UbcH5c, active
N-terminal HA, 6His-tagged, recombinant human UbcH5c full length, expressed in E.coli.
Biological information
Background
Ubiquitin-conjugating (E2) enzymes are characterized by the presence of a highly conserved ubiquitin-conjugating domain which accommodates ATP-activated ubiquitin (Ub) via a covalently linked thioester onto its active-site residue. E2 enzymes act via selective protein-protein interactions with the ubiquitin-activating E1 enzyme and ubiquitin ligase E3 enzymes and are able to differentiate effects on downstream substrates, either with a single Ub molecule or a Ub chain. While E3s are involved in substrate selection, E2s are the main determinants for selection of the lysine to construct Ub chains, which thereby directly control the cellular fate of the substrate.
The UbcH5 family (UbcH5a, UbcH5b and UbcH5c) have been shown to be the most active class of E2 enzymes in cell extracts and are associated with the control of a number of proteins including the transcriptional regulators p53, IκBα and HIF-1α.
Target class
Ubiquitin
Family
E2
Accession number
GenBank NM_181888
Target Name
UbcH5c, active
Target Alias
E2(17)KB3, UBC4/5, UBCH5C
Origin
Human
Theori. MW
19 kDa
Affinity tag
N-terminal HA, 6His-tag
Product specifications
Expression system
expressed in E. coli cells
Purity
99%
Purification method
Immobilized metal affinity chromatography
Sample Buffer
3.33 mg/ml of enzyme in 50 mM Tris/HCl pH 7.5, 300 mM NaCl, 0.1 mM EGTA, 0.03% Brij-35, 270 mM sucrose, 1 mM benzamidine, 0.2 mM PMSF, 0.1% 2-mercaptoethanol. Frozen solution.
Specified activity
Refer to CoA
Application
For Research Only
Storage conditions
1 year at -70°C
Usage disclaimer
For Research Only
Chemical data
Background
Ubiquitin-conjugating (E2) enzymes are characterized by the presence of a highly conserved ubiquitin-conjugating domain which accommodates ATP-activated ubiquitin (Ub) via a covalently linked thioester onto its active-site residue. E2 enzymes act via selective protein-protein interactions with the ubiquitin-activating E1 enzyme and ubiquitin ligase E3 enzymes and are able to differentiate effects on downstream substrates, either with a single Ub molecule or a Ub chain. While E3s are involved in substrate selection, E2s are the main determinants for selection of the lysine to construct Ub chains, which thereby directly control the cellular fate of the substrate.
The UbcH5 family (UbcH5a, UbcH5b and UbcH5c) have been shown to be the most active class of E2 enzymes in cell extracts and are associated with the control of a number of proteins including the transcriptional regulators p53, IκBα and HIF-1α.
Compound name
Ubiquitin
Catalog number
23-035
Molecular formula
CAS
MW
Ka
Percent composition
Product specifications
Physical state
Purity (HPLC 214nm)
Retention time (RP18 HPLC)
CMC
Exact mass
Stability
For Research Only
Solubility structure
Datasheets
23-035
Datasheet