Porcine dynorphin A(1-13)
(Synonyms: 强啡肽A(1-13),Dynorphin A Porcine Fragment 1-13) 目录号 : GC36947
Porcine dynorphin A (1-13) 是一个有效的内源性阿片受体 (κ opioid receptor) 激动剂，在生理浓度下它有镇痛作用。
Cas No.:72957-38-1
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.50%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Porcine dynorphin A (1-13) is a potent, endogenous κ opioid receptor agonist and is antinociceptive at physiological concentrations.
Dynorphin A (1-13) exposure (33 μM) causes a significant loss in neuronal viability at 4 h with a visible destruction in neuronal morphology seen at 16 h. Exposure to dynorphin A (1-13) causes acute increases in [Ca2+]i in individual neurons similar to increases seen with acute NMDA treatment. Continuous exposure to dynorphin A (1-13) (100 μM) causes a significant loss of neurons over time[1].
References:
[1]. Hauser KF, et al. Dynorphin A (1-13) neurotoxicity in vitro: opioid and non-opioid mechanisms in mouse spinal cord neurons. Exp Neurol. 1999 Dec;160(2):361-75.
| Cas No. | 72957-38-1 | SDF | |
| 别名 | 强啡肽A(1-13),Dynorphin A Porcine Fragment 1-13 | ||
| 分子式 | C75H126N24O15 | 分子量 | 1603.96 |
| 溶解度 | Water: ≥ 60 mg/mL (37.41 mM) | 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 | 0.6235 mL | 3.1173 mL | 6.2346 mL |
| 5 mM | 0.1247 mL | 0.6235 mL | 1.2469 mL |
| 10 mM | 0.0623 mL | 0.3117 mL | 0.6235 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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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。
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Dynorphin-(1-13), an extraordinarily potent opioid peptide
Proc Natl Acad Sci U S A 1979 Dec;76(12):6666-70.PMID:230519DOI:10.1073/pnas.76.12.6666.
We describe the opioid properties of a tridecapeptide, the sequence of which corresponds to the NH2-terminal sequence of dynorphin, a novel porcine pituitary endorphin. It contains [Leu]enkephalin. In the guinea pig ileum longitudinal muscle preparation it is about 700 times more potent than [Leu]enkephalin. Its effects in this tissue are blocked completely by naloxone, but the apparent affinity of naloxone is 1/13th that for blockade of [Leu]enkephalin or normorphine. In the mouse vas deferens, this peptide is 3 times more potent than [Leu]enkephalin. Well-washed rat brain membranes degrade the peptide rapidly, suggesting the presence of a membrane-bound degradative enzyme. The peptide displays considerable immunoreactivity in assays with antisera that have been used for the immunohistochemical localization of [Leu]enkephalin. The remarkable enhancement of the potency of [Leu]enkephalin by the COOH-terminal extension -Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-OH suggests new interpretations concerning the structure of opiate receptors and the function of the enkephalin pentapeptides.
A dynorphin-like opioid in the central nervous system of an amphibian
Proc Natl Acad Sci U S A 1982 May;79(10):3345-9.PMID:6124969DOI:10.1073/pnas.79.10.3345.
We have provided evidence for the existence of a biologically active opioid in toad (Bufo marinus) brain that is immunoreactive with antiserum raised against dynorphin (1-13). Compared with porcine dynorphin, this opioid is similar in apparent molecular weight on the basis of gel permeation chromatography and is more hydrophobic on the basis of high-performance liquid chromatography. After purification, its opioid biological activity was demonstrated on the guinea pig ileum myenteric plexus-longitudinal muscle preparation. It was found to be less potent, and to have a similar sensitivity to antagonism by naloxone, in comparison with porcine dynorphin. Because it is immunoreactive with antiserum specific for porcine dynorphin, it probably has considerable sequence homology. Generally, the tissue distribution of immunoreactive dynorphin in the toad is similar to that in the rat, with highest concentrations in the neurointermediate lobe of the pituitary. However, the anterior lobe of the toad pituitary contains considerably lower concentrations than are found in the rat anterior lobe. There appear to be three size classes of immunoreactive dynorphin in toad neural tissue, each with apparent molecular weight below 12,000, similar to the size classes of immunoreactive dynorphin found in pig and rat. However, in toad spinal cord (and possibly in brain) there is immunoreactive dynorphin of greater apparent molecular weight, which has not been reported in mammalian tissue. The contribution of each molecular size to the total immunoreactivity varies from tissue to tissue and is different from that observed in the rat.
