产品名称
RBX1 Rabbit Polyclonal Antibody
蛋白名称
E3 ubiquitin-protein ligase RBX1 (EC 6.3.2.-) (Protein ZYP) (RING finger protein 75) (RING-box protein 1) (Rbx1) (Regulator of cullins 1)
存储缓冲液
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% New type preservative N.
Human Gene Link
http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&term=9978
Human Swissprot No.
P62877
Human Swissprot Link
https://www.uniprot.org/uniprot/P62877
Mouse Gene Link
http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&term=56438
Mouse Swissprot No.
P62878
Mouse Swissprot Link
https://www.uniprot.org/uniprotkb/P62878/entry
特异性
This antibody detects endogenous levels of RBX1 at Human, Mouse
运输及保存条件
-15°C to -25°C/1 year(Do not lower than -25°C)
细胞定位
Cytoplasm . Nucleus .
功能
E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair . CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets . The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. As a component of the CSA complex promotes the ubiquitination of ERCC6 resulting in proteasomal degradation. Recruits the E2 ubiquitin-conjugating enzyme CDC34 to the complex and brings it into close proximity to the substrate. Probably also stimulates CDC34 autoubiquitination. May be required for histone H3 and histone H4 ubiquitination in response to ultraviolet and for subsequent DNA repair. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M. Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. In concert with ATF2 and CUL3, promotes degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM.