Calcitonin (8-32), salmon
目录号 : GC35586
Calcitonin (8-32), salmon 是具有高度选择性的糊精受体 (amylin receptor) 的拮抗剂。
Cas No.:155069-90-2
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
Calcitonin (8-32), salmon is a highly selective amylin receptor antagonist[1].
[1]. Silvestre RA, et al. Effect of (8-32) salmon calcitonin, an amylin antagonist, on insulin, glucagon and somatostatin release: study in the perfused pancreas of the rat. Br J Pharmacol. 1996 Jan;117(2):347-50.
| Cas No. | 155069-90-2 | SDF | |
| 分子式 | C119H198N36O37 | 分子量 | 2725.06 |
| 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 | 0.367 mL | 1.8348 mL | 3.6696 mL |
| 5 mM | 0.0734 mL | 0.367 mL | 0.7339 mL |
| 10 mM | 0.0367 mL | 0.1835 mL | 0.367 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。
Effect of (8-32) salmon calcitonin, an amylin antagonist, on insulin, glucagon and somatostatin release: study in the perfused pancreas of the rat
Br J Pharmacol 1996 Jan;117(2):347-50.PMID:8789389DOI:10.1111/j.1476-5381.1996.tb15197.x.
1. The 8-32 fragment of salmon calcitonin ((8-32) sCT) has been proposed as a highly selective amylin receptor antagonist. 2. In the present study, we have studied the influence of (8-32) sCT on the inhibitory effect of both amylin and its structural congener, calcitonin gene-related peptide (CGRP), on insulin secretion in the rat perfused pancreas. 3. Both amylin and CGRP, at 75 pM, clearly inhibited glucose-induced insulin release (by 80% and by 70%, respectively). Simultaneous infusion of 10 microM (8-32) sCT reversed the inhibitory effect of amylin (by 80%; P < 0.05 vs. amylin experiments) but did not significantly affect the inhibition of glucose-induced insulin output elicited by CGRP. Furthermore, at the same concentration (10 microM), (8-32) sCT alone potentiated the insulin response to 7 mM glucose (2.5 fold; P < 0.05) whilst it did not affect glucagon or somatostatin secretion. 4. The observation that infusion of an amylin antagonist into the rat pancreas potentiates the insulin response to glucose, favours the concept of endogenous amylin as an inhibitor of insulin release. 5. Finally, as an amylin antagonist at the level of the beta-cell, (8-32) sCT might be considered of potential interest in experimental and clinical pharmacology.
Novel calcitonin-(8-32)-sensitive adrenomedullin receptors derived from co-expression of calcitonin receptor with receptor activity-modifying proteins
Biochem Biophys Res Commun 2003 Feb 7;301(2):460-4.PMID:12565884DOI:10.1016/s0006-291x(02)03072-3.
We tested whether heterodimers comprised of calcitonin (CT) receptor lacking the 16-amino acid insert in intracellular domain 1 (CTR(I1-)) and receptor activity-modifying protein (RAMP) can function not only as calcitonin gene-related peptide (CGRP) receptors but also as adrenomedullin (AM) receptors. Whether transfected alone or together with RAMP, human (h)CTR(I1-) appeared mainly at the surface of HEK-293 cells. Expression of CTR(I1-) alone led to significant increases in cAMP in response to hCGRP or hAM, though both peptides remained about 100-fold less potent than hCT. However, the apparent potency of AM, like that of CGRP, approached that of CT when CTR(I1-) was co-expressed with RAMP. CGRP- or AM-evoked cAMP production was strongly inhibited by salmon CT-(8-32), a selective amylin receptor antagonist, but not by hCGRP-(8-37) or hAM-(22-52), antagonists of CGRP and AM receptors, respectively. Moreover, the inhibitory effects of CT-(8-32) were much stronger in cells co-expressing CTR(I1-) and RAMP than in cells expressing CTR(I1-) alone. Co-expression of CTR(I1-) with RAMP thus appears to produce functional CT-(8-32)-sensitive AM receptors.
Type II Turn of Receptor-bound salmon calcitonin Revealed by X-ray Crystallography
J Biol Chem 2016 Jun 24;291(26):13689-98.PMID:27189946DOI:10.1074/jbc.M116.726034.
Calcitonin is a peptide hormone consisting of 32 amino acid residues and the calcitonin receptor is a Class B G protein-coupled receptor (GPCR). The crystal structure of the human calcitonin receptor ectodomain (CTR ECD) in complex with a truncated analogue of salmon calcitonin ([BrPhe(22)]sCT(8-32)) has been determined to 2.1-Å resolution. Parallel analysis of a series of peptide ligands showed that the rank order of binding of the CTR ECD is identical to the rank order of binding of the full-length CTR, confirming the structural integrity and relevance of the isolated CTR ECD. The structure of the CTR ECD is similar to other Class B GPCRs and the ligand binding site is similar to the binding site of the homologous receptors for the calcitonin gene-related peptide (CGRP) and adrenomedulin (AM) recently published (Booe, J. M., Walker, C. S., Barwell, J., Kuteyi, G., Simms, J., Jamaluddin, M. A., Warner, M. L., Bill, R. M., Harris, P. W., Brimble, M. A., Poyner, D. R., Hay, D. L., and Pioszak, A. A. (2015) Mol. Cell 58, 1040-1052). Interestingly the receptor-bound structure of the ligand [BrPhe(22)]sCT(8-32) differs from the receptor-bound structure of the homologous ligands CGRP and AM. They all adopt an extended conformation followed by a C-terminal β turn, however, [BrPhe(22)]sCT(8-32) adopts a type II turn (Gly(28)-Thr(31)), whereas CGRP and AM adopt type I turns. Our results suggest that a type II turn is the preferred conformation of calcitonin, whereas a type I turn is the preferred conformation of peptides that require RAMPs; CGRP, AM, and amylin. In addition the structure provides a detailed molecular explanation and hypothesis regarding ligand binding properties of CTR and the amylin receptors.
