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IGF-I 30-41 Sale

(Synonyms: Insulin-like Growth Factor I (30-41)) 目录号 : GC36300

IGF-I (30-41) 是类胰岛素生长因子I 30 至 41 的氨基酸片段。IGF-I 对生长激素的活性有着重要的作用,但是IGF-I本身也具有一些自身的特性,如合成代谢、抗氧化、抗炎和细胞保护作用。

IGF-I 30-41 Chemical Structure

Cas No.:82177-09-1

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产品描述

IGF-I (30-41) is amino acids 30 to 41 fragment of Insulin-like Growth Factor I (IGF-I). IGF-I is partly responsible for systemic GH activities although it possesses a wide number of own properties (anabolic, antioxidant, anti-inflammatory and cytoprotective actions)[1].

[1]. Puche JE, et al. Human conditions of insulin-like growth factor-I (IGF-I) deficiency. J Transl Med. 2012 Nov 14;10:224.

Chemical Properties

Cas No. 82177-09-1 SDF
别名 Insulin-like Growth Factor I (30-41)
分子式 C51H83N19O19 分子量 1266.34
溶解度 Soluble in DMSO 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 0.7897 mL 3.9484 mL 7.8968 mL
5 mM 0.1579 mL 0.7897 mL 1.5794 mL
10 mM 0.079 mL 0.3948 mL 0.7897 mL
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Research Update

Isolation and partial characterization of six somatomedin-like peptides from human plasma Cohn fraction IV

Acta Endocrinol (Copenh) 1986 Feb;111(2):271-84.PMID:3953237DOI:10.1530/acta.0.1110271.

Six somatomedin-like peptides were purified from human plasma Cohn fraction IV by a six-step procedure which included ethanol precipitation, reversed-phase extraction, gel filtration, chromatofocusing and reversed-phase high pressure liquid chromatography (HPLC). Purification was monitored with a competitive protein binding assay using a crude preparations of somatomedin carrier protein. The peptides isolated were homogeneous by reversed-phase HPLC and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Their apparent isoelectric points determined by chromatofocusing were 9.2 (Sm I), (Sm II), 8.2 (Sm III), 6.7 (Sm IV), 6.3 (Sm V), and 6.15 (Sm VI). SDS-PAGE under reducing conditions revealed that they are composed of a single peptide chain with apparent molecular weights of 6800 for Sm I, II and IV and 6400 for Sm III, V, and VI. They were equally potent in the porcine costal cartilage in vitro bioassay. The basic peptides (Sm I-III) were significantly more active in radioimmunoassays for somatomedin C (SmC) and insulin-like growth factor I C-peptide (IGF-I (30 - 41], while only the slightly acidic peptides were active in a radioimmunoassay for insulin-like growth factor II C-peptide (IGF-II (33-40]. When receptor binding was tested with human placental cell membranes and Sm III as tracer, the basic peptides were significantly more potent than Sm IV-VI. With rat liver cell membranes and Sm V as tracer the slightly acidic peptides were more potent. These findings suggest 1) that human plasma may contain other somatomedin-like peptides besides the major components IGF-I/SmC and IGF-II, and 2) that the basic peptides are structurally related to IGF-I/SmC and the slightly acidic peptides are related to IGF-II.