- SynonymUCHL3,Ubiquitin thioesterase L3
- SourceHuman UCH-L3, His Tag (UC3-H5141) is expressed from E.coli cells. It contains AA Glu 2 - Ala 230 (Accession # P15374-1).Predicted N-terminus: MetRequest for sequence
- Molecular Characterization

This protein carries a polyhistidine tag at the N-terminus.
The protein has a calculated MW of 27.0 kDa. The protein migrates as 27 kDa under reducing (R) condition (SDS-PAGE).
- EndotoxinLess than 1.0 EU per μg by the LAL method.
- Purity
>95% as determined by SDS-PAGE.
- Formulation
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
- Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
- Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.

Human UCH-L3, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
- BackgroundUbiquitin carboxyl-terminal hydrolase isozyme L3 (UCH-L3), a member of peptidase C12 family, is also known as ubiquitin thioesterase L3. Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. UCH-L3 is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. UCH-L3 indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. It is also required for stress-response retinal, skeletal muscle and germ cell maintenance. Furthermore, UCH-L3 may be involved in working memory and can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.
- References
- (1)Nam M.J., et al., 2003, Proteomics 3:2108-2115.
- (2)Setsuie R., et al., 2009, Neurochem. Int. 54:314-321.
- (3)Iphofer A., et al., 2012, ChemBioChem 13:1416-1420.
Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.
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最好能说得具体点,小弟对此几乎一窍不通
谢谢
1. 粗纯:将制备抗体的血清或是腹水,细胞上清,直接用盐析法进行处理,这样可以将这些物质里面的其他杂质去掉,获得蛋白的成分,但是由于是粗纯,里面会混有大量的其他蛋白,这样获得的抗体,纯度较低,用于实验中背景比较高。
2.通用型纯化:用抗体结合蛋白Protein A,Protein G或者Protein L。因为不同来源的抗体和这些抗体结合蛋白的结合能力不同,所以需要根据抗体来源选择使用哪种抗体将诶和蛋白最好。对于有一些单链抗体,则多半使用protein L来进行纯化。经过抗体结合蛋白的亲和纯化后,溶液中基本只保留了抗体的成分,其他蛋白都去掉了,抗体纯度可以比较高。相对来说,这种方法是大规模抗体制备中,用得最多的纯化方法,很多抗体公司都采用这种方法来对抗体进行纯化。
3.特异型纯化:但是有些抗体,需要纯度特别高,特异性特别好,就不能简单采用上述两种方法进行纯化了。必须要通过将抗原固定制备成特异的亲和纯化柱,再纯化抗体。这个时候得到的就全是针对一种抗原的抗体了,特异性最好。当然,由于牵涉到抗原固定等操作,成本相应是最高的。
1. 粗纯:将制备抗体的血清或是腹水,细胞上清,直接用盐析法进行处理,这样可以将这些物质里面的其他杂质去掉,获得蛋白的成分,但是由于是粗纯,里面会混有大量的其他蛋白,这样获得的抗体,纯度较低,用于实验中背景比较高。
2.通用型纯化:用抗体结合蛋白Protein A,Protein G或者Protein L。因为不同来源的抗体和这些抗体结合蛋白的结合能力不同,所以需要根据抗体来源选择使用哪种抗体将诶和蛋白最好。对于有一些单链抗体,则多半使用protein L来进行纯化。经过抗体结合蛋白的亲和纯化后,溶液中基本只保留了抗体的成分,其他蛋白都去掉了,抗体纯度可以比较高。相对来说,这种方法是大规模抗体制备中,用得最多的纯化方法,很多抗体公司都采用这种方法来对抗体进行纯化。
3.特异型纯化:但是有些抗体,需要纯度特别高,特异性特别好,就不能简单采用上述两种方法进行纯化了。必须要通过将抗原固定制备成特异的亲和纯化柱,再纯化抗体。这个时候得到的就全是针对一种抗原的抗体了,特异性最好。当然,由于牵涉到抗原固定等操作,成本相应是最高的。

