factor I Deficiency

0.01 mg

155 USD

0.05 mg

240

0.1 mg

330

0.5 mg

920

1 mg

1575