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Prepro VIP (111-122), human Sale

目录号 : GC36964

Prepro VIP (111-122), human 是一种前体血管活性肠肽 (VIP) 的衍生肽,对应其 111-122 残基氨基酸序列。血管活性肠肽存在于周围和中枢神经系统中,作为一种非镇静、非胆碱能神经递质或神经调节剂发挥作用。

Prepro VIP (111-122), human Chemical Structure

Cas No.:123025-94-5

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产品描述

Prepro VIP (111-122), human is a prepro-vasoactive intestinal polypeptide (VIP)-derived peptide, corresponding to residues 111-122. VIP is present in the peripheral and the central nervous systems where it functions as a nonadrenergic, noncholinergic neurotransmitter or neuromodulator[1][2].

[1]. Bredkjaer HE, et al. Location of PHM/VIP mRNA in human gastrointestinal tract detected by in situ hybridization. Cell Tissue Res. 1994 May;276(2):229-38. [2]. Henning RJ, et al. Vasoactive intestinal peptide: cardiovascular effects. Cardiovasc Res. 2001 Jan;49(1):27-37.

Chemical Properties

Cas No. 123025-94-5 SDF
分子式 C53H87N13O21 分子量 1242.33
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 0.8049 mL 4.0247 mL 8.0494 mL
5 mM 0.161 mL 0.8049 mL 1.6099 mL
10 mM 0.0805 mL 0.4025 mL 0.8049 mL
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Research Update

Characterization and regional distribution of peptides derived from the vasoactive intestinal peptide precursor in the normal human brain

J Neurochem 1989 Oct;53(4):1142-8.PMID:2769258DOI:10.1111/j.1471-4159.1989.tb07407.x.

To study the biosynthetic processing of the precursor for vasoactive intestinal peptide (prepro-VIP) in the human brain, we have developed antisera against the five functional domains of the precursor molecule: prepro-VIP 22-79, peptide histidine methionine (PHM), Prepro-VIP 111-122, VIP, and prepro-VIP 156-170. The antisera were used in radioimmunoassays in combination with HPLC to identify and quantify the peptides in regions of the human brain. All five peptides were expressed, but mainly in nonequimolar ratios. In only three regions were the same amounts of VIP and PHM found; in the remaining areas the concentration of PHM was two-thirds that of VIP. The concentrations of prepro-VIP 22-79, Prepro-VIP 111-122, and prepro-VIP 156-170 were considerably lower than the corresponding VIP concentrations, and the relative concentration of Prepro-VIP 111-122 differed between cortical and subcortical areas. A small proportion of the VIP precursor followed a pathway in which the dibasic conversion site after PHM is not cleaved, as evidenced by the presence of a C-terminally extended form of PHM. Finally, it was found that the C-terminal lysine residue of prepro-VIP is not removed during processing. The findings indicate that differences in the posttranslational processing of prepro-VIP exist in subpopulations of neurons in the human brain.

Location of PHM/VIP mRNA in human gastrointestinal tract detected by in situ hybridization

Cell Tissue Res 1994 May;276(2):229-38.PMID:8020060DOI:10.1007/BF00306108.

The expression of the gene for vasoactive intestinal polypeptide (VIP) and peptide histidine methionine (PHM) in the human gastrointestinal tract was studied by in situ hybridization and Northern blotting for PHM/VIP mRNA and immunocytochemistry using specific antisera against the bioactive peptides PHM and VIP. In the colon sigmoideum, antisera against all five putative processing products of the VIP precursor (prepro-VIP) were used, namely prepro-VIP 22-79, PHM, Prepro-VIP 111-122, VIP and prepro-VIP 156-170. Furthermore, RNA extracted from various regions of the gastrointestinal tract was examined by Northern blots and hybridization to a VIP-cDNA probe. Throughout the gastrointestinal tract, PHM/VIP mRNA was found in neurons only. Using single- or double-staining methods, we demonstrated both PHM/VIP mRNA and the corresponding peptides PHM and VIP in the neurons. In the sigmoideum, the single-staining methods were extended to investigate whether the neurons simultaneously contained PHM/VIP mRNA and each of the five prepro-VIP-derived peptides. Only one major band of PHM/VIP mRNA (1.9 kb) was found by Northern blotting in the tissue of the gastrointestinal tract.

Characterization of a novel prepro VIP derived peptide

Biochem Biophys Res Commun 1986 Sep 30;139(3):1142-9.PMID:3767995DOI:10.1016/s0006-291x(86)80296-0.

A newly identified, large molecular weight form of peptide histidine methionine (PHM), has been found not only where it was first revealed, in the stomach, but also in high concentrations in the nasal mucosa and urogenital system, though not in the central nervous system, intestine and lung. An antibody to the spacer peptide sequence Prepro-VIP 111-122, lying between PHM and VIP, also reacts directly with the large molecular form of PHM. It is suggested that the post-translational processing of prepro-VIP differs between tissues and in some, cleavage may not occur at the C-terminal end of PHM. The biological significance of this is currently unclear.