Receptor pharmacology
Adv Pharmacol 2005;52:47-65.PMID:16492540DOI:10.1016/S1054-3589(05)52003-9.
Despite clear evidence for a distinct amylin pharmacology and localization of such pharmacology to sites such as the nucleus accumbens,efforts to clone an amylin receptor were fruitless for over a decade. This enigma led many to doubt the status of amylin as a bona fide hormone. Yet it became apparent during those cloning efforts that, whatever the amylin receptor was, it was somehow similar to a calcitonin receptor. The enigma of the amylin receptor was solved following the identification of receptor activity modifying proteins (RAMPs). These single transmembrane spanning molecules, when associated with a calcitonin receptor, altered its pharmacology from calcitonin-preferring to amylin-preferring. With at least two forms of the calcitonin receptor and three forms of RAMP, there is the potential for six subtypes of amylin receptors. Of these, two appear to predominate. The CTa (shorter form) calcitonin receptor, dimerized with RAMP1 [amylin 1 (a) receptor], appears to represent binding sites at the nucleus accumbens and the subfornical organ. Binding sites at area postrema appear to be composed of CTa + RAMP3 [amylin3 (a) receptors]. Thus far, RAMP proteins have been associated in vivo only with the CT/CLR receptor system. It is presently unknown whether RAMPs are more general modulators of receptor function, dynamically modifying responsivity with time or across other receptor classes. The largest and first identified amylin-binding field was in the nucleus accumbens. The function of these receptors is yet undetermined, but because the nucleus accumbens is within the blood-brain barrier, the cognate ligand is unlikely to be circulating amylin. Dense amylin binding is present at the circumventricular organs, including the subfornical organ, the organum vasculosum lateralis terminalis (OVLT), and the area postrema. There is no diffusional (blood-brain) barrier at these structures, so they most likely respond to circulating (beta-cell-derived) amylin. Despite pharmacological evidence of amylin sensitivity in several peripheral tissues, selective amylin binding outside of the brain is observed only in the renal cortex. The newly designated amylinomimetic drug class was defined on the basis of its unique pharmacology prior to the molecular characterization of amylin receptors. Currently, the class includes any agent that acts as antagonist at characterized amylin receptors. Several peptides, typically analogs of truncated salmon calcitonin, have been developed as potent and selective amylin antagonists and have been useful in identifying amylinergic responses. Of these, AC187 (30Asn32Tyr[8-32]sCT; Amylin Pharmaceuticals Inc.) is particularly selective and potent, and has been most often cited in studies using amylin antagonists. Antagonism of a response with an order of potency of AC187> AC66 > CGRP[8-37] is suggestive that it is mediated via amylin receptors. Activation of a response with salmon calcitonin (sCT) > amylin >calcitonin gene-related peptide (CGRP) > mammalian CT suggests activation via the amylinl (a) receptor, while sCT = amylin >> CGRP >mammalian CT suggests activation via amylin3 (a) receptors. Absence of response to other ligands (e.g., adrenomedullin) is useful for excluding certain pharmacologies.
The presence of islet amyloid polypeptide/calcitonin gene-related peptide/salmon calcitonin binding sites in the rat nucleus accumbens
Eur J Pharmacol 1994 Sep 1;262(1-2):133-41.PMID:7813564DOI:10.1016/0014-2999(94)90036-1.
Receptor autoradiographic analysis of binding in rat brain sections for [125I]islet amyloid polypeptide (IAPP), [125I]calcitonin gene-related peptide (CGRP) and [125I]salmon calcitonin indicated dense binding for all three ligands in the nucleus accumbens. Membrane binding studies revealed the existence of high affinity sites for all three peptides. The order of potency of various related peptides at each binding site was investigated and found for [125I]IAPP to be salmon calcitonin > IAPP = alpha CGRP > salmon calcitonin-(8-32); for [125I]CGRP to be alpha CGRP > IAPP > salmon calcitonin; and for [125I]salmon calcitonin to be salmon calcitonin > alpha CGRP > rat calcitonin > salmon calcitonin-(8-32) > IAPP, suggesting that [125I]IAPP targets the CGRP3 receptor subtype. This study confirms the existence of two receptors in the rat nucleus accumbens binding salmon calcitonin, one of which binds alpha CGRP and IAPP with a high affinity.