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SUMO 蛋白酶/Ulp1肽酶(Ulp1)
Ulp1 (SUMO Protease /Ulp1 peptidase)
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买2送1活动进行中!购买任意2个规格产品,免费赠送100μL装一支。
活动截止时间:2024年1月31日
                            
                                
                                买2送1活动进行中!购买任意2个规格产品,免费赠送100μL装一支。
活动截止时间:2024年1月31日
Ulp1 (SUMO Protease /Ulp1 peptidase)(货号:PRP3001)是一种基于酿酒酵母SUMO蛋白酶的重组工具酶,通过特异性识别SUMO蛋白三级结构,高效切除SUMO融合标签,适用于重组蛋白纯化流程中标签的精准去除。
SUMO(小分子泛素修饰)蛋白酶1(Ulp1)属于半胱氨酸蛋白酶家族,其独特之处在于通过构象识别而非氨基酸序列特异性结合SUMO(Smt3)蛋白。该酶源于酿酒酵母ULP1亚型(UniProt Q02724),能显著提升融合蛋白在原核/真核表达系统中的溶解性和稳定性。本产品采用大肠杆菌表达系统制备重组酵母ULP1片段(403-621 aa),N/C端均带有His标签,冻干形态可最大限度保持酶活性,为蛋白质工程提供关键酶解工具。
应用领域:主要应用于重组蛋白纯化过程中的SUMO标签切除,特别适用于提高原核/真核系统表达蛋白的溶解性与得率,在蛋白质工程、结构生物学研究及生物制药领域具有核心应用价值。
                                    | 中文名称 | SUMO 蛋白酶/Ulp1肽酶(Ulp1) | 
| 英文名称 | Ulp1 (SUMO Protease /Ulp1 peptidase) | 
| 产品货号 | PRP3001 | 
| 序列 | 氨基酸序列来源于:ULP1 亚型(Q02724)(403-621 aa + N-terminal Poly-6*His tag C-terminal Poly-6*His tag)表达的蛋白片段。 | 
| 蛋白长度 | 重组酵母ULP1由219个氨基酸组成,预测分子量为28.7 KD。由于糖基化,在还原性条件下的SDS-PAGE中,重组人ULP1的分子量约为28 KD。 | 
| 表达宿主 | 大肠杆菌 | 
| 纯度 | > 90 % ,使用SDS-PAGE检测 | 
| 产品形式 | 冻干粉,冻干缓冲液为无菌的20 mM Tris,500 mM NaCl,pH 8.0。 | 
| 分子量 | 28.7 kDa | 
| 基因ID | 856087 | 
| 蛋白质ID | Q02724 | 
| 蛋白序列链接 | https://www.uniprot.org/uniprot/Q02724 | 
| 注意事项 | 打开试管前一定要进行离心。建议使用我们提供的缓冲液将冻干的Ulp1重新配制至5 U/μ L,然后将其进一步稀释到其他水溶液中。鉴定活动的结果所产生的SUMO蛋白酶的分子量可参考图。 | 
| 保存建议 | 冻干Ulp1蛋白制品应在-20℃以下干燥保存。请避免冻融循环。 | 
| 运输条件 | 冰袋运输(蓝冰) | 
| 警告 | 本文列出的产品仅供研究使用,不适用于人类或临床诊断。我们产品所推荐应用,不是建议使用我们的产品去违反任何专利或许可证。对于使用本产品可能发生的专利侵权或其他违规行为,我们不承担任何责任。 | 
Amino acid sequence derived from Ulp1 isoform (Q02724) ( 403-621 aa + N-terminal Poly-6*His tag C-terminal Poly-6*His tag) was expressed.
The recombinant human Ulp1 consists of 219 amino acids and has a predicted molecular mass of 28.7 kDa.
Lyophilized from sterile 20 mM Tris, 500 mM NaCl pH 8.0.
One unit of SUMO Protease is defined as the amount of enzyme needed to cleave 85% of 2 µg of substrate protein at 30°C in one hour.
4°C enzyme digestion overnight is recommended, users can explore according to their own research target protein.After digestion, a small amount of samples can be taken for SDS-PAGE analysis.To remove the Ulp1 in the digested system, use His tag purification resin affinity chromatography.
Lyophilized Ulp1 protein product should be stored desiccated below -20°C. Please prevent freeze-thaw cycles.
Fig1. SDS-PAGE analysis of Ulp1.
Fig1. SDS-PAGE analysis of Ulp1.
Always centrifuge tubes before opening. It is recommended to reconstitute the lyophilized Ulp1 to 5 U/μ L using the buffer we provided, which can then be further diluted to other aqueous solutions. The results of the identification of the activity of the produced SUMO Protease enzyme can be referred to the figure.
25 μ g
5 μ L
2 μ L
50 μ L
25 μ g
25 μ g
5 μ L
5 μ L
2 μ L
2 μ L
50 μ L
50 μ L
Figure 2. The effect of SUMO Protease on cleaving the target protein with SUMO tag. 25 µg of purified SUMO fusion protein was used for each sample, and the reaction system was 50 uL. 1:SUMO Protease; 2 :SUMO fusion protein; 3 :The reaction effect as shown in the above figure; 4-13: The cleavage effects with the enzyme amount halved successively. All reactions were sampled after 1 hour of digestion at 30℃ for SDS-PAGE electrophoresis and Coomassie brilliant blue staining.
(Note:10×SUMO Protease Buffer includes 500 mM Tris, 2% NP-40, 10 mM DTT; pH8.0)
Figure 2. The effect of SUMO Protease on cleaving the target protein with SUMO tag. 25 µg of purified SUMO fusion protein was used for each sample, and the reaction system was 50 uL. 1:SUMO Protease; 2 :SUMO fusion protein; 3 :The reaction effect as shown in the above figure; 4-13: The cleavage effects with the enzyme amount halved successively. All reactions were sampled after 1 hour of digestion at 30℃ for SDS-PAGE electrophoresis and Coomassie brilliant blue staining.
(Note:10×SUMO Protease Buffer includes 500 mM Tris, 2% NP-40, 10 mM DTT; pH8.0)
Note: The product listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.
Note: The product listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.
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杂志名称: EMBO reports | 作者: McNeil, J. Bryan, et al.
IF: 6 | 发表时间: 2024
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