Xenopsin
(Synonyms: 爪蟾肽) 目录号 : GC34043
A neurotensin-like octapeptide
Cas No.:51827-01-1
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
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- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Xenopsin is a neurotensin-like octapeptide that has been found in X. laevis skin.1 It inhibits neurotensin binding to rat brain synaptic membranes (Ki = 1.5 nM) and induces contraction of isolated guinea pig ileum in the presence of neostigmine .2 Xenopsin (0.1 μM) increases the firing rate of dopaminergic neurons in rat substantia nigra slices by 58.5%.3 Intravenous infusion of xenopsin (2 μg/kg per hour) increases adrenal, pancreatic, and ileal blood flow and plasma levels of pancreatic polypeptide, glucagon, substance P, and cortisol, as well as reduces tetragastrin-induced gastric acid secretion in dogs.1
1.Zinner, M.J., Kasher, F., Modlin, I.M., et al.Effect of xenopsin on blood flow, hormone release, and acid secretionAm. J. Physiol.243(3)G195-199(1982) 2.Granier, C., van Rietschoten, J., Kitabgi, P., et al.Synthesis and characterization of neurotensin analogues for structure/activity relationship studies. Acetyl-neurotensin-(8--13) is the shortest analogue with full binding and pharmacological activitiesEur. J. Biochem.124(1)117-124(1982) 3.Pozza, M.F., Küng, E., Bischoff, S., et al.The neurotensin analog xenopsin excites nigral dopamine neuronsEur. J. Pharmacol.145(3)341-343(1988)
| Cas No. | 51827-01-1 | SDF | |
| 别名 | 爪蟾肽 | ||
| Canonical SMILES | {Glp}-Gly-Lys-Arg-Pro-Trp-Ile-Leu | ||
| 分子式 | C47H73N13O10 | 分子量 | 980.16 |
| 溶解度 | Water: 10 mg/ml | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.0202 mL | 5.1012 mL | 10.2024 mL |
| 5 mM | 0.204 mL | 1.0202 mL | 2.0405 mL |
| 10 mM | 0.102 mL | 0.5101 mL | 1.0202 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
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| % DMSO % % Tween 80 % saline | ||||||||||
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工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
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The visual pigment Xenopsin is widespread in protostome eyes and impacts the view on eye evolution
Elife 2020 Sep 3;9:e55193.PMID:32880369DOI:10.7554/eLife.55193.
Photoreceptor cells in the eyes of Bilateria are often classified into microvillar cells with rhabdomeric opsin and ciliary cells with ciliary opsin, each type having specialized molecular components and physiology. First data on the recently discovered Xenopsin point towards a more complex situation in protostomes. In this study, we provide clear evidence that Xenopsin enters cilia in the eye of the larval bryozoan Tricellaria inopinata and triggers phototaxis. As reported from a mollusc, we find Xenopsin coexpressed with rhabdomeric-opsin in eye photoreceptor cells bearing both microvilli and cilia in larva of the annelid Malacoceros fuliginosus. This is the first organism known to have both Xenopsin and ciliary opsin, showing that these opsins are not necessarily mutually exclusive. Compiling existing data, we propose that Xenopsin may play an important role in many protostome eyes and provides new insights into the function, evolution, and possible plasticity of animal eye photoreceptor cells.
Extraocular, rod-like photoreceptors in a flatworm express Xenopsin photopigment
Elife 2019 Oct 22;8:e45465.PMID:31635694DOI:10.7554/eLife.45465.
Animals detect light using opsin photopigments. Xenopsin, a recently classified subtype of opsin, challenges our views on opsin and photoreceptor evolution. Originally thought to belong to the Gαi-coupled ciliary opsins, xenopsins are now understood to have diverged from ciliary opsins in pre-bilaterian times, but little is known about the cells that deploy these proteins, or if they form a photopigment and drive phototransduction. We characterized Xenopsin in a flatworm, Maritigrella crozieri, and found it expressed in ciliary cells of eyes in the larva, and in extraocular cells around the brain in the adult. These extraocular cells house hundreds of cilia in an intra-cellular vacuole (phaosome). Functional assays in human cells show Maritigrella Xenopsin drives phototransduction primarily by coupling to Gαi. These findings highlight similarities between Xenopsin and c-opsin and reveal a novel type of opsin-expressing cell that, like jawed vertebrate rods, encloses the ciliary membrane within their own plasma membrane.
