Hersteller |
Cusabio
|
Kategorie |
|
Typ |
Proteins Recombinant |
Specific against |
other |
Format |
Liquid or Lyophilized powder |
Menge |
10ug |
ArtNr |
CSB-CF822821HU-10 |
eClass 6.1 |
34160400 |
eClass 9.0 |
42020190 |
Lieferbar |
|
Research Topic |
Epigenetics and Nuclear Signaling |
Uniprot ID |
Q8NHY2 |
Gene Names |
RFWD2 |
Organism |
Homo sapiens(Human) |
AA Sequence |
MSGSRQAGSGSAGTSPGSSAASSVTSASSSLSSSP SPPSVAVSAAALVSGGVAQAAGSGGLGGPVRPVLV APAVSGSGGGAVSTGLSRHSCAARPSAGVGGSSSS LGSGSRKRPLLAPLCNGLINSYEDKSNDFVCPICF DMIEEAYMTKCGHSFCYKCIHQSLEDNNRCPKCNY VVDNIDHLYPNFLVNELILKQKQRFEEKRFKLDHS VSSTNGHRWQIFQDWLGTDQDNLDLANVNLMLELL VQKKKQLEAESHAAQLQILMEFLKVARRNKREQLE QIQKELSVLEEDIKRVEEMSGLYSPVSEDSTVPQF EAPSPSHSSIIDSTEYSQPPGFSGSSQTKKQPWYN STLASRRKRLTAHFEDLEQCYFSTRMSRISDDSRT ASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNG SSIVSSIEFDRDCDYFAIAGVTKKIKVYEYDTVIQ DAVDIHYPENEMTCNSKISCISWSSYHKNLLASSD YEGTVILWDGFTGQRSKVYQEHEKRCWSVDFNLMD PKLLASGSDDAKVKLWSTNLDNSVASIEAKANVCC VKFSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVF KGHRKAVSYAKFVSGEEIVSASTDSQLKLWNVGKP YCLRSFKGHINEKNFVGLASNGDYIACGSENNSLY LYYKGLSKTLLTFKFDTVKSVLDKDRKEDDTNEFV SAVCWRALPDGESNVLIAANSQGTIKVLELV |
Expression Region |
1-731aa |
Sequence Info |
Full Length |
Source |
in vitro E.coli expression system |
Tag Info |
N-terminal 6xHis-tagged |
MW |
84.5 kDa |
Alternative Name(s) |
Constitutive photomorphogenesis protein 1 homolog Short name: hCOP1 RING finger and WD repeat domain protein 2 RING finger protein 200 |
Relevance |
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. |
Reference |
"Characterization of human constitutive photomorphogenesis protein 1, a RING finger ubiquitin ligase that interacts with Jun transcription factors and modulates their transcriptional activity."Bianchi E., Denti S., Catena R., Rossetti G., Polo S., Gasparian S., Putignano S., Rogge L., Pardi R.J. Biol. Chem. 278:19682-19690(2003) |
Purity |
Greater than 90% as determined by SDS-PAGE. |
Storage Buffer |
Tris-based buffer, 50% glycerol |
Storage |
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C. |
Notes |
Repeated freezing and thawing is not recommended. Store working aliquots at 4C for up to one week. |
Function |
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif (Probable). |
Subcellular Location |
Nucleus speckle, Cytoplasm |
Protein Families |
COP1 family |
Tissue Specificity |
Ubiquitously expressed at low level. Expressed at higher level in testis, placenta, skeletal muscle and heart. |
Paythway |
p53signalingpathway |
Tag Information |
N-terminal 6xHis-tagged |
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