CRF, bovine
(Synonyms: CRF,CRH,促肾上腺皮质激素释放激素,Corticotropin Releasing Factor bovine) 目录号 : GC35748
CRF, bovine 是一种有效的 CRF 受体激动剂，能够取代 [125I-Tyr]ovine CRF，Ki 值为3.52 nM。
Cas No.:92307-52-3
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: | CRF (1 μM) is added to the cell cultures that are further incubated for 5, 15 and 30 min at 37°C. Control cells are incubated with medium only. Following incubation time, cells are lysed directly on the growth dish using the detergent provided by the cAMP enzyme immunoassay kit. Following trypan blue staining to ensure complete lysis, the cell lysate is collected and assayed for cAMP. In some cases, the brain microvessel endothelial cells (BMEC) are treated with forskolin or pretreated either with the CRFR antagonist Antalarmin (1 μM) or the ATP analogue 2′5′-deoxyadenosine for 5 min at 37°C[3]. |
References: [1]. Hogg JE, et al. The human neuroblastoma cell line, IMR-32, expresses functional corticotropin-releasing factor receptors. Eur J Pharmacol. 1996 Sep 26;312(2):257-61. | |
CRF, bovine is a potent agonist of CRF receptor, and displaces [125I-Tyr]ovine CRF with a Ki of 3.52 nM. Ki: 3.52 nM (CRF receptor)[1]
CRF, bovine is a potent agonist of CRF receptor, and displaces [125I-Tyr]ovine CRF with a Ki of 3.52 nM[1]. CRF shows pEC50s of 11.16, 8.53 and 8.70 for human CRF1, human CRF2 and rat CRF2α[2]. CRF is released from hypothalamic-pituitary-adrenal (HPA) axis induced by stress, and leads to production of glucocorticoids which down regulate immune responses. CRF also has proinflammatory effects. CRF affects brain microvessel endothelial cells (BMEC) structure or function, CRF (100 nM) significantly increases cAMP in BMEC[3].
[1]. Hogg JE, et al. The human neuroblastoma cell line, IMR-32, expresses functional corticotropin-releasing factor receptors. Eur J Pharmacol. 1996 Sep 26;312(2):257-61. [2]. Smart D, et al. Characterisation using microphysiometry of CRF receptor pharmacology. Eur J Pharmacol. 1999 Aug 27;379(2-3):229-35. [3]. Esposito P, et al. Corticotropin-releasing factor (CRF) can directly affect brain microvessel endothelial cells. Brain Res. 2003 Apr 11;968(2):192-8.
| Cas No. | 92307-52-3 | SDF | |
| 别名 | CRF,CRH,促肾上腺皮质激素释放激素,Corticotropin Releasing Factor bovine | ||
| 分子式 | C206H340N60O63S | 分子量 | 4697.34 |
| 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 | 0.2129 mL | 1.0644 mL | 2.1289 mL |
| 5 mM | 0.0426 mL | 0.2129 mL | 0.4258 mL |
| 10 mM | 0.0213 mL | 0.1064 mL | 0.2129 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。
A comparison between the equine and bovine hypothalamus-pituitary-adrenocortical axis
Domest Anim Endocrinol 2016 Jul;56 Suppl:S101-11.PMID:27345307DOI:10.1016/j.domaniend.2016.02.008.
In this review, we address the function of the hypothalamus-pituitary-adrenocortical (HPA) axis with special emphasis on the comparison between the bovine and equine species. The pars intermedia of the pituitary gland is particularly well developed in horses and cattle. However, its function is not well appreciated in cattle yet. The Wulzen's cone of the adenohypophysis is a special feature of ruminants. Total basal cortisol concentration is much higher in horses than that in cows with similar free cortisol fractions. Corticotropin-releasing factor (CRF) concentrations in equine pituitary venous blood are lower compared with other species, whereas plasma ACTH concentrations in cows are higher than those in horses. A CRF challenge test induced a more pronounced cortisol response in horses compared with cattle, whereas regarding ACTH challenge testing, the opposite seems true. Based on data from literature, the bovine species is characterized by relatively high basal blood CRF and ACTH and low cortisol and glucose concentrations. Obviously, further lowering of blood cortisol in cattle is easily prevented by the high sensitivity to ACTH, and as a consequence, subsequent increased gluconeogenesis prevents imminent hypoglycemia. Hypoglycemia is less likely in horses given their high muscle glycogen content and their relatively high cortisol concentration. When assessing HPA axis reactivity, response patterns to exogenous ACTH or CRH might be used as a reliable indicator of animal welfare status in cows and horses, respectively, although it is emphasized that considerable caution should be exercised in using measures of HPA activity solely to assess animal welfare.
In vivo and in vitro comparisons of biological activities of bovine, ovine and rat CRF (corticotrophin-releasing factor)
Acta Endocrinol (Copenh) 1984 Jun;106(2):158-67.PMID:6328821DOI:10.1530/acta.0.1060158.
The biological activity of partially purified bovine hypothalamic CRF (corticotrophin- releasing factor) was compared to those of synthetic CRFs (ovine, rat) sauvagine and vasopressin in vivo and in vitro. ACTH-primed hypophysectomized rats with heterotopically transplanted pituitaries and medial basal hypothalamic ablation (H-T + MBHA ), and intact rats pre-treated with chlorpromazine, morphine and Nembutal (C-M-N) were used for in vivo CRF assays. Perifused rat adenohypophyseal fragments were employed for in vitro studies. CRF-A (void volume fractions, 'big' CRF) and CRF-B (Kav = 0.583) purified from bovine hypophyseal stalk, synthetic ovine and rat CRF, and sauvagine all induced significant stimulation of ACTH and/or corticosterone secretion in these systems. Synthetic ovine and rat CRF and sauvagine showed comparable CRF potency. The CRF dose-response slopes for bovine CRF were somewhat steeper than those for ovine CRF or sauvagine in the in vitro system. Vasopressin had the least steep dose-response slope. Intravenous bolus administration of ovine CRF caused a more prolonged (greater than 20 min) elevation of plasma ACTH compared to a relatively short duration after bovine CRF-A. These data suggest that bovine hypothalamus contains substance(s) which exhibits different CRF characteristics from those of ovine CRF.
