SEC
目录号 : GC60336
SEC通过AMPK/mTORC1/STAT3信号通路诱导ANXA7GTPase的激活。SEC选择性的促进癌细胞的凋亡，诱导ITGB4核转位，表达高水平ITGB4。
Cas No.:1802997-81-4
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
SEC induces activation of ANXA7 GTPase via the AMPK/mTORC1/STAT3 signaling pathway. SEC selectively promotes apoptosis in cancer cells, expressing a high level of ITGB4 by inducing ITGB4 nuclear translocation[1][2].
SEC (20 µM) inhibits the cell migration of HEK 293T RKIP-/- cells and PC3 prostate cancer cells[1].SEC (20 µM) significantly increases AMPK phosphorylation in PC3 cells, which is inverted by ANXA7 GTPase specific inhibitor ABO, indicating that activated ANXA7 with enhanced phosphorylation level promotes AMPK phosphorylation (cell selectively)[1]. Cell Viability Assay[1] Cell Line: HEK293T RKIP-/- cells.[1]
SEC (3 mg/kg/day or 18 mg/kg/day) suppresses metastasis in PC-3M-Luc orthotopic implantation nude mice model[1]. Animal Model: Luciferase-labeled PC-3M-Luc cells (2×106 per 50 µL sterile HBSS-/-) are orthotopically inoculated into the prostates of 8-week-old nude mice[1].
[1]. ShuYan Liu, et al. SEC-induced Activation of ANXA7 GTPase Suppresses Prostate Cancer Metastasis. Cancer Lett. 2018 Mar 1;416:11-23. [2]. ShuYan Liu, et al. A small molecule induces integrin β4 nuclear translocation and apoptosis selectively in cancer cells with high expression of integrin β4. Oncotarget. 2016 Mar 29; 7(13): 16282-16296.
| Cas No. | 1802997-81-4 | SDF | |
| Canonical SMILES | O=C(OCC)C1=CC(C2=CC=C(C=C2)OC)=NN1C[C@@H](COC3=CC=C(C=C3)Cl)O | ||
| 分子式 | C22H23ClN2O5 | 分子量 | 430.88 |
| 溶解度 | 储存条件 | ||
| 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 | 2.3208 mL | 11.6042 mL | 23.2083 mL |
| 5 mM | 0.4642 mL | 2.3208 mL | 4.6417 mL |
| 10 mM | 0.2321 mL | 1.1604 mL | 2.3208 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。
How Quality Control Systems AID Sec-Dependent Protein Translocation
Front Mol Biosci 2021 Apr 13;8:669376.PMID:33928127DOI:10.3389/fmolb.2021.669376.
The evolutionarily conserved SEC machinery is responsible for transporting proteins across the cytoplasmic membrane. Protein substrates of the SEC machinery must be in an unfolded conformation in order to be translocated across (or inserted into) the cytoplasmic membrane. In bacteria, the requirement for unfolded proteins is strict: substrate proteins that fold (or misfold) prematurely in the cytoplasm prior to translocation become irreversibly trapped in the cytoplasm. Partially folded SEC substrate proteins and stalled ribosomes containing nascent SEC substrates can also inhibit translocation by blocking (i.e., "jamming") the membrane-embedded SEC machinery. To avoid these issues, bacteria have evolved a complex network of quality control systems to ensure that SEC substrate proteins do not fold in the cytoplasm. This quality control network can be broken into three branches, for which we have defined the acronym "AID": (i) avoidance of cytoplasmic intermediates through cotranslationally channeling newly synthesized SEC substrates to the SEC machinery; (ii) inhibition of folding SEC substrate proteins that transiently reside in the cytoplasm by molecular chaperones and the requirement for posttranslational modifications; (iii) destruction of products that could potentially inhibit translocation. In addition, several stress response pathways help to restore protein-folding homeostasis when environmental conditions that inhibit translocation overcome the AID quality control systems.
The unique tRNASec and its role in selenocysteine biosynthesis
Amino Acids 2018 Sep;50(9):1145-1167.PMID:29948343DOI:10.1007/s00726-018-2595-6.
