Description
Recombinant Human STUB1 Protein | PKSH032367 | Gentaur US, UK & Europe Disrtribition
Synonyms: E3 Ubiquitin-Protein Ligase CHIP; Antigen NY-CO-7; CLL-Associated Antigen KW-8; Carboxy Terminus of Hsp70-Interacting Protein; STIP1 Homology and U Box-Containing Protein 1; STUB1; CHIP
Active Protein: N/A
Activity: Recombinant Human E3 Ubiquitin-Protein Ligase CHIP is produced by our E.coli expression system and the target gene encoding Met1-Tyr303 is expressed.
Protein Construction: Recombinant Human E3 Ubiquitin-Protein Ligase CHIP is produced by our E.coli expression system and the target gene encoding Met1-Tyr303 is expressed.
Fusion Tag:
Species: Human
Expressed Host: E.coli
Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.
Purity: > 90 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
Molecular Mass: 34.9 kDa
Formulation: Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.
Reconstitution: Not Applicable
Background: E3 Ubiquitin-Protein Ligase CHIP is a cytoplasmic protein. CHIP is highly expressed in skeletal muscle, heart, pancreas, brain and placenta. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain; lead to in client substrate ubiquitylation and degradation by the proteasome. CHIP targets misfolded chaperone substrates towards proteasomal degradation. CHIP mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. CHIP plays a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. It also may regulate the receptor stability and activity through proteasomal degradation.
Research Area: Signal Transduction, epigenetics and nuclear signal,
