Recombinant human Ubiquitin thioesterase L3/UCHL3 protein Reference: RP10188LQ Ubiquitin C-terminal hydrolase L3 (UchL3) is a deubiquitinase enzyme (DUB), which performs hydrolysis of the bond at the C terminus of the ubiquitin and trims down the polyubiquitin chain into monomers. UchL3 has been found to also process a ubiquitin-like substrate called NEDD8. It is 52% identical to the amino acid sequence of its related DUB, UchL1, and may share roles in maintaining neurons of the gracile tract in mice.
26S proteasome Reference: RP10189TLQ The 26S proteasome is an approximately 2.5 mDa large complex composed of the 20S proteasome and the 19S regulatory particle (also called PA700 in mammals). The 20S proteasome has 28 subunits that form a barrel – shaped structure arranged as four heptomeric ring of αββα. Three β subunits have peptidase activities that hydrolyze proteins. Either one or both ends of the 20S proteasome can associate with PA700 to form the 26S proteasome. PA700 contains 19 different proteins that have the ability to bind, deubiquitinate and unfold polyubiquitinated proteins with the consumption of ATP hydrolysis. The 26S proteasome degrades polyubiquitinated proteins, which plays essential roles in regulating various cellular events including protein quality control, gene transcription and signal transduction.
19S proteasome/PA700 Reference: RP10190TLQ The 19S regulatory particle (PA700) locates on either one or both ends of the 20S core particle of the 26S proteasome. It has 19 subunits including six AAA ATPases that associate with α subunits of the 20S proteasome to form the 26S proteasome. PA700 plays an essential role in preparing substrate proteins to be degraded by the 20S proteasome, including binding, deubiquitinating and unfolding polyubiquitinated proteins.
immuno 20S proteasome Reference: RP10192TLQ Upon stimulation with IFN – γ, the expression of the three catalytic β subunits β1, β2, and β5 with iso-forms β1i (LMP2), β2i (MECL – 1), and β5i (LMP7) are induced, respectively. These subunits are incorporated into the 20S proteasome to form the immune 20S proteasome. It was reported that the immunoproteasome has altered proteolytic activities compared to its normal form, which favor the generation of immunopeptides for antigen presentation.
Recombinant human Ubiquitin-activating enzyme E1/UBE1/UBA1 protein Reference: RP10193LQ UBE1 is an E1 enzyme within the E1, E2, E3 cascade which conjugates Ub to protein substrates. UBE1 activates Ub by catalyzing an ATP – dependent reaction; Ub is conjugated onto the catalytic cysteine residue of UBE1 by formation of a thioester bond. The activated Ub is then passed on to a Ub-conjugating enzyme E2; Ub charged E2 binds a Ub ligase E3 that directly binds substrate proteins. Ub is transferred to the HECT domain E3s prior to being conjugated on substrate proteins. For RING domain E3s, Ub is transferred directly from an E2 to substrate proteins.
K29-linked diUb Reference: RP10197D This product is a native K29-linked diUb which can be used as a substrate of deubiquitinating enzyems. It can also be used to investigate linkage specificity of proteins that contain ubiquitin-associated domains or ubiquitin-interacting motifs. This product is formed by chemical ligation.
K33-linked diUb Reference: RP10198D This product is a native K33-linked diUb which can be used as a substrate for deubiquitinating enzymes. It can also be used to investigate linkage specificity of proteins that contain ubiquitin-associated domains or ubiquitin-interacting motifs). This product is formed by chemical ligation.
N-terminal TAMRA-Ubiquitin Reference: RP10200DLQ N-terminal TARMA-Ub (also called TARMA-Ub) is a fluorescent Ub, in which TAMRA (5-tetramethylrhodamine) is covalently conjugated on the N-terminus of Ub. All seven lysine residues in TARMA-Ub are available for ubiquitination. This product can be used for determination of protein ubiquitination or E1/E2/E3 enzyme activity using sensitive in-gel fluorescence. TAMRA fluorescence is detected using excitation/emission wavelengths at 550 nm/590 nm, respectively.
Recombinant human Ubiquitin carboxyl-terminal hydrolase 7/USP7 protein Reference: RP10202LQ USP7 is a cysteine protease, belongs to the family of ubiquitin-specific proteases. USP7 was first discovered as a binding enzyme to the Herpes simplex viral protein. Studies have shown that USP7 could deubiquitinate the autoubiquitination of an E3 ligase called HDM2 that promotes ubiquitination and subsequent degradation of p53. The USP7/HDM2/p53 interaction results in higher protein levels of HDM2 and lower levels of p53. Because of its apparent role in different types of pathologies, including lung and liver cancer, it has become a possible target for drug therapies.
Recombinant human Ubiquitin carboxyl-terminal hydrolase 11/USP11 protein Reference: RP10203LQ Deubiquitinating enzymes (DUBs) are proteases that posses the ability to cleave ubiquitin chains or the isopeptide bond that conjugates ubiquitin with a substrate. Human cells have approximately 100 DUBs that play important roles in regulating various cellular events. Usp11 belongs to the ubiquitin-specific protease family. It helps in repairing DNA damage. It has been found to interact with RanBPM, a RanGTP-binding protein.
Recombinant human Ubiquitin carboxyl-terminal hydrolase 16 protein Reference: RP10204LQ USP16 is an active deubiquitinating enzyme (DUB) encoded on chromosome 21, trisomy of which causes Down’s syndrome (DS). USP16 is a phosphoprotein, phosphorylation of USP16 controls its cellular localization, but no effect on its DUB activity. USP16 deubiquitinates histone 2A (H2A), through which USP16 might regulate gene expression and cell cycle progression. Increased USP16 protein levels in people with DS might contribute to the development of certain phenotypes of DS.
Recombinant human Ubiquitin carboxyl-terminal hydrolase 35/USP35 protein Reference: RP10205LQ USP35 is a 1018 amino acid cysteine DUB that was found to be overexpressed in certain breast cancers. Its USP domain ranges from amino acids 425 to 926, with cysteine 450 as the catalytic cysteine residue.