Corticotropin releasing factor (CRF)-like immunoreactivity in the hypothalamus and posterior pituitary of the goat, bovine, rat, monkey and human
Endocrinol Jpn 1984 Feb;31(1):7-13.PMID:6428866DOI:10.1507/endocrj1954.31.7.
Goat hypothalamic extract prepared by HCl extraction and chromatographed on a Sephadex G-50 column showed two immunoreactive CRF peaks. Most of the immunoreactivity coeluted with synthetic ovine CRF, and a small peak eluted near the void volume. Bovine, monkey, rat and human hypothalamic extracts prepared by acid-acetone or acid-methanol extraction showed three immunoreactive peaks. Most of the immunoreactivity coeluted with ovine CRF, and other smaller peaks eluted near the void volume and slightly before arginine vasopressin. Goat hypothalamic extract showed the highest cross-reactivity with anti-ovine CRF serum, followed by bovine hypothalamic extract. Less cross-reactivity was found in human, rat and monkey hypothalamic extracts. CRF immunoreactivity in goat hypothalamic extract coeluted with ovine CRF on reversed phase high performance liquid chromatography (HPLC) and main CRF immunoreactivity in human and rat hypothalamic extracts eluted slightly later than ovine CRF. These results suggest that there is a heterogeneity among the CRF molecules in these species and that goat CRF may be more similar to that of sheep CRF and the amino acid sequence or molecular weight of other animals CRF may be different from that of sheep CRF. The monkey posterior pituitary and rat neurointermediate lobe showed similar elution patterns of CRF immunoreactivity to their hypothalamic extracts on Sephadex gel filtration and HPLC. These results indicate that the posterior pituitary contains a similar CRF to hypothalamic CRF.
Differential effects of dithiothreitol and iodoacetamide on corticotropin-releasing factor (CRF) activity of bovine hypothalamic CRFs and vasopressin
Endocrinology 1982 Jun;110(6):2074-80.PMID:6280987DOI:10.1210/endo-110-6-2074.
Various fractions were tested in vivo for corticotropin-releasing factor (CRF) activity after Sephadex G-100 fractionation of 0.1-N HCl extracts of bovine hypophyseal stalk or cerebral cortex. Female rats pretreated with chlorpromazine, morphine, and Nembutal were used for CRF assay. CRF-A (void volume fractions; big CRF), CRF-B (Kav = 0.583), and CRF-C (salt volume fractions) of bovine hypophyseal stalk and lysine or arginine vasopressin all induced clear-cut stimulation of ACTH and corticosterone in the assay rat, whereas they were ineffective in acutely hypophysectomized rats. Control fractions purified from bovine cerebral cortex had no CRF activity. Treatment of arginine and lysine vasopressin and CRF-C with dithiothreitol and iodoacetamide completely abolished their CRF activity, whereas the CRF activities of CRF-A and CRF-B were unaltered by these treatments. Treatment with iodoacetamide alone had no effect on the CRF activity of any of these substances. Fractionation of either CRF-C or arginine vasopressin on Sephadex G-15 yielded a CRF-active peak at a Kav of 0.35. We conclude that 1) three different forms of CRF exist in bovine hypophyseal stalk; 2) CRF-A and CRF-B are unrelated to vasopressin and require neither a disulfide bond(s) nor a sulfhydryl group(s) for their CRF activity; 3) reduction of the disulfide bond of vasopressin destroys both CRF and antidiuretic activities; 4) CRF-C requires an intact disulfide bond(s) for its CRF activity and is likely to be either vasopressin itself or a substance closely related to vasopressin; and 5) CRF-B is likely to be the physiologically important form of bovine CRF.
beta-Lactotensin derived from bovine beta-lactoglobulin suppresses food intake via the CRF system followed by the CGRP system in mice
Peptides 2009 Dec;30(12):2228-32.PMID:19720102DOI:10.1016/j.peptides.2009.08.018.
We found that beta-lactotensin (His-Ile-Arg-Leu), which has been isolated as an ileum-contracting peptide from chymotrypsin digest of bovine beta-lactoglobulin, dose-dependently suppresses food intake after intracerebroventricular (i.c.v.) or intraperitoneal administration at a dose of 40 nmol/mouse or 100mg/kg, respectively, in fasted mice. Orally administered beta-lactotensin also suppressed food intake at 500 mg/kg. We previously reported that beta-lactotensin acts as an agonist for neurotensin receptors; however, the anorexigenic activity of beta-lactotensin was not inhibited by i.c.v. co-administration with SR48692 or levocabastine, an antagonist for neurotensin NT(1) or NT(2) receptor, respectively. On the other hand, the anorexigenic effect of beta-lactotensin was blocked by i.c.v. co-administration with astressin or calcitonin gene-related peptide (CGRP)(8-37), an antagonist for corticotropin releasing factor (CRF) or CGRP, respectively. beta-Lactotensin had affinity for neither CRF nor CGRP receptor. In addition, CRF-induced anorexigenic activity after i.c.v. administration was completely blocked by CGRP(8-37), while CGRP-induced anorexigenic activity was not inhibited by astressin. These results suggest that the CGRP system is activated downstream of the CRF system in food intake regulation. Taken together, beta-lactotensin may suppress food intake by activating the CRF system followed by the CGRP system, independently of the neurotensin system.