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商品描述
Ubiquitin (Ub) is a 76 amino acid protein widely expressed in the cytoplasmic and nucleus of cells. Ub is posttranslationally conjugated to proteins by the E1, E2, E3 protein ubiquitination cascade. Ub can be conjugated on proteins as monoUb or polyUb chains. Protein ubiquitination plays both proteolytic and nonproteolytic functions. Usually, polyubiquitinated proteins are targeted to the 26S proteasome for proteolysis. Typical concentration to support in vitro ubiquitination is 50-100 µM. In Ub(K48 only), all lysine residues but lysine 48 were substituted with arginines, thereby it only supports the formation of lysine 48-linked polyubiquitin chains.
Additional Information
| Product Name: | 6xHis-Ubiquitin (K48 only) |
|---|---|
| Also Known As: | 6xHis-[K48-only]Ub |
| Catalog No.: | E1870 |
| Size: | 1 mg |
| Molecular Weight: | 8.5 kDa |
| Species: | Human |
| Source: | Bacterial recombinant |
| Stock: | 20 mM Tris, 150 mM NaCl, 2 mM βME, 10% Glycerol |
| Concentration: | See tube label |
| Quality Assurance: | ~95% by SDS-PAGE, see datasheet for gel image |
| Storage: | Store at -80°C; avoid multiple freeze-thaw cycles |
| PDF Data Sheet: | PDF Datasheet， MSDS |
| NCBI RefSeq: | N/A |
| Image(s): | No |
| Shipping Method: | Dry ice shipping |
| References: | 1. Hershko A, et al. (1980) Proc Natl Acad Sci USA 77(4), 1783 – 1786. 2. Pickart CM (1997) FASEB 11(13), 1055 – 1066. 3. Hershko A, et al. (1998) Ann Rev Biochem 67, 425 – 479. 4. Jiang X, et al. (2012) Nature Reviews Immunology 12, 35 – 48. 5. Bremm A, et al. (2012) Methods Mol Biol 832, 291 – 228. |
Details
Ubiquitin (Ub) is a 76 amino acid protein widely expressed in the cytoplasmic and nucleus of cells. Ub is posttranslationally conjugated to proteins by the E1, E2, E3 protein ubiquitination cascade. Ub can be conjugated on proteins as monoUb or polyUb chains. Protein ubiquitination plays both proteolytic and nonproteolytic functions. Usually, polyubiquitinated proteins are targeted to the 26S proteasome for proteolysis. Typical concentration to support in vitro ubiquitination is 50-100 µM. In Ub(K48 only), all lysine residues but lysine 48 were substituted with arginines, thereby it only supports the formation of lysine 48-linked polyubiquitin chains.
Images (Click image to enlarge)
Coomassie-stained SDS-PAGE Lane 1: Molecular weight markers Lane 2: 5 µg purified 6xHis-Ubiquitin (K0)
Lane 3: 5 µg purified 6xHis-Ubiquitin (K6 only) Lane 4: 5 µg purified 6xHis-Ubiquitin (K11 only)
Lane 5: 5 µg purified 6xHis-Ubiquitin (K27 only) Lane 6: 5 µg purified 6xHis-Ubiquitin (K29 only)
Lane 7: 5 µg purified 6xHis-Ubiquitin (K33 only) Lane 8: 5 µg purified 6xHis-Ubiquitin (K48 only)
Lane 9: 5 µg purified 6xHis-Ubiquitin (K63 only)
UBPBio are formed by conjugating the C-terminal glycine residue of Ub onto any of seven internal lysine residues or the amino group of the previous Ub. Ub chains are classified by the lysine residue used to link Ubs; different Ub chain topologies can result in different signals. For instance, Ub chains linked through lysine 6, 11, 27, 29, 33 and 48 are capABLe of targeting proteins for proteasomal degradation; in contrast, Ub chains linked through lysine 63 or the N-terminal amino group (linear Ub chains) often play important nonproteolytic functions including regulation of kinase activation and protein translation. All Ub chain products are produced by using of human wild type Ub reacting with specific E2s.Additional InformationProduct Name:K11-Ub(n≥3)Also Known As:K11-Ub(n≥3)Catalog No.:D3301Size:50 µgMolecular Weight:N/ASpecies:HumanSource:Bacterial recombinantStock:20 mM Tris, 150 mM NaCl, 2 mM βME, 10% GlycerolConcentration:See tube labelQuality Assurance:~95% by SDS-PAGE, see datasheet for gel imageStorage:Store at -80°C; avoid multiple freeze-thaw cyclesPDF Data Sheet:PDF Datasheet， MSDSNCBI RefSeq:N/AImage(s):N/AShipping Method:Dry ice shippingReferences:1. Hershko A, et al. (1980)Proc Natl Acad Sci USA 77(4), 1783 – 1786.2. Pickart CM, (1997) FASEB 11(13), 1055 – 1066.3. Hershko A, et al. (1998) Ann Rev Biochem 67, 425 – 479.4. Jiang X, et al. (2012) Nature Reviews Immunology 12, 35 – 48.DetailsUb chains are formed by conjugating the C-terminal glycine residue of Ub onto any of seven internal lysine residues or the amino group of the previous Ub. Ub chains are classified by the lysine residue used to link Ubs; different Ub chain topologies can result in different signals. For instance, Ub chains linked through lysine 6, 11, 27, 29, 33 and 48 are capable of targeting proteins for proteasomal degradation; in contrast, Ub chains linked through lysine 63 or the N-terminal amino group (linear Ub chains) often play important nonproteolytic functions including regulation of kinase activation and protein translation. All Ub chain products are produced by using of human wild type Ub reacting with specific E2s. Images (Click image to enlarge)
Coomassie-stained SDS-PAGE Lane 1: Molecular weight markers Lane 2: 5 µg purified 6xHis-Ubiquitin (K0)
Lane 3: 5 µg purified 6xHis-Ubiquitin (K6 only) Lane 4: 5 µg purified 6xHis-Ubiquitin (K11 only)
Lane 5: 5 µg purified 6xHis-Ubiquitin (K27 only) Lane 6: 5 µg purified 6xHis-Ubiquitin (K29 only)
Lane 7: 5 µg purified 6xHis-Ubiquitin (K33 only) Lane 8: 5 µg purified 6xHis-Ubiquitin (K48 only)
Lane 9: 5 µg purified 6xHis-Ubiquitin (K63 only)
