Category: Proteins & Peptides

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Reference: RP10082LQ

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. Studies have shown that polyUb chains formed by the Ub(L73P) mutant are resistant to deubiquitination catalyzed by many deubiquitination enzymes.

Reference: RP10083LQ

Ub75 lacks the amino acid glycine 76, which is required to form thioester bond with Ub activating enzyme E1. Therefore, Ub75 can not react with E1, E2 and E3 enzymes; and does not support ubiquitination. It can be used as a negative control in ubiquitination reactions; or to assay binding of Ub with Ub binding proteins or ubiquitination enzymes.

Reference: RP10084LQ

Uch37 is one of the deubiquitinating enzymes of the human 26S proteasome, belongs to the Ub C-terminal hydrolases. Uch37 was found to bind both Adrm1 and S5a subunits of the 26S proteasome. Uch37 likely contributes to the Ub chain trimming activity of the 26S proteasome that shortens a polyUb chain from the distal end of the chain.

Reference: RP10088LQ

APPBP1/UBA3 is the heterodimeric E1 enzyme that conjugates Nedd8 to protein substrates. Nedd8 is conjugated onto the catalytic cysteine residue of UBA3 by formation of a thioester bond in an ATP-dependent reaction. The activated Nedd8 is then passed on to an E2 (Ubc12) to be finally attached to a substrate. Nedd8 is mainly conjugated on Cullins to increase the activity of the Cullin – RING E3 Ub ligases.

Reference: RP10094LQ

This product contains authentic K63-linked isopeotide bonds, synthesized by an enzymatic reaction containing UbE1, GST-E2-25K and fluorescein-Ub (catalog # E1155/E1156). Mainly contain Ub(2-7) 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.

Reference: RP10098LQ

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. A20 downregulates the NF-κB pathway and proinflammatory gene expression in cells such as macrophages. The N-terminal domain of A20 contains the DUB activity.

Reference: RP10099LQ

Ataxin3 is a Machado-Josephine domain-containing deubiquitinating enzyme. Machado–Joseph disease (MJD) is a neurodegenerative disorder caused by polyQ expansion in ataxin-3. Ataxin3 is involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates.

Reference: RP10101LQ

hHR23A and hHR23B are the human homologues of yeast Rad23. Rad23 can interact with the Rpn10 and Rpn1 subunits of the 26S proteasome via its N-terminal Ub-like domain (UBL). Rad23 also contains two Ub-associated domains (UBA), through which it binds polyubiquitinated proteins for proteasomal degradation. In addition, Rad23 can also bind DNA repair factors to regulate nucleotide excision repair from UV damage.

Reference: RP10102LQ

JOSD2 (Josephin-2) is a member of the Machado-Joseph Domain (MJD) deubiquitinating enzyme family. Other family members include: Ataxin-3, Ataxin-3L, and JOSD1. JOSD2 preferentially cleaves K63-linked ubiquitin chains, with much weaker activity toward K48-linked ubiquitin chains in vitro.

Reference: RP10103LQ

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.

Reference: RP10104LQ

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.