Recombinant human Proteasome inhibitor PI31 subunit protein Reference: RP10021LQ PI31 is a proline-rich protein and its C-terminal region can act as a potent 20S proteasome inhibitor in vitro. In cells, it plays a role in regulating 26S proteasome assembly and activity.
Recombinant human SENP1 (catalytic domain) protein Reference: RP10024LQ SUMO1-3 (small ubiquitin-related modifiers) are ubiquitin-like proteins that can be conjugated to substrate proteins using a cascade of enzymatic reactions. Protein sumoylation can be reversed by the sentrin-specific (SUMO is also named sentrin) proteases (SENPs). In human cells, SENPs have six members including SENP1, SENP2, SENP3, SENP5, SENP6 and SENP7. SENPs mostly reside in the nucleus. They function to generate mature SUMO1-3 from the SUMO precursors and attenuate signals mediated by sumoylation. The SENP1 catalytic domain comprises amino acid from 419 to 644.
Recombinant human Ubiquitin-conjugating enzyme E2 S/UBE2S(1-156) protein Reference: RP10058LQ UbE2S is an E2 enzyme, which is part of the E1, E2, and E3 cascade responsible for ubiquitination of protein substrates. UbE2S works with the Ub ligase, anaphase-promoting complex (APC/C), to ubiquitinate proteins like Cyclin B1. UbE2S was found to mediate synthesis of K11-specific polyubiquitin chains. UbE2S(1-156) lacks the C-terminal region of UbE2S, and this truncated version is more efficient than UbE2S in catalyzing synthesis of K11-linked polyubiquitin chains.
Recombinant human Ubiquitin (K48R) protein Reference: RP10077LQ 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. In Ub(K48R), lysine 48 was substituted with an arginine, thereby it cannot form lysine 48-linked polyubiquitin chains.
Recombinant human Ubiquitin carboxyl-terminal hydrolase 14 protein Reference: RP10085LQ Usp14 is one of the deubiquitinating enzymes of the human 26S proteasome. Usp14 belongs to the Ub-specific proteases family. Usp14 catalyzes Ub chain trimming that shortens a polyUb chain from the distal end of the Ub chain. Usp14 was found to play an essential role in maintaining the protein levels of monomeric Ub in cells. Interestingly, Usp14 was also found to inhibit proteasomal degradation independent of its deubiquitinating activity.
Recombinant human ADRM1&UCH-L5 protein Reference: RP10087LQ Adrm1 is an integral Ub receptor of the 26S proteasome. Adrm1 binds both Ub and polyUb chains via its N-terminal Pru domain. The Pru domain also binds S1 to locate Adrm1 on the 26S proteasome. The C-terminal domain of Adrm1 binds and activates the deubiquitinating enzyme Uch37, though which Uch37 is recruited to the 26S proteasome. Currently, it is not known whether Adrm1 activates Uch37 to deubiquitinate polyUb chains.
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.