Recombinant human Fluorescein labeled K48-Ub(2-10) protein Reference: RP10092LQ This product contains authentic K48-linked isopeotide bonds, synthesized by an enzymatic reaction containing UbE1, GST-E2-25K and fluorescein-Ub (catalog # E1155/E1156). Mainly contain Ub(2-10) chains with residual monoubiquitin. Can be visualized with in-gel Fluorescein fluorescence (excitation at ~490 nm), that is more quantitative than immunoblotting and sensitive in assays including deubiquitination and ubiquitin binding.
Recombinant human Deubiquitinase DESI2 protein Reference: RP10100LQ DESI-2 (desumoylating isopeptidase 2, also called Permuted Papain fold Peptidases of DsRNA viruses and Eukaryotes (PPPDE1)) and DESI-1 (also called PPPDE2) contain a Ub-binding domain and a cysteine protease domain. They catalyze both desumolyating and deubiquitinating activities.
Recombinant human Atrophin-1 interacting protein 4/ITCH protein Reference: RP10137LQ ITCH, also called atrophin-1 interacting protein 4 (AIP4), is a HECT-type E3 ubiquitin ligase. It contains an N-terminal Ca-dependent phospholipid-binding C2 domain, four WW domains, and a C-terminal HECT domain. Mice deficient in ITCH protein display many autoimmune-like disease characteristics such as lymphoproliferation in the spleen and lymph nodes. More than a dozen of substrates of ITCH have been identified including p63, p73 and Notch1. The ligase may be responsible for ubiquitinating proteins with K29-, K48-, and/or K63-linked ubiquitin chains.
Recombinant human K11-Ub2 protein Reference: RP10139LQ 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-Ub4 protein Reference: RP10149LQ 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 TNF-alpha protein Reference: RP10171LQ TNFalpha (Tumor necrosis factor alpha) is produced by immune and epithelial cells. It plays important roles in regulating inflammation, apoptosis, and immune response. It exerts its function mainly by binding of two cell surface receptors TNFR1 and TNFR2. Treating cells with TNFalpha activates the NFkappaB, MAPK, and death signaling pathways. The recombinant TNFalpha protein consists of the extracellular domain (amino acids 77-233) of full length TNFalpha. It induces apoptosis of various cancer cells at the concentration of 10-100 ng/mL + 1 ug/mL cycloheximide (a protein translation inhibitor). It is generated from GST-TNFalpha (catlog # U1130) by removal of the N-terminal GST tag.
Recombinant human Ubiquitin protein Reference: RP10173LQ 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 Ubiquitin(+1) protein Reference: RP10174LQ Ubiquitin (+1) consists of the first 75 amino acids of ubiquitin, but lacks glycine 76 because of the deletion of two of the three nucleotides that encode glycine 76. The resulting frame shift leads to the addition of 20 amino acids (YADLREDPDRQDHHPGSGAQ) after glycine 75. Ubiquitin (+1) can not support ubiquitination reactions. When expressed at high levels, it could inhibit proteasomal degradation. Ubiquitin (+1) was also found in protein aggregates in patient brains of Alzheimer’s disease and other neurodegenerative diseases.
20S proteasome Reference: RP10191TLQ The 20S proteasome has a barrel – shaped structure arranged as four heptomeric rings of αββα. In eukaryotes, each of α and β ring is composed of seven different proteins. The β1, β2 and β5 subunits have ‘caspase-like’, ‘trypsin-like’ and ‘chymotypsin-like’ activities, respectively. In 26S proteasome-mediated protein degradation, to entry the β chamber of the 20S proteasome that houses the proteolytic sites, a substrate protein has to pass through a substrate translocation channel consisting of the double-ring formed by six ATPases of PA700 and the α chamber formed by α subunits of the 20S proteasome.
K6-linked diUb Reference: RP10195D This product is a native K6-linked diUb which can be used as a substrate for deubiquitinating enzymes. It can also be used to investigate linkage specificiy of proteins that contain ubiquitin-associated domains or ubiquitin-interacting motifs. This product is formed by chemical ligation.
N-terminal Biotin-Ubiquitin Reference: RP10199DLQ A single biotin moiety is conjugated on the N-terminus of ubiquitin. All lysine residues of ubiquitin are still available for formation of polyubiquitin chains. The extremely high binding affinity between biotin and streptavidin allows the use of N-terminal biotin-ubiquitin for the following in vitro assays: 1) rapid and efficient purification of polyubiquitinated substrate proteins; 2) monitoring substrate ubiquitination using an HRP-conjugated streptavidin antibody; and 3) setting up high throughput FRET assays to monitor substrate ubiquitination in assays screening E3 ubiquitin ligase inhibitors.
Recombinant human Ubiquitin carboxyl-terminal hydrolase 7/USP7 protein Reference: RP10201LQ 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.