Pancreatic Polypeptide, rat (Rat pancreatic polypeptide)
(Synonyms: Rat pancreatic polypeptide) 目录号 : GC33785
Pancreatic Polypeptide, rat (Rat pancreatic polypeptide) 是一种 NPY 受体激动剂，对 NPYR4 具有高亲和力。
Cas No.:90419-12-8
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
Cell experiment: | To assess the effects of NPY and Pancreatic Polypeptide on rodent BRIN-BD11 and human 1.1B4 beta-cell proliferation, cells are seeded at a density of 150,000 cells per well and cultured overnight in the presence of NPY or Pancreatic Polypeptide (1 μM), and compared to positive control GLP-1 (1 μM). Cells are washed with PBS and fixed using 4% paraformaldehyde. After antigen retrieval with citrate buffer at 95°C for 20 min, tissue is blocked using 2% BSA for 45 min. The slides are then incubated with rabbit anti-Ki-67 primary antibody, and subsequently with Alexa Fluor® 594 secondary antibody. Slides are viewed using fluorescent microscope and photographed by DP70 camera adapter system. Proliferation frequency is determined in a blinded fashion and expressed as % of total cells analysed. Approximately 150 cells per replicate are analysed. For analysis of ability of NPY and Pancreatic Polypeptide to protect against streptozotocin-induced DNA damage, BRIN-BD11 and 1.1B4 cells are seeded. Cells are then exposed to streptozotocin (5 mM) in the presence or absence of NPY or Pancreatic Polypeptide (1 μM) for 2 h, with GLP-1 (1 μM) as positive control. Cells are then harvested and a comet assay is performed. Resulting gels are stained using DAPI (4′,6-diamidino-2-phenylindole) (100 μg/mL) and slides are viewed under appropriate filter. Comet score software is used for the analysis of % tail DNA (100 cells per gel) and olive tail moment[1]. |
Animal experiment: | Mice[1]Plasma glucose and insulin responses are evaluated after intraperitoneal (i.p.) injection of glucose alone (18 mmol/kg body weight) or in combination with test peptides (Pancreatic Polypeptide, etc.; 25 nmol/kg body weight) in overnight (18 h) fasted C57BL/6 mice. In a second series of experiments, 18 h fasted mice are used to assess the effects of respective test peptides on food intake. Mice receive an i.p. injection of saline alone (0.9% (w/v) NaCl) or in combination with test peptides (25 nmol/kg body weight) and food intake measured at 30 min intervals for 180 min. A dose of 25 nmol/kg is chosen with other NPYR modulators on glucose homeostasis, insulin secretion and feeding at this dose[1]. |
References: [1]. Khan D, et al. Influence of neuropeptide Y and pancreatic polypeptide on islet function and beta-cell survival. Biochim Biophys Acta. 2017 Apr;1861(4):749-758. | |
Pancreatic Polypeptide, rat is an agonist of NPY receptor, with high affinity at NPYR4.
Pancreatic Polypeptide, rat is an agonist of NPY receptor, with high affinity at NPYR4. Pancreatic Polypeptide (1 μM) does not alter proliferation in BRIN BD11 or 1.1B4 beta-cells, but reverses the decreased cell viability in BRIN BD11 cells induced by streptozotocin. Pancreatic Polypeptide (0.1 nM-1 μM) shows no effect on insulin secretion from isolated mouse islets, and does not affect the membrane potential and (Ca2+)i levels in BRIN BD11 cells at 1 μM[1].
Pancreatic Polypeptide (25 nmol/kg bw, i.p.) reduces glucose-stimulated insulin concentrations but shows no effect on acute feeding behaviour in overnight fasted mice[1].
[1]. Khan D, et al. Influence of neuropeptide Y and pancreatic polypeptide on islet function and beta-cell survival. Biochim Biophys Acta. 2017 Apr;1861(4):749-758.
