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Human RBX1 Recombinant Protein (N-His) (HX852022)

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Overview
Catalog No.HX852022
Description
Recombinant Human RBX1 Protein, N-His (HX852022) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% as determined by SDS-PAGE.
Expression systemE. coli
AccessionP62877
Protein lengthMet1-His108
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesE3 ubiquitin-protein ligase RBX1, E3 ubiquitin-protein ligase RBX1, N-terminally processed, E3 ubiquitin-protein transferase RBX1, E3 ubiquitin-protein transferase RBX1, N-terminally processed, EC:2.3.2.27, EC:2.3.2.32, Protein ZYP, RBX1, RING finger protein 75, RING-box protein 1, RNF75, ROC1, Rbx1, Regulator of cullins 1
Background

E3 ubiquitin-protein ligase RBX1 is a ~12 kDa protein. 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 mediates ubiquitination of Pol II subunit POLR2A at 'Lys-1268', a critical TC-NER checkpoint. Core component of the Cul7-RING(FBXW8) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.

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3. Zheng, N. et al. (2002) Nature 416, 703-9. PMID: 11961546
4. Zhang, DD. et al. (2005) The Journal of biological chemistry 280, 30091-9. PMID: 15983046
5. Wang, H. et al. (2006) Molecular cell 22, 383-94. PMID: 16678110
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7. Isobe, T. et al. (2009) The Journal of biological chemistry 284, 27766-27779. PMID: 19679664
8. Duda, DM. et al. (2012) Molecular cell 47, 371-82. PMID: 22748924
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10. Scott, DC. et al. (2016) Cell 166, 1198-1214.e24. PMID: 27565346
Note For research use only
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