Catalog# |
C115 |
Source |
E.coli |
Description |
Recombinant Human E3 Ubiquitin-Protein Ligase CHIP/CHIP is produced with our E. coli expression system. The target protein is expressed with sequence (Met1-Tyr303) of Human CHIP. |
Names |
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 |
Accession # |
Q9UNE7 |
Formulation |
Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2 |
Shipping |
The product is shipped on dry ice/ice packs. |
Storage |
Store at < -20°C, stable for 6 months after receipt.
Please minimize freeze-thaw cycles. |
Purity |
Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. |
Endotoxin |
Less than 0.1 ng/μg (1 IEU/μg). |
Amino Acid Sequence |
MKGKEEKEGGARLGAGGGSPEKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTN RALCYLKMQQHEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLN FGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLSRLIAAERERELEECQRNHEGDEDDSHVRA QQACIEAKHDKYMADMDELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEH LQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY
|
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. |