| Cas No. | 90419-12-8 | SDF | |
| 别名 | Rat pancreatic polypeptide | ||
| Canonical SMILES | Ala-Pro-Leu-Glu-Pro-Met-Tyr-Pro-Gly-Asp-Tyr-Ala-Thr-His-Glu-Gln-Arg-Ala-Gln-Tyr-Glu-Thr-Gln-Leu-Arg-Arg-Tyr-Ile-Asn-Thr-Leu-Thr-Arg-Pro-Arg-Tyr-NH2 | ||
| 分子式 | C195H298N58O57S | 分子量 | 4398.87 |
| 溶解度 | Soluble in DMSO | 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 | 0.2273 mL | 1.1367 mL | 2.2733 mL |
| 5 mM | 0.0455 mL | 0.2273 mL | 0.4547 mL |
| 10 mM | 0.0227 mL | 0.1137 mL | 0.2273 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 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
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计算结果:
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。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Pancreatic polypeptide immunoreactivity in rat brain is actually neuropeptide Y
Neuroscience 1985 Aug;15(4):1149-57.PMID:3900804DOI:10.1016/0306-4522(85)90259-3.
Radioimmunoassay was combined with high pressure liquid chromatography and immunohistochemistry to establish the identity of pancreatic polypeptide-like immunoreactive material in the central nervous system of the rat. Antisera to avian pancreatic polypeptide, bovine pancreatic polypeptide, the invariant amidated carboxyterminal hexapeptide fragment of mammalian pancreatic polypeptides and the structurally related peptide, neuropeptide Y, were used immunocytochemically to localize neurons containing immunoreactive pancreatic polypeptide-like material in rat brain. Adjacent brain sections stained by the indirect immunofluorescent technique and single sections from double-staining experiments demonstrated that identical fibers and perikarya stained for pancreatic polypeptide-like immunoreactive material by antisera directed against each of the four peptides. Characterization of pancreatic polypeptide-like immunoreactive material in chromatographed rat brain extracts by radioimmunoassay using antisera to either neuropeptide Y or the carboxy-terminal portion of the pancreatic polypeptide molecule revealed that the major peak of immunoreactive material, as measured by either assay, appeared to co-elute with synthetic porcine neuropeptide Y. A minor peak of immunoreactive material co-eluting with peptide YY standard was indicated by the neuropeptide Y radioimmunoassay. This was contrasted by data obtained from chromatographic profiles of rat pancreas, which showed that the main immunoreactive peak, as measured by the neuropeptide Y assay, co-eluted with porcine peptide YY, with a minor peak co-eluting with porcine neuropeptide Y. The main peak of immunoreactive material in pancreas, as measured by the pancreatic polypeptide carboxy-terminal radioimmunoassay, eluted considerably earlier than standard peptide YY, neuropeptide Y and bovine pancreatic polypeptide, and is probably identical to Rat pancreatic polypeptide.(ABSTRACT TRUNCATED AT 250 WORDS)
Action of pancreatic polypeptide on rat pancreatic secretion: in vivo and in vitro
Am J Physiol 1985 Oct;249(4 Pt 1):G489-95.PMID:2413769DOI:10.1152/ajpgi.1985.249.4.G489.
The biological activity of bovine pancreatic polypeptide (BPP) on rat exocrine pancreatic secretion was compared in vivo and in vitro. In anesthetized rats prepared with a bile-pancreatic duct cannula, BPP inhibited cholecystokinin (CCK)-stimulated (10 IDU . kg-1 X h-1) protein secretion in a dose-related manner (P less than 0.001). CCK, from 5-20 IDU . kg-1 X h-1, did not alter the degree of inhibition by BPP at 40 micrograms . kg-1 X h-1, suggesting a nonsurmountable inhibition. Analogues of BPP, including Rat pancreatic polypeptide, neuropeptide Y, peptide YY, and the C-terminal hexapeptide of PP, also inhibited CCK-stimulated protein secretion. To determine whether BPP acts directly on acinar cells to suppress enzyme secretion, in vitro studies were performed. BPP and its analogues did not suppress octapeptide of CCK (CCK-8)-stimulated amylase release from either isolated rat pancreatic acini or preparations of pancreatic lobules. Specific binding of 125I-BPP to pancreatic acini was also not observed. From our data we conclude that BPP acts to inhibit pancreatic enzyme secretion in the rat in a noncompetitive manner. Absence of an effect by BPP or its analogues in vitro coupled with an absence of 125I-BPP binding to acini suggest that the inhibitory action of PP on exocrine pancreatic function is mediated by indirect mechanisms.
Intracisternal Rat pancreatic polypeptide stimulates gastric emptying in the rat
Am J Physiol 1995 Jul;269(1 Pt 2):R167-72.PMID:7631889DOI:10.1152/ajpregu.1995.269.1.R167.
