SPOP Human
Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.
Description
SPOP Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 394 amino acids (1-374 a.a.) and having a molecular mass of 44.3kDa.
The SPOP is purified by proprietary chromatographic techniques.
Product Specs
Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.
MGSSHHHHHH SSGLVPRGSH MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE
VSVVQDSVNI SGQNTMNMVK VPECRLADEL GGLWENSRFT DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR VEINDVEPEV FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA EAYRSLASAQ CPFLGPPRKR LKQS.
Product Science Overview
Speckle-Type POZ Protein (SPOP) is a protein encoded by the SPOP gene in humans . It is a substrate adaptor of the Cullin3 (CUL3)-based E3 ubiquitin ligase complex, playing a crucial role in the ubiquitination and degradation of various substrate proteins . SPOP is involved in several cellular processes, including transcriptional repression, cell proliferation, migration, and apoptosis .
SPOP contains a typical POZ/BTB domain at the N-terminal and a MATH/TRAF domain at the C-terminal . The POZ/BTB domain binds to the ubiquitin ligase CUL3, while the MATH/TRAF domain binds to specific substrates . This dual-domain structure allows SPOP to act as a substrate adaptor, recognizing and recruiting substrate proteins for ubiquitination and subsequent degradation .
SPOP has been extensively studied for its role in various cancers. It functions as a tumor suppressor in several types of cancer, including prostate cancer and renal cell carcinoma (RCC) . In prostate cancer, SPOP promotes the degradation of bromodomain and extraterminal (BET) proteins, impacting the effectiveness of BET inhibitors . Additionally, SPOP regulates androgen receptor (AR) signaling, with down-expression leading to the activation of AR signaling and exerting oncogenic effects .
In RCC, SPOP is overexpressed in cancer tissues compared to adjacent normal tissues . Overexpression of SPOP inhibits cell proliferation, migration, and invasion while increasing cell apoptosis . These findings suggest that SPOP could be a potential tumor inhibitor in RCC .
SPOP has potential as a biomarker for cancer diagnosis and prognostic stratification . Higher expression of SPOP is associated with earlier clinical stages, better differentiation, and improved overall survival in various cancers . Its role in promoting ubiquitination-mediated degradation of programmed death ligand 1 (PD-L1) also highlights its importance in cancer immune surveillance .
