Urechistachykinin I
(Synonyms: Uru-TK I) 目录号 : GC37862
Urechistachykinin I (Uru-TK I) 是一种从棘虫体内分离出的无脊椎动物速激肽相关肽 (TRPs)，具有抗菌活性且无溶血作用。
Cas No.:149097-03-0
Sample solution is provided at 25 µL, 10mM.
;)
,-1-7$$$37316672.jpg');)
;)
;)
$$$36806353.jpg');)
;33(7)%EF%BC%9A546-561$$$37156877.jpg');)
;)
;)
;)
%201124-1138.$$$35908550.jpg');)
%20766-780.$$$37100057.jpg');)
%20418-432.$$$36893736.jpg');)
%EF%BC%9A-240-255.$$$35108512.jpg');)
533-545$$$36543525.jpg');)
%201-13.$$$36600053.jpg');)
;)
Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Urechistachykinin I (Uru-TK I), an invertebrate tachykinin-related peptides (TRPs) isolated from echiuroid worms, shows antimicrobial activities without a hemolytic effect[1][2].
[1]. Sung WS, et al. Antimicrobial effect and membrane-active mechanism of Urechistachykinins, neuropeptides derived from Urechis unicinctus. FEBS Lett. 2008 Jul 9;582(16):2463-6. [2]. Kawada T, et al. Identification of multiple urechistachykinin peptides, gene expression, pharmacological activity, and detection using mass spectrometric analyses. Peptides. 2000 Dec;21(12):1777-83.
| Cas No. | 149097-03-0 | SDF | |
| 别名 | Uru-TK I | ||
| 分子式 | C50H85N19O14 | 分子量 | 1176.33 |
| 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。 |
||
| 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 | |||
 |
1 mg | 5 mg | 10 mg |
| 1 mM | 0.8501 mL | 4.2505 mL | 8.501 mL |
| 5 mM | 0.17 mL | 0.8501 mL | 1.7002 mL |
| 10 mM | 0.085 mL | 0.4251 mL | 0.8501 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。
The functional role of the tachykinin consensus region of urechistachykinin peptide family for its antimicrobial activity
Biol Pharm Bull 2011;34(6):921-4.PMID:21628896DOI:10.1248/bpb.34.921.
In our previous study, we reported that Urechistachykinin I (U I) and II (U II) exerted antimicrobial effects. To find out how the tachykinin consensus sequence of the urechistachykinin peptide family affects its antimicrobial activity, analogues substituting the amino acid residues phenylalanine (Phe-6; Anal 1), glycine (Gly-8; Anal 2), and arginine (Arg-10; Anal 3) of U II to alanine (Ala) were designed. Subsequently, the antimicrobial activity was shown on the order of Anal 3>U II=Anal 2>Anal 1, and this activity pattern was correlated with membrane studies such as propidium iodide (PI) influx and fluorescein isothiocyanate dextran (FD) leakage assay. These results suggest that the antimicrobial activity is related to the hydrophobicity values of the peptides. In regards to the activity of U II, it is determined that the hydrophobic Phe-6 plays a more critical role than Gly-8 or Arg-10.
Identification of multiple urechistachykinin peptides, gene expression, pharmacological activity, and detection using mass spectrometric analyses
Peptides 2000 Dec;21(12):1777-83.PMID:11150637DOI:10.1016/s0196-9781(00)00338-7.
Urechistachykinin I and II (Uru-TK I and II) are invertebrate tachykinin-related peptides (TRPs), which have been isolated from echiuroid worms. The cDNA sequence encoding the Uru-TK I and II revealed that the precursor also encoded five TRP-like peptides. Here, we report the characterization of these Uru-TK-like peptides named as Uru-TK III-VII. Northern and Southern blot analyses demonstrated that Uru-TK mRNA is localized in nerve tissue. In addition, the presence of the Uru-TK-like peptides as matured forms in the nerve tissue was detected by mass spectrometric analysis, and identified these peptides were shown to exhibit a contractile activity on cockroach hindgut that was as potent as that of Uru-TK II. Furthermore, synthetic Uru-TK-like peptide analogs which contained Met-NH2 instead of Arg-NH2 at their C-termini were shown to possess a potential to bind to a mammalian tachykinin receptor, indicating that Uru-TK-like peptides are likely to correspond to vertebrate tachykinins, except for the difference at the C-terminal residue. These findings show that Uru-TK-like peptides are essentially equivalent to Uru-TK I and II, leading to the proposal that Uru-TK-like peptides play an essential role as invertebrate tachykinin neuropeptides.
Two novel tachykinin-related neuropeptides in the echiuroid worm, Urechis unicinctus
Biochem Biophys Res Commun 1993 Apr 15;192(1):1-6.PMID:8476410DOI:10.1006/bbrc.1993.1373.
Two novel neuropeptides, Urechistachykinin I (H-Leu-Arg-Gln-Ser-Gln-Phe-Val-Gly-Ser-Arg-NH2) and urechistachykinin II (H-Ala-Ala-Gly-Met-Gly-Phe-Phe-Gly-Ala-Arg-NH2), were isolated from the ventral nerve cords of the echiuroid worm, Urechis unicinctus. These peptides showed a contractile action on the inner circular body-wall muscle of the animal. Their amino acid sequences were found to be significantly homologous with those of the vertebrate and insect tachykinins. The urechistachykinins potentiated spontaneous rhythmic contractions of the cockroach hindgut.
Characterization of a novel cDNA sequence encoding invertebrate tachykinin-related peptides isolated from the echiuroid worm, Urechis unicinctus
Biochem Biophys Res Commun 1999 Oct 5;263(3):848-52.PMID:10512769DOI:10.1006/bbrc.1999.1465.
Tachykinin is one of the most well-known bioactive peptides found in vertebrates, and tachykinin-related peptides have also been isolated from various invertebrate species. Urechistachykinin I (Leu-Arg-Gln-Ser-Gln-Phe-Val-Gly-Ser-Arg-NH(2)) and II (Ala-Ala-Gly-Met-Gly-Phe-Phe-Gly-Ala-Arg-NH(2)) were purified from the ventral nerve cords of echiuroid worm, Urechis unicinctus. In the present study, we described the characterization of a novel cDNA encoding the urechistachykinin precursor. Amino acid sequence analysis of the deduced polypeptide revealed that the urechistachykinin precursor included seven structurally related peptides, unlike mammalian tachykinin precursors which encode only one or two tachykinin peptides. This is the first identification of an invertebrate tachykinin-related peptide cDNA.
Actions of tachykinins on the ion transport across the frog skin
Peptides 1998;19(8):1435-8.PMID:9809659DOI:10.1016/s0196-9781(98)00080-1.
The tachykinin-dependent stimulation of ion transport across frog skin was studied. Tachykinin stimulation was due to interaction with an NK1-like receptor as [Sar9-Met(O2)11]-Substance P (a very selective NK1 agonist) strongly stimulated SCC, whereas [beta-Ala8]-Neurokinin A 4-10 (a very selective NK2 agonist) did not. The rank order of tachykinin potency was: PG-KI > Uperolein > Hylambatin > Kassinin > Phyllomedusin > [Sar9-Met(O2)11]-Substance P > Ranatachykinin A > Physalaemin > Ranakinin > Substance P and Eledoisin >> Neurokinin A. Neurokinin B, Scyliorhinin I, Urechistachykinin I and Urechistachykinin II had no effect. We conclude that the minimal structural requirements for stimulating SCC in the frog skin were the presence of: a) the C-terminal sequence Phe-X-Gly-Leu-Met-NH2; b) at least one Pro residue in the N-terminal sequence.