Category: Proteins & Peptides

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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.

Reference: RP10105LQ

NEDD4 (neural precursor cell expressed developmentally down-regulated protein 4) is a widely expressed HECT domain-containing E3 ubiquitin ligase. NEDD4 ubiquitinates a few membrane proteins, including IGF-1R and PTEN, by which it regulates signal transduction.

Reference: RP10106LQ

NF-κB essential modulator (NEMO) is a regulatory subunit within IκB kinase (IKK). IKK is also composed of two unrelated catalytic subunits called IKKα and IKKβ. NEMO is additionally referred to as IKKγ, IKKAP1, or FIP-3. IKK is responsible for activating the transcription factor, NF-κB, which is involved in immune response. NEMO prefers to bind K63-linked or linear polyubiquitin chains.

Reference: RP10108LQ

GST was fused on the N-terminus of the linear polyubiquitin chain binding domain of NEMO en-compassing amino acids 183-339. This fusion protein can be used for in vitro GST pulldown as-says and for enrichment of cellular proteins conjugated with linear polyubiquitin chains in whole cell or tissue lysates. GST-NEMO (UBAN) can be precipitated using glutathione resin. After washing, GST-NEMO (UBAN)and its bound proteins can be eluted by a buffer containing 10 mM glutathione.

Reference: RP10109LQ

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. OTUB1 is a member of the ovarian tumor domain family. It is recognized as a K48 ubiquitin chain-specific DUB and can inhibit E2 enzymes, especially Ubc13 (also known as Ube2N), which is known to synthesize K63-linked ubiquitin chains. OTUB1 may also deubiquitinate TRAF3 and -6. This would negatively regulate virus-triggered type I IFN induction.

Reference: RP10111LQ

RING-finger 4 (RNF4), also known as Snurf, is an E3 ubiquitin ligase. RNF4 is composed of four SUMO interaction motifs (SIMs) at the N-terminal and a RING domain at the C-terminal. The SIM domains prefer binding polySUMO chains; RNF4 functions to ubiquitinate polysumolyated proteins including promyelocytic leukaemia (PML), which target them for proteasomal degradation.

Reference: RP10112LQ

S5a is one of the integral Ub receptors of the 26S proteasome. It’s N-terminal vWA domain interacts with Rpn9 and Rpn10 on the 26S proteasome. The C-terminal domain of S5a contains two Ub-interacting motifs (UIMs) that bind Ub and Ub chains. S5a prefers to bind polyUb chains; it also binds proteins containing a Ub-like domain. It may directly recognize ubiquitinated proteins or coordinate with other Ub receptors to target substrates for proteasomal degradation.

Reference: RP10115LQ

SUMO (small Ub-related modifier) is a Ub-like protein. Three types of SUMO are most commonly studied, SUMO 1, SUMO 2, and SUMO 3. SUMO 2 and SUMO 3 are almost identical isoforms and thus share many functions. Like Ub, SUMO can be conjugated to its target proteins as a polymeric chain. However, SUMO 1 forms chains inefficiently as compared to SUMO 2 and SUMO 3. SUMO is conjugated to target proteins by the E1 (SAE1/SAE2), E2 (Ube2I or Ubc9), E3 (RanBP2/Nup358, amongst others). Protein sumoylation is involved in many cellular processes including gene transcription.

Reference: RP10117LQ

SUMO (small Ub-related modifier) is a Ub-like protein. Three types of SUMO are most commonly studied, SUMO 1, SUMO 2, and SUMO 3. SUMO 2 and SUMO 3 are almost identical isoforms and thus share many functions. Like Ub, SUMO can be conjugated to its target proteins as a polymeric chain. However, SUMO 1 forms chains inefficiently as compared to SUMO 2 and SUMO 3. SUMO is conjugated to target proteins by the E1 (SAE1/SAE2), E2 (Ube2I or Ubc9), E3 (RanBP2/Nup358, amongst others). Protein sumoylation is involved in many cellular processes including gene transcription.

Reference: RP10118LQ

GST was fused on the N-terminus of the lysine 63 polyubiquitin chain binding domain of TAB2 encompassing amino acids 627-693. This fusion protein can be used for in vitro GST pulldown assays and for enrichment of cellular proteins conjugated with lysine 63 polyubiquitin chains in whole cell or tissue lysates. GST-TAB2 (NZF) can be precipitated using glutathione resin. After washing, GST-TAB2 (NZF) and its bound proteins can be eluted by a buffer containing 10 mM glutathione.

Reference: RP10119LQ

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 apoptotic signaling pathways. The recombinant GST-TNFalpha protein consists of a N-terminal GT tag with the C-terminal extracellular domain (amino acids 77-233) of full length TNFalpha. It can be used for pulldown assays. It binds TNFR1 and TNFR2 to induce downstream signaling pathways, but often requires higher concentrations than TNFalpha (catalog # U1120).