Selenium (Se) is an essential trace element for several organisms and is mostly present in proteins as L-selenocysteine (SEC or U). SEC is synthesized on its L-seryl-tRNASec to produce Sec-tRNASec molecules by a dedicated selenocysteine synthesis machinery and incorporated into selenoproteins at specified in-frame UGA codons. UGA-Sec insertion is signaled by an mRNA stem-loop structure called the SElenoCysteine Insertion Sequence (SECIS). tRNASec transcription regulation and folding have been described showing its importance to SEC biosynthesis. Here, we discuss structural aspects of Sec-tRNASec and its role in SEC biosynthesis as well as SEC incorporation into selenoproteins. Defects in the SEC biosynthesis or incorporation pathway have been correlated with pathological conditions.
Structural Basis of the SEC Translocon and YidC Revealed Through X-ray Crystallography
Protein J 2019 Jun;38(3):249-261.PMID:30972527DOI:10.1007/s10930-019-09830-x.
Protein translocation and membrane integration are fundamental, conserved processes. After or during ribosomal protein synthesis, precursor proteins containing an N-terminal signal sequence are directed to a conserved membrane protein complex called the SEC translocon (also known as the SEC translocase) in the endoplasmic reticulum membrane in eukaryotic cells, or the cytoplasmic membrane in bacteria. The SEC translocon comprises the Sec61 complex in eukaryotic cells, or the SecY complex in bacteria, and mediates translocation of substrate proteins across/into the membrane. Several membrane proteins are associated with the SEC translocon. In Escherichia coli, the membrane protein YidC functions not only as a chaperone for membrane protein biogenesis along with the SEC translocon, but also as an independent membrane protein insertase. To understand the molecular mechanism underlying these dynamic processes at the membrane, high-resolution structural models of these proteins are needed. This review focuses on X-ray crystallographic analyses of the SEC translocon and YidC and discusses the structural basis for protein translocation and integration.
The SEC System: Protein Export in Escherichia coli
EcoSal Plus 2017 Nov;7(2):10.1128/ecosalplus.ESP-0002-2017.PMID:29165233DOI:10.1128/ecosalplus.ESP-0002-2017.
In Escherichia coli, proteins found in the periplasm or the outer membrane are exported from the cytoplasm by the general secretory, SEC, system before they acquire stably folded structure. This dynamic process involves intricate interactions among cytoplasmic and membrane proteins, both peripheral and integral, as well as lipids. In vivo, both ATP hydrolysis and proton motive force are required. Here, we review the SEC system from the inception of the field through early 2016, including biochemical, genetic, and structural data.
The SEC translocon mediated protein transport in prokaryotes and eukaryotes
Mol Membr Biol 2014 Mar-May;31(2-3):58-84.PMID:24762201DOI:10.3109/09687688.2014.907455.
Protein transport via the SEC translocon represents an evolutionary conserved mechanism for delivering cytosolically-synthesized proteins to extra-cytosolic compartments. The SEC translocon has a three-subunit core, termed Sec61 in Eukaryotes and SecYEG in Bacteria. It is located in the endoplasmic reticulum of Eukaryotes and in the cytoplasmic membrane of Bacteria where it constitutes a channel that can be activated by multiple partner proteins. These partner proteins determine the mechanism of polypeptide movement across the channel. During SRP-dependent co-translational targeting, the ribosome threads the nascent protein directly into the SEC channel. This pathway is in Bacteria mainly dedicated for membrane proteins but in Eukaryotes also employed by secretory proteins. The alternative pathway, leading to post-translational translocation across the SEC translocon engages an ATP-dependent pushing mechanism by the motor protein SecA in Bacteria and a ratcheting mechanism by the lumenal chaperone BiP in Eukaryotes. Protein transport and biogenesis is also assisted by additional proteins at the lateral gate of SecY/Sec61α and in the lumen of the endoplasmic reticulum or in the periplasm of bacterial cells. The modular assembly enables the SEC complex to transport a vast array of substrates. In this review we summarize recent biochemical and structural information on the prokaryotic and eukaryotic SEC translocons and we describe the remarkably complex interaction network of the SEC complexes.