Co-localization of Xenopsin and gastrin immunoreactivity in gastric antral G-cells
Histochemistry 1986;85(2):135-8.PMID:3528076DOI:10.1007/BF00491760.
Studies indicating evidence for the presence of the amphibian octapeptide Xenopsin in gastric mucosa of mammals prompted us to investigate the cellular localization of this peptide. Using the peroxidase-antiperoxidase method and a specific antiserum to Xenopsin (Xen-7) on paraffin and adjacent semithin sections of gastric antral mucosa from man, dog, and Tupaia belangeri, we found numerous epithelial cells showing a specific positive immunoreaction. These cells were of typical pyramidal shape and could be classified as of the "open" type. Cell quantification in serial sections processed for Xenopsin and gastrin immunoreactivity, respectively, revealed an identical number of cells per section and an identical distribution of these cells in the middle zone of the antral mucosa. Furthermore, adjacent semithin sections demonstrated the colocalization of Xenopsin and gastrin immunoreactivity within the same G-cell. The Xenopsin antiserum could be completely absorbed with synthetic Xenopsin but not with gastrin. Preabsorption tests with neurotensin, a Xenopsin related peptide, or with somatostatin, glucagon, and enkephalins gave no evidence for crossreactivity of the Xenopsin antiserum with these peptides. It is concluded that gastric antral G-cells in addition to gastrin also contain the amphibian peptide Xenopsin.
Xenopsin: the neurotensin-like octapeptide from Xenopus skin at the carboxyl terminus of its precursor
Proc Natl Acad Sci U S A 1984 Jan;81(2):380-4.PMID:6582494DOI:10.1073/pnas.81.2.380.
We have synthesized two oligodeoxyribonucleotide mixtures that contain sequences complementary to different parts of the hypothetical mRNA sequence of Xenopsin, a biologically active octapeptide found in skin extracts from Xenopus laevis. The two primer pools were independently used to initiate reverse transcription on skin poly(A)+ RNA and the resulting cDNAs were then used to screen in parallel a cDNA library prepared from skin poly(A)+ RNA. One of the clones that hybridized with both probes was subjected to sequence analysis. It contains a nearly full-length DNA copy of a mRNA of approximately equal to 490 nucleotides that encodes a Xenopsin precursor protein. The deduced precursor is 80 amino acids long, exhibits a putative signal sequence at the NH2 terminus, and contains the biologically active peptide at the COOH terminus. The region corresponding to the NH2-terminal portion of the Xenopsin precursor shows a striking nucleotide and amino acid sequence homology with the precursor of PYLa, another recently described peptide from Xenopus skin.
Caerulein-and xenopsin-related peptides with insulin-releasing activities from skin secretions of the clawed frogs, Xenopus borealis and Xenopus amieti (Pipidae)
Gen Comp Endocrinol 2011 Jun 1;172(2):314-20.PMID:21458457DOI:10.1016/j.ygcen.2011.03.022.
Caerulein-related peptides were identified in norepinephrine-stimulated skin secretions of the tetraploid frog Xenopus borealis and the octoploid frog Xenopus amieti using negative ion electrospray mass spectrometry and their primary structures determined by positive ion tandem (MS/MS) mass spectrometry. X. borealis caerulein-B1 (pGlu-Gln-Asp-Tyr(SO(3))-Gly-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains an additional Gly(5) residue compared with X. laevis caerulein and caerulein-B2 (pGlu-Asp-Tyr(SO(3))-Thr-Gly-Trp-Met-Asp-Phe.NH2) contains a Gln(2) deletion. X. amieti caerulein was identical to the X. laevis peptide. In addition, Xenopsin, identical to the peptide from X. laevis, together with xenopsin-AM2 (pGlu-Gly-Arg-Arg-Pro-Trp-Ile- Leu) that contains the substitution Lys(3)→Arg were isolated from X. amieti secretions. X. borealis caerulein-B1, and X. amieti Xenopsin and xenopsin-AM2 produced significant (P<0.05) and concentration-dependent stimulations of insulin release from the rat BRIN-BD11 clonal β cell line at concentrations ⩾30nM. The peptides did not stimulate the release of lactate dehydrogenase at concentrations up to 3μM demonstrating that the integrity of the plasma membrane had been preserved. While their precise biological role is unclear, the caerulein- and xenopsin-related peptides may constitute a component of the animal's chemical defenses against predators.