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AB271787

Recombinant Human CUL-2 + Elongin-B + Elongin-C + RBX1 + VHL protein (6x His N-Term, DDDDK N-Term)

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(1 Publication)

Recombinant Human CUL-2 + Elongin-B + Elongin-C + RBX1 + VHL protein (6x His N-Term, DDDDK N-Term) is a Human Full Length protein, in the 2 to 108 aa range, expressed in HEK 293 cells, with >80%, suitable for SDS-PAGE, FuncS.

View Alternative Names

Cullin-2, CUL-2, CUL2, RNF75, ROC1, RBX1, E3 ubiquitin-protein ligase RBX1, E3 ubiquitin-protein transferase RBX1, Protein ZYP, RING finger protein 75, RING-box protein 1, Regulator of cullins 1, Rbx1, TCEB2, ELOB, Elongin-B, EloB, Elongin 18 kDa subunit, RNA polymerase II transcription factor SIII subunit B, SIII p18, Transcription elongation factor B polypeptide 2, TCEB1, ELOC, Elongin-C, EloC, Elongin 15 kDa subunit, RNA polymerase II transcription factor SIII subunit C, SIII p15, Transcription elongation factor B polypeptide 1, von Hippel-Lindau disease tumor suppressor, Protein G7, pVHL, VHