Pancreatic Polypeptide, bovine
目录号 : GC30456
PancreaticPolypeptide,bovine是由36个氨基酸组成的直链多肽，由胰腺中产生，能够抑制由分泌素和胆囊素诱导的胰腺分泌。PancreaticPolypeptide,bovine是神经肽(NPY)受体激动剂，对NPYR4有很高的亲和性。
Cas No.:179986-89-1
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- 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, bovine, a 36-amino acid, straight chain polypeptide derived primarily from the pancreas, inhibits secretin- and cholecystokinin-stimulated pancreatic secretion; Pancreatic Polypeptide, bovine acts as an agonist of NPY receptor, with high affinity at NPYR4.
Pancreatic Polypeptide, bovine 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, bovine inhibits secretin- and cholecystokinin-stimulated pancreatic secretion. 125I-Pancreatic Polypeptide, bovine shows no specific binding to pancreatic acini[2].
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]. Pancreatic Polypeptide, bovine (BPP; 40 μg/kg) inhibits CCK-33-induced pancreatic protein output during the entire bovine Pancreatic Polypeptide infusion period, but shows no effect on biliary protein output during CCK-33 or CCK-8 infusion[2].
[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. [2]. Louie DS, et al. Action of pancreatic polypeptide on rat pancreatic secretion: in vivo and in vitro. Am J Physiol. 1985 Oct;249(4 Pt 1):G489-95.
| Cas No. | 179986-89-1 | SDF | |
| Canonical SMILES | Ala-Pro-Leu-Glu-Pro-Glu-Tyr-Pro-Gly-Asp-Asn-Ala-Thr-Pro-Glu-Gln-Met-Ala-Gln-Tyr-Ala-Ala-Glu-Leu-Arg-Arg-Tyr-Ile-Asn-Met-Leu-Thr-Arg-Pro-Arg-Tyr-NH2 | ||
| 分子式 | C186H287N53O56S2 | 分子量 | 4225.78 |
| 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 | 0.2366 mL | 1.1832 mL | 2.3664 mL |
| 5 mM | 0.0473 mL | 0.2366 mL | 0.4733 mL |
| 10 mM | 0.0237 mL | 0.1183 mL | 0.2366 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 | ||||||||||
| 计算重置 | ||||||||||
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. A review
Pancreatic polypeptide (PP), 36-amino acid peptide, may function as an important feedback inhibitor of pancreatic secretion after a meal. It arises from both islet and acinar cells of the pancreas. Release of PP by a meal, primarily protein, occurs in a biphasic manner. The first rapid release occurs as a result of vagal stimulation; the second, more prolonged rise (the so-called intestinal phase) occurs in response to hormonal stimulation, predominantly cholecystokinin. Plasma PP levels increase with age; PP levels are elevated above those of age-controlled normal subjects in diabetic patients and in some patients with pancreatic amine precursor uptake decarboxylase tumors. The value of plasma PP as a possible marker for pancreatic tumors is as yet unsettled but may be a valuable tool.
Candidate hormones of the gut. VI. Bovine pancreatic polypeptide (BPP) and avian pancreatic polypeptide (APP)
Bovine pancreatic polypeptide as an antagonist of muscarinic cholinergic receptors
In dispersed acini from rat pancreas, it was found that bovine pancreatic polypeptide (BPP) and its C-fragment hexapeptide amide (PP-6), at concentrations of 0.1 and 30 microM, respectively, could significantly inhibit amylase secretion stimulated by carbachol (P less than 0.01 or 0.05, respectively), and this inhibition by BPP was dose dependent. 45Ca outflux induced by carbachol was also inhibited by BPP or PP-6, but they had no effect on cholecystokinin octapeptide- (CCK-8) or A23187-stimulated 45Ca outflux. BPP was also capable of displacing the specific binding of [3H]quinuclidinyl benzilate to its receptors, and it possessed a higher affinity (ki 35 nM) than carbachol (Ki 1.8 microM) in binding with M-receptors. It is concluded from this study that BPP acts as an antagonist of muscarinic cholinergic receptors in rat pancreatic acini. In addition, BPP inhibited the potentiation of amylase secretion caused by the combination of carbachol plus secretin or vasoactive intestinal peptide. This may be a possible explanation of the inhibitory effect of BPP on secretin-induced pancreatic enzyme secretion shown in vivo, since pancreatic enzyme secretion stimulated by secretin under experimental conditions may be the result of potentiation of enzyme release produced by the peptide in combination with a cholinergic stimulant.
Effect of bovine pancreatic polypeptide on basal pancreatic and biliary outputs in man
Basal pancreatic and biliary outputs were examined in seven healthy volunteers during intravenous infusion of bovine pancreatic polypeptide (BPP) at a mean dose of 320 pmol/kg/hr. BPP significantly (P less than 0.02) inhibited outputs of trypsin and bilirubin, without affecting bicarbonate. These studies suggest the possibility that pancreatic polypeptide may have a role in the regulation of biliary and pancreatic enzyme secretion in man.
Bovine pancreatic polypeptide (bPP) undergoes significant changes in conformation and dynamics upon binding to DPC micelles
The pancreatic polypeptide (PP), a 36-residue, C-terminally amidated polypeptide hormone is a member of the neuropeptide Y (NPY) family. Here, we have studied the structure and dynamics of bovine pancreatic polypeptide (bPP) when bound to DPC-micelles as a membrane-mimicking model as well as the dynamics of bPP in solution. The comparison of structure and dynamics of bPP in both states reveals remarkable differences. The overall correlation time of 5.08ns derived from the 15N relaxation data proves unambiguously that bPP in solution exists as a dimer. Therein, intermolecular as well as intramolecular hydrophobic interactions from residues of both the amphiphilic helix and of the back-folded N terminus contribute to the stability of the PP fold. The overall rigidity is well-reflected in positive values for the heteronuclear NOE for residues 4-34. The membrane-bound species displays a partitioning into a more flexible N-terminal region and a well-defined alpha-helical region comprising residues 17-31. The average RMSD value for residues 17-31 is 0.22(+/-0.09)A. The flexibility of the N terminus is compatible with negative values of the heteronuclear NOE observed for the N-terminal residues 4-12 and low values of the generalized order parameter S(2). The membrane-peptide interface was investigated by micelle-integrating spin-labels and H,2H exchange measurements. It is formed by those residues which make contacts between the C-terminal alpha-helix and the polyproline helix. In contrast to pNPY, also residues from the N terminus display spatial proximity to the membrane interface. Furthermore, the orientation of the C terminus, that presumably contains residues involved in receptor binding, is different in the two environments. We speculate that this pre-positioning of residues could be an important requirement for receptor activation. Moreover, we doubt that the PP fold is of functional relevance for binding at the Y(4) receptor.