Recombinant Human Poly-SUMO3 Wild-type Chains (2-8), CF Summary
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins.Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration.The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard.In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
ULC-310
| Formulation | X mg/ml in 50 mM HEPES pH 8, 100 mM NaCl, 1 mM DTT |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: Poly-SUMO3
Human Small Ubiquitin-like Modifier 3 (SUMO3), also known as SMT3A, is synthesized as a 103 amino acid (aa), propeptide with a predicted 11.5 kDa. SUMO3 contains a two aa C-terminal prosegment. Poly-SUMO3 represents chains of wild-type recombinant human SUMO3 molecules linked via lysine residue 11, which is the point of attachment for the C-terminal glycine residue of the preceding SUMO3 (1). SUMO3 monomers and dimers have been removed from the chain mixture. Human SUMO3 shares 83% sequence identity with mouse SUMO3. Di-SUMO3 can be used as a substrate for SUMO-specific isopeptidases (SENPs) and DeSUMOylating Isopeptidase 1 (DeSI-1) that cleave the isopeptide linkage between two SUMO3 molecules (2). It can also be used to investigate mechanisms of binding and recognition by SUMO-activating (E1) enzymes, SUMO-conjugating (E2) enzymes, SUMO ligases (E3s), and other proteins that contain SUMO binding domains.
SUMOs are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed SUMOylation (3-5). Unlike SUMO1 which is usually conjugated to proteins as a monomer, SUMO2 and SUMO3 form high molecular weight polymers on proteins. All SUMO proteins share a conserved Ubiquitin domain and a C-terminal diglycine cleavage/attachment site. Following prosegment cleavage, the C-terminal glycine residue of SUMO3 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO3 is conjugated to a variety of molecules in the presence of the SAE1/UBA2 SUMO-activating (E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme (6,7). In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p (8).
Poly-SUMO-3 chains can be used to investigate mechanisms of chain recognition, binding and hydrolysis by SUMO-specific isopeptidases (SENPs), SUMO-specific E3 ligases or other proteins that contain SUMO-3 binding domains. This product is formed enzymatically with wild type Human Recombinant SUMO-3 linked via lysine 11 which is the point of attachment for the C-terminal glycine of the preceding SUMO-3. Mono-SUMO-3 has been removed from the chain mixture.
- Bylebyl, G.R. et al. (2003) J. Biol. Chem. 278:44113.
- Shin, E.J. et al. (2012) EMBO Rep. 13:339.
- Desterro, J.M. et al. (1997) FEBs. Lett. 417:297.
- Bettermann, K. et al. (2012) Cancer Lett. 316:113.
- Praefcke, G.J. et al. (2012) Trends Biochem. Sci. 37:23.
- Okuma, T. et al. (1999) Biochem. Biophys. Res. Commun. 254:693.
- Tatham, M.H. et al. (2001) J. Biol. Chem. 276:35368.
- Johnson, E.S. et al. (1997) EMBO J. 16:5509.
Citation for Recombinant Human Poly-SUMO3 Wild-type Chains (2-8), CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products.The data collected includes not only links to publications in PubMed,but also provides information about sample types, species, and experimental conditions.
1Citation: Showing 1 - 1
- The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1? sumoylation and poly-SUMO chain elongationProc Natl Acad Sci USA, 2016;113(24):6725-30.Species: HumanSample Types: Recombinant ProteinApplications: Bioassay
FAQs
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各位业内前辈，我们正在考虑引进符合GMP认证标准的CHO细胞系，用于表达可做疫苗生产的重组蛋白类。目前已有符合标准信息的是Thermofisher的CHO-S悬浮培养细胞资料，希望能再多了解一些和这株细胞类似的其他公司符合GMP标准的生产株细胞做个比较。谢谢指教！
国内或者国外进口皆可！？看来你不缺钱啊！
这个问题问的过于笼统！
首先，蛋白表达与纯化包括很多种类型，比如原核蛋白表达，哺乳动物蛋白表达，酵母蛋白表达以及昆虫蛋白表达等等，而现在生物实验中常说的蛋白表达纯化通常是指利用大肠杆菌表达系统的原核蛋白表达，这种表达方式比较简单，普遍都可以做。但是如果是指很多种蛋白表达系统的话，可以做的单位就比较少了。
另外，蛋白的表达成功与否还需要取决于蛋白的性质，所以前期一定要问清楚！
事实上,现在多数药用级别白蛋白都是用血清生产的.
白蛋白的销售方向若是面向实验室,可采用重组质粒转到微生物发酵的方法生产,对土地面积的要求小,更集约,成本效率更高.
我想在体外培养的细胞中，加入PD-L1重组蛋白，激活PD-L1:PD-1通路，但我没能查到相关的文献，不清楚PD-L1重组蛋白的用量。请问各位有相关的经验吗？或者阅读过相关的文献？
而没答案
帮帮我
给我提供答案
考研细胞的题答案
基因敲除除可中止某一基因的表达外，还包括引入新基因及引入定点突变。既可以是用突变基因或其它基因敲除相应的正常基因，也可以用正常基因敲除相应的突变基因。 基因敲除是80年代后半期应用DNA同源重组原理发展起来的一门新技术。80年代初，胚胎干细胞（ES细胞）分离和体外培养的成功奠定了基因敲除的技术基础。1985年，首次证实的哺乳动物细胞中同源重组的存在奠定了基因敲除的理论基础。到1987年，Thompsson首次建立了完整的ES细胞基因敲除的小鼠模型。此后的几年中，基因敲除技术得到了进一步的发展和完善。
基因敲除的技术路线如下：
（1）构建重组基因载体﹔
（2）用电穿孔、显微注射等方法把重组DNA转入受体细胞核内﹔
（3）用选择培养基筛选已击中的细胞﹔
（4）将击中细胞转入胚胎使其生长成为转基因动物，对转基因动物进行形态观察及分子生物学检测。
基因敲除的靶细胞目前最常用的是小鼠ES细胞。基因敲除的技术路线虽不复杂，但由于高等真核细胞内外源DNA与靶细胞DNA序列自然发生同源重组的机率非常低，约为百万分之一，要把基因敲除成功的细胞筛选出来是一件非常困难的工作。因此，同源重组的筛选和检测就成了基因敲除技术所要解决的关键问题。目前已有多种筛
