RBX1 Antibody (YA1124)
(Synonyms: ROC1; RNF75; RBX1; E3 ubiquitin-protein ligase RBX1; RING finger protein 75; RING-box protein 1 (Rbx1))RBX1 Antibody (YA1124) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to RBX1.
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Host:
Rabbit
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Isotype:
IgG
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Application:
IHC-P
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Reactivity :
Human
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Formulation:
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide, pH 7.158.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|
| Dilution Ratio | 1:100-1:200 |
Product Details
RBX1 Antibody (YA1124) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to RBX1.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 12 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 12 kDa
A synthesized peptide derived from human ROC1
Endogenous
Affinity Purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide, pH 7.158.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
RBX1 is an 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. Core component of a Cul9-RING ubiquitin ligase complex composed of CUL9 and RBX1, which mediates mono-ubiquitination of p53/TP53. 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. As part of a multisubunit complex composed of elongin BC complex (ELOB and ELOC), elongin A/ELOA, RBX1 and CUL5; polyubiquitinates monoubiquitinated POLR2A[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21].
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Subcellular Localization
Cytoplasm; Nucleus
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Expression
Tissue_specificity:Widely expressed -
Subunit
Component of multiple Cul1-RING E3 ubiquitin-protein ligase complexes commonly known as SCF (SKP1-CUL1-F-box) complexes, consisting of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein (PubMed:10230406, PubMed:11961546, PubMed:20596027, PubMed:22748924, PubMed:38326650, PubMed:39880951).
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SwissProt ID
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Synonyms
ROC1; RNF75; RBX1; E3 ubiquitin-protein ligase RBX1; RING finger protein 75; RING-box protein 1 (Rbx1)
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Research Field
Cell Biology
Documentation
[1]. Ohta T, et al. ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. Mol Cell. 1999 Apr;3(4):535-41. [Content Brief]
[2]. Kamura T, et al. The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2. Genes Dev. 1999 Nov 15;13(22):2928-33. [Content Brief]
[3]. Zheng N, et al. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature. 2002 Apr 18;416(6882):703-9. [Content Brief]
[4]. Zhang DD, et al. Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway. J Biol Chem. 2005 Aug 26;280(34):30091-9. [Content Brief]
[5]. Wang H, et al. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol Cell. 2006 May 5;22(3):383-94. [Content Brief]
[6]. Cen B, et al. Histidine triad nucleotide-binding protein 1 up-regulates cellular levels of p27KIP1 by targeting ScfSKP2 ubiquitin ligase and Src. J Biol Chem. 2009 Feb 20;284(8):5265-76. [Content Brief]
[7]. Isobe T, et al. Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase. J Biol Chem. 2009 Oct 9;284(41):27766-27779. [Content Brief]
[8]. Duda DM, et al. Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase through masking of its E2-binding surface. Mol Cell. 2012 Aug 10;47(3):371-82. [Content Brief]
[9]. Beck J, et al. Ubiquitylation-dependent localization of PLK1 in mitosis. Nat Cell Biol. 2013 Apr;15(4):430-9. [Content Brief]
[10]. Scott DC, et al. Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation. Cell. 2016 Aug 25;166(5):1198-1214.e24. [Content Brief]
[11]. Chen J, et al. KLHL22 activates amino-acid-dependent mTORC1 signalling to promote tumorigenesis and ageing. Nature. 2018 May;557(7706):585-589. [Content Brief]
[12]. van der Weegen Y, et al. The cooperative action of CSB, CSA, and UVSSA target TFIIH to DNA damage-stalled RNA polymerase II. Nat Commun. 2020 Apr 30;11(1):2104. [Content Brief]
[13]. Chagraoui J, et al. UM171 Preserves Epigenetic Marks that Are Reduced in Ex Vivo Culture of Human HSCs via Potentiation of the CLR3-KBTBD4 Complex. Cell Stem Cell. 2021 Jan 7;28(1):48-62.e6. [Content Brief]
[14]. Liwocha J, et al. Mechanism of millisecond Lys48-linked poly-ubiquitin chain formation by cullin-RING ligases. Nat Struct Mol Biol. 2024 Feb;31(2):378-389. [Content Brief]
[15]. Blears D, et al. Redundant pathways for removal of defective RNA polymerase II complexes at a promoter-proximal pause checkpoint. Mol Cell. 2024 Dec 19;84(24):4790-4807.e11. [Content Brief]
[16]. Cacioppo R, et al. CRL3(ARMC5) ubiquitin ligase and Integrator phosphatase form parallel mechanisms to control early stages of RNA Pol II transcription. Mol Cell. 2024 Dec 19;84(24):4808-4823.e13. [Content Brief]
[17]. Kokic G, et al. Structural basis for RNA polymerase II ubiquitylation and inactivation in transcription-coupled repair. Nat Struct Mol Biol. 2024 Mar;31(3):536-547. [Content Brief]
[18]. Kokic G, et al. Structural basis of human transcription-DNA repair coupling. Nature. 2021 Oct;598(7880):368-372. [Content Brief]
[19]. Hopf LVM, et al. Structure of CRL7(FBXW8) reveals coupling with CUL1-RBX1/ROC1 for multi-cullin-RING E3-catalyzed ubiquitin ligation. Nat Struct Mol Biol. 2022 Sep;29(9):854-862. [Content Brief]
[20]. Horn-Ghetko D, et al. Noncanonical assembly, neddylation and chimeric cullin-RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex. Nat Struct Mol Biol. 2024 Jul;31(7):1083-1094. [Content Brief]
[21]. Harreman M, et al. Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proc Natl Acad Sci U S A. 2009 Dec 8;106(49):20705-10. [Content Brief]
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