Pancreatic polypeptide (PP) has been shown to alter gastrointestinal functions, including increased gastric acid secretion and motility following brain stem injections of PP. The present study investigated the effect of an intracisternal injection of PP on the rate of gastric emptying. Additionally, the efficacy of the rat and bovine forms of the peptide was compared. Rats anesthetized with ether received an intracisternal injection of rat PP, bovine PP, or vehicle and, upon regaining consciousness, were fed a liquid test "meal." Intracisternal rat PP produced a marked enhancement in gastric emptying compared with control animals. Bovine PP, at doses equimolar to or three times greater than the effective rat PP dose, produced no change in gastric emptying. Pretreatment with systemic atropine prior to central injection of rat PP eliminated the stimulation of emptying, suggesting that PP acts through a cholinergic mechanism. When equimolar doses of rat or bovine PP were microinjected directly into the dorsal vagal complex, the region containing PP receptors, both were capable of stimulating antral motility. The response to bovine PP, however, was delayed and reduced compared with that seen following rat PP. The results suggest that rat PP strongly stimulates gastric emptying in rats and that bovine PP, depending on the route of administration, is either ineffectual or a weaker agonist for central PP receptors.
Pancreatic polypeptide-like material in nerves and endocrine cells of the rat
Peptides 1983 Mar-Apr;4(2):245-53.PMID:6353389DOI:10.1016/0196-9781(83)90122-5.
A region-specific antiserum (AbS11) raised against the carboxyl-terminal hexapeptide of pancreatic polypeptide has been employed to measure Rat pancreatic polypeptide specifically and to demonstrate apparent immunoreactivity in nerves and in endocrine cells outside the pancreas. The concentration of pancreatic polypeptide in the head of the rat pancreas measured with AbS11 (176 +/- 47 pmol/g) was 750 fold higher than that measured with a conventional anti-bPP antiserum (0.23 +/- 0.08 pmol/g). Column chromatographs of rat pancreatic extracts demonstrated two peaks of immunoreactivity both eluting after the porcine pancreatic polypeptide standard. AbS11 also detected specific immunoreactivity in rat brain (470 fmol/g) which went undetected in convention assays. Although immunohistochemical studies with AbS11 and human pancreatic polypeptide antiserum demonstrated immunoreactivity in the same population of pancreatic endocrine cells, immunoreactive nerve fibres and enteroglucagon cells were only demonstrable with AbS11. These studies demonstrate that the carboxyl terminus of Rat pancreatic polypeptide is immunochemically similar to that of higher mammals. Furthermore, neural and extrapancreatic endocrine variants of this peptide share an immunochemical determinant contained within the carboxyl-terminal hexapeptide.
Effects of Rat pancreatic polypeptide on islet-cell secretion in the perfused rat pancreas
Metabolism 1992 Mar;41(3):306-9.PMID:1347399DOI:10.1016/0026-0495(92)90276-g.
Pancreatic polypeptide (PP) secretory cells are abundant in the islets of Langerhans. Results concerning the effects of exogenous PP on islet-cell secretion are controversial. This might be due in part to species specificity, given that most reports refer to studies performed using PP of bovine, porcine, or human origin in a heterologous animal model. Thus, we have investigated the influence of synthetic rat PP (80 nmol/L) on unstimulated insulin, glucagon, and somatostatin release, and on the responses of these hormones to glucose (11 mmol/L) and to arginine (3.5 mmol/L) in a homologous animal model, the perfused rat pancreas. Infusion of rat PP (rPP) reduced unstimulated insulin release by 35% (P = .03), and the insulin responses to glucose by 65% (P = .029) and to arginine by 50% (P = .026), without modifying glucagon output. rPP did not affect somatostatin secretion, either in unstimulated conditions or in the presence of 11 mmol/L glucose. However, it induced a clear-cut increase in somatostatin release during 3.5 mmol/L arginine infusion. Our observation that rPP inhibited insulin secretion without affecting glucagon and somatostatin output points to a direct effect of PP on B-cell function. However, during aminogenic priming of the D cell, the inhibition of insulin output induced by rPP was accompanied by an increase in somatostatin release. Thus, in this circumstance, it might be considered that the blocking effect of PP on B-cell secretion could be, at least in part, mediated by a D-cell paracrine effect.