Presence of dynorphin-like immunoreactivity in rat pituitary gland and hypothalamus
Regul Pept 1981 Jun;2(3):201-8.PMID:6114520DOI:10.1016/0167-0115(81)90014-8.
Using a highly specific and sensitive radioimmunoassay for dynorphin(1-13), dynorphin-like immunoreactivity (dynorphin-LI) was detected in rat pituitary and hypothalamus. Gel chromatographic studies on Sephadex G-50 revealed three components of dynorphin-LI with molecular weights of approximately 7500-9500 (big dynorphin), 3500-5500 (intermediate dynorphin) and 1600-1900 (small dynorphin), the latter of which eluted at the same position as authentic dynorphin contamination in porcine ACTH extracts (Sigma). Dynorphin-LI in rat anterior pituitary existed mainly as big dynorphin, whereas dynorphin-LI in rat intermediate-posterior pituitary and hypothalamus eluted mainly at the position of authentic small dynorphin.
Purification and characterization of a detergent-requiring membrane-bound metalloendopeptidase from porcine brain
Eur J Biochem 1999 Mar;260(2):318-24.PMID:10095765DOI:10.1046/j.1432-1327.1999.00151.x.
A detergent-requiring metalloendopeptidase cleaving a progastrin-C-terminal peptide (progastrin-(88-101)) mainly at the Arg95-Gly96 bond was solubilized from porcine cerebral vesicular membranes and purified to homogeneity as examined by PAGE. The purified enzyme had a molecular mass of approximately 76 kDa as estimated by both SDS/PAGE and Sephacryl S-300 gel filtration. It hydrolyzed progastrin-(88-101) peptide, BAM-12P, and bradykinin fairly specifically, and more efficiently than various other neuropeptides and related oligopeptides examined as substrates. It was inactive in the absence of detergents, and required certain detergents such as Triton X-100 or Lubrol PX for activity. Its optimum pH was about 6.5 and was strongly inhibited by metal-chelating agents such as EDTA, EGTA, and o-phenanthroline. It was extremely sensitive to EDTA and was completely inhibited even by 0.3 microM EDTA; the activity was fully restored by addition of a 10-fold higher concentration of Zn2+, CO2+, or Mn2+ ions over EDTA. On the other hand, dynorphin A-(1-13) peptide, a strong inhibitor of neurolysin, failed to inhibit the enzyme. The various characteristics indicated that the present enzyme is a unique membrane-bound metalloendopeptidase.
Synthesis of porcine leumorphin and some of its biological activities
Regul Pept 1983 May;6(2):163-8.PMID:6308716DOI:10.1016/0167-0115(83)90009-5.
The carboxy-terminal nonacosapeptide sequence of porcine preproenkephalin B contains the sequence of Leu-enkephalin at its amino terminus. The endogenous existence of this peptide, leumorphin, has not yet been proved. Synthesis of leumorphin was carried out by a solid-phase technique and the purity and structure of the synthetic peptide were confirmed. Synthetic porcine leumorphin exhibited a dose-dependent opiate effect (ED50 4.70 X 10(-9) M) on electrically stimulated contraction of the guinea pig ileum preparation. The potency was about 100 times as high as that of Leu-enkephalin. Leumorphin was less potent than dynorphin(1-13) (ED50 0.38 X 10(-9) M) but it was more active than beta h-endorphin (ED50 18 X 10(-9) M). The opiate activity was only partially reversed by naloxone. Intracisternal injection of synthetic leumorphin caused significant analgesia in mice (ED50 7.31 nmol/mouse). The potency was lower than that of beta h-endorphin (ED50 0.60 nmol/mouse) but higher than that of dynorphin(1-13) (ED50 16.10 nmol/mouse). Intracisternally injected leumorphin did not produce such a violent behavioral effect as did dynorphin(1-13), and it exhibited a mild sedative effect. The data supports the concept that leumorphin is a new type of opioid peptide and that the synthetic preparation will be useful for further biological and immunological studies on this peptide.