SS28
目录号 : GC37678
SS28是具有口服生物利用度的SRT501 类似物，可抑制微管蛋白聚合，在G2/M引起细胞周期阻滞。SS28会引起细胞凋亡而不是坏死。
Cas No.:141172-08-9
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
SS28, a SRT501 analog with oral bioavailability, inhibits tubulin polymerization to cause cell cycle arrest at G2/M phase. SS28 results in apoptosis rather than necrosis tubulin[1]. Tubulin[1].
SS28 (0-20 μM) induces cytotoxicity in different cancer cell lines[1].SS28 treatment (5 μM for A549 and 2 μM for CEM) results in cell cycle arrest at G2/M phase leading to apoptosis upon further incubation[1]. Cell Proliferation Assay[1] Cell Line: CEM, Reh, Nalm6, SUDHL8, Molt4, A549, HeLa 293T cells.
SS28 (15 mg/kg. b.wt.) treatment results in inhibition of tumor cell proliferation[1]. Animal Model: BALB/c mice using EAC cells[1].
[1]. Thomas E, et al. A Novel Resveratrol Based Tubulin Inhibitor Induces Mitotic Arrest and Activates Apoptosis in Cancer Cells. Sci Rep. 2016 Oct 17;6:34653.
| Cas No. | 141172-08-9 | SDF | |
| Canonical SMILES | CC1=CC=C(/C=C\C2=CC(OC)=C(OC)C(OC)=C2)C=C1 | ||
| 分子式 | C18H20O3 | 分子量 | 284.35 |
| 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 | 3.5168 mL | 17.584 mL | 35.1679 mL |
| 5 mM | 0.7034 mL | 3.5168 mL | 7.0336 mL |
| 10 mM | 0.3517 mL | 1.7584 mL | 3.5168 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。
[111In-DOTA]LTT-SS28, a first pansomatostatin radioligand for in vivo targeting of somatostatin receptor-positive tumors
J Med Chem 2014 Aug 14;57(15):6564-71.PMID:25007399DOI:10.1021/jm500581d.
Radiolabeled pansomatostatin-like analogues are expected to enhance the diagnostic sensitivity and to expand the clinical indications of currently applied sst2-specific radioligands. In this study, we present the somatostatin mimic [DOTA]LTT-SS28 {[(DOTA)Ser1,Leu8,D-Trp22,Tyr25]SS28} and its 111In radioligand. [DOTA]LTT-SS28 exhibited a pansomatostatin-like profile binding with high affinity to all five hsst1-hsst5 subtypes (IC50 values in the lower nanomolar range). Furthermore, [DOTA]LTT-SS28 behaved as an agonist at hsst2, hsst3, and hsst5, efficiently stimulating internalization of the three receptor subtypes. Radioligand [111In-DOTA]LTT-SS28 showed good stability in the mouse bloodstream. It displayed strong and specific uptake in AR42J tumors 4 h postinjection (9.3±1.6% ID/g vs 0.3±0.0% ID/g during sst2 blockade) in mice. Significant and specific uptake was also observed in HEK293-hsst2-, HEK293-hsst3-, and HEK293-hsst5-expressing tumors (4.43±1.5, 4.88±1.1, and <3% ID/g, respectively, with values of <0.5% ID/g during receptor blockade). In conclusion, the somatostatin mimic [111In-DOTA]LTT-SS28 specifically localizes in sst2-, sst3-, and sst5-expressing xenografts in mice showing promise for multi-sst1-sst5 targeted tumor imaging.
Somatostatin in epithelial cells of intestinal mucosa is present primarily as somatostatin 28
Peptides 1984 May-Jun;5(3):615-21.PMID:6147821DOI:10.1016/0196-9781(84)90092-5.
Region-specific antisera to [Tyr14]-SS28(1-14) were used to identify cells containing immunoreactivity to the SS28(1-14) fragment of somatostatin 28 (SS28) in gastric and intestinal mucosal epithelium and in pancreatic islets by immunoperoxidase staining. Radioimmunoassay with iodinated [Tyr14]-SS28(1-14) identified one antiserum (F4) to SS28(1-14) that cross-reacted equally with SS28(1-12), SS28(1-14) and SS28. Two other antisera (F3 and F8) to SS28(1-14) did not cross-react with SS28(1-12) and showed insignificant cross-reactivity to SS28. Immunostaining results showed that F4 stained the same cells that reacted with antiserum AS-10, which is specific for the cyclic tetradecapeptide somatostatin, SS28(15-28). Antisera F3, F4, and F8 all reacted with islet D cells and with somatostatin cells in the antral mucosa. However, only antiserum F4 detected immunoreactivity in mucosal epithelial cells; F3 and F8 did not bind to these cells. After sections of intestine were exposed to trypsin, however, epithelial cells containing immunoreactivity to SS28(1-14) were detected in intestinal mucosa with antisera F3 and F8. These results were obtained for duodenum, jejunum, ileum, and colon, but most of the epithelial cells with immunoreactivity to SS28(1-14) were in the duodenum. Both radioimmunoassay and immunostaining results suggest that F3 and F8 bind to a region of SS28(1-14) that is unavailable to antibodies in the intact SS28 molecule.(ABSTRACT TRUNCATED AT 250 WORDS)
A Novel Resveratrol Based Tubulin Inhibitor Induces Mitotic Arrest and Activates Apoptosis in Cancer Cells
Sci Rep 2016 Oct 17;6:34653.PMID:27748367DOI:10.1038/srep34653.
Resveratrol is one of the most widely studied bioactive plant polyphenols which possesses anticancer properties. Previously we have reported synthesis, characterization and identification of a novel resveratrol analog, SS28. In the present study, we show that SS28 induced cytotoxicity in several cancer cell lines ex vivo with an IC50 value of 3-5 μM. Mechanistic evaluation of effect of SS28 in non-small cell lung cancer cell line (A549) and T-cell leukemic cell line (CEM) showed that it inhibited Tubulin polymerization during cell division to cause cell cycle arrest at G2/M phase of the cell cycle at 12-18 h time period. Immunofluorescence studies confirmed the mitotic arrest upon treatment with SS28. Besides, we show that SS28 binds to Tubulin with a dissociation constant of 0.414 ± 0.11 μM. Further, SS28 treatment resulted in loss of mitochondrial membrane potential, activation of Caspase 9 and Caspase 3, leading to PARP-1 cleavage and finally cell death via intrinsic pathway of apoptosis. Importantly, treatment with SS28 resulted in regression of tumor in mice. Hence, our study reveals the antiproliferative activity of SS28 by disrupting microtubule dynamics by binding to its cellular target Tubulin and its potential to be developed as an anticancer molecule.
A comparative analysis of the distribution of prosomatostatin-derived peptides in human and monkey neocortex
J Comp Neurol 1991 Jan 22;303(4):584-99.PMID:1672875DOI:10.1002/cne.903030406.
Comparative analyses were made of the immunohistochemical and biochemical distributions of three prosomatostatin-derived peptides (PSDP) in human, perfused monkey, and unperfused monkey neocortex. The PSDP we examined were the tetradecapeptide somatostatin 14 (SS14); the N-terminal extension of this peptide, somatostatin 28 (SS28); and somatostatin 28(1-12) (SS28(1-12)). In immunohistochemical experiments, numerous SS28-immunoreactive perikarya were located in both superficial and deep layers of perfused monkey cortex, but none were present in the cerebral cortex from unperfused monkey or autopsied human brains. In contrast, the number of SS28(1-12)-immunoreactive neurons was five times greater in the superficial cortical layers of unperfused monkey than of perfused monkey brain. Moreover, unperfused monkey and human cortex contained notably more SS14-immunoreactive processes than perfused monkey cortex. These data suggested that SS28 may have been converted into SS14 and SS28(1-12) in unperfused tissue during the post-mortem interval. This hypothesis was examined biochemically by measuring the levels of immunoreactivity of SS14, SS28, and SS28(1-12) in samples of unperfused monkey cortex frozen at different time intervals after removal from the brain. Samples frozen 10 minutes or longer after removal contained only 10-20% the level of SS28 immunoreactivity measured in samples frozen immediately or 1 minute after removal. The levels of SS14 and SS28(1-12) immunoreactivity did not demonstrate such reductions, and may instead have increased at early time points. To further characterize post-mortem effects on PSDP and to explore for species differences, we performed a detailed comparison of the regional, laminar, and cellular distribution of SS28(1-12) immunoreactivity under the three conditions. A progressive loss of immunoreactivity, particularly in radial fibers, was found at increasing post-mortem intervals in unperfused monkey neocortex, indicating that differences in density and distribution of immunoreactive fibers between human and perfused monkey may result from post-mortem peptide degradation in unperfused tissue. In contrast, the larger size of SS28(1-12)-immunoreactive white matter neurons in humans as compared to monkeys appeared partially due to a post-mortem effect but also reflected a species difference. In addition, the density of white matter neurons was found to be significantly greater in human than in perfused or unperfused monkey. These data indicate that any study of human autopsy material must be assessed in light of possible post-mortem effects.(ABSTRACT TRUNCATED AT 250 WORDS)
The effect of albumin fusion structure on the production and bioactivity of the somatostatin-28 fusion protein in Pichia pastoris
J Ind Microbiol Biotechnol 2014 Jun;41(6):997-1006.PMID:24752560DOI:10.1007/s10295-014-1440-5.
Somatostatin, a natural inhibitor of growth hormone (GH), and its analogs have been used in clinical settings for the treatment of acromegaly, gigantism, thyrotropinoma, and other carcinoid syndromes. However, natural somatostatin is limited for clinical usage because of its short half-life in vivo. Albumin fusion technology was used to construct long-acting fusion proteins and Pichia pastoris was used as an expression system. Three fusion proteins (SS28)(2)-HSA, (SS28)(3)-HSA, and HSA-(SS28)(2), were constructed with different fusion copies of somatostatin-28 and fusion orientations. The expression level of (SS28)(3)-HSA was much lower than (SS28)(2)-HSA and HSA-(SS28)(2) due to the additional fusion of the somatostatin-28 molecule. MALDI-TOF mass spectrometry revealed that severe degradation occurred in the fermentation process. Similar to the standard, somatostatin-14, all three fusion proteins were able to inhibit GH secretion in blood, with (SS28)(2)-HSA being the most effective one. A pharmacokinetics study showed that (SS28)(2)-HSA had a prolonged half-life of 2 h. These results showed that increasing the number of small protein copies fused to HSA may not be a suitable method for improving protein bioactivity.