- Home
- About
- Products
- E1 Activating
- E2 Conjugating
- E3 Ligase
- Deconjugating
- Proteasome
- Ubiquitin
- All
- Ubiquitin and Ubiquitin Derivatives
- Ubiquitin Chains
- DUB-Resistant, Non-Hydrolyzable Chains
- NH Isopeptide-linked chains
- DCA Linked Chains
- K6-linked Chains (DCA)
- Agarose Bound K6-linked Chains (DCA)
- K11-linked Chains (DCA)
- Agarose Bound K11-linked Chains (DCA)
- K29-linked Chains (DCA)
- Agarose Bound K29-linked Chains (DCA)
- K33-linked Chains (DCA)
- Agarose Bound K33-linked Chains (DCA)
- K48-linked Chains (DCA)
- Agarose Bound K48-linked Chains (DCA)
- K63-linked Chains (DCA)
- Agarose Bound K63-linked Chains (DCA)
- K76-linked Chains (DCA)
- Agarose Bound K76-linked Chains (DCA)
- Ubiquitin Mutants
- Labeled Ubiquitin Proteins
- Antibodies, ELISAs and Kits
- SUMO
- NEDD8
- ISG15
- UFM1
- URM1
- Autophagy
- FAT10
- Inhibitors
- Antibodies
- Kits
- Buffers, Solutions, Standards
- Substrate Proteins
- Affinity Matrices / Proteins
- Fractions
- FUBI
- References
- Orders
- Contact
Material Data Sheet
Methylated Ubiquitin
Price: $44.00
Methylated Ubiquitin
Price:
209
Quantity:
1 mg, 5 mg
Data Sheet:
Reductive methylation of lysine residues renders ubiquitin unable to form poly-ubiquitin chains. Methylated Ub can form an E1-catalyzed active thioester at the C-terminus allowing the molecule to be transferred to the lysines of substrate proteins (mono-ubiquitination). Ideal for studies in which a reduction in poly-ubiquitin chain length is desired, or in instances when multi-mono-ubiquitination of a substrate protein is needed.
Product Information
MW:
8.5 kDa
Purity:
>95% by SDS-PAGE
Solubility:
Soluble in aqueous buffers up to 50 mg/ml.
Supplied:
This is a lyophilized powder Use & Storage
Use:
Typical concentrations for non rate-limiting support of in vitro conjugation reactions are 100 μM-500 µM depending on reaction conditions.
Storage:
Store at -20°C after solubilization. Avoid multiple freeze/thaw cycles.
Literature
References:
Hershko A. and Heller H. (1985) Bioch.Biophys.Res Comm. 128:1079-1086
Hershko A., et al. (1991) J.Biol.Chem. 266: 16376-16370
Jentoft N. and Dearborn D.G. (1979) J.Biol.Chem. 254:4359-4365
Jentoft N. and Dearborn D.G. (1980) Anal.Biochem. 106:186-190
Jentoft N. and Dearborn D.G. (1983) Methods.Enz. 91:570-579
0 items $0.00
