Recombinant human Ubiquitin protein Reference: RP10134LQ 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.
Recombinant human Heat shock 70 kDa protein 1A/HSP70 protein Reference: RP10135LQ HSP70 a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, Hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Hsp70 and Hsp40 recruit some misfolded proteins to the ubiquitin E3 ligase CHIP for ubiquitination.
Recombinant human K11-Ub(n≥3) protein Reference: RP10138LQ Ub 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.
Recombinant human K48-Ub(2-8) protein Reference: RP10141LQ Ub 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.
Recombinant human K48-Ub2 protein Reference: RP10142LQ Ub 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.
Recombinant human K48-Ub3 protein Reference: RP10143LQ Ub 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.
Recombinant human K48-Ub4 protein Reference: RP10144LQ Ub 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.
Recombinant human K63-Ub(2-12) protein Reference: RP10146LQ Ub 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.
Recombinant human K63-Ub2 protein Reference: RP10147LQ Ub 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.
Recombinant human Linear Ub2 protein Reference: RP10152LQ The linear ubiquitin chains are formed by conjugating the N-terminal methionine residue of one ubiquitin with the C-teminal glycine residue of another ubiquitin. This product is expressed in E. coli as a fusion protein.
Recombinant human Non-cleavable Linear Ub6 protein Reference: RP10156LQ Non-cleavable linear Ub6 was a derivative of 6xHis-non-cleavable linear Ub6 by removal of the N-terminal 6xHis and 3xHA tags using TEV digestion. The G76V substitution was introduced in the first five Ub moieties and the last Ub has G76.
Recombinant human Non-cleavable SUMO-2 Chain (2-6) protein Reference: RP10157LQ Non-cleavable SUMO2 chains are made of the SUMO2(Q90P) mutant, this substitution makes the formed polySUMO chains to be resistant to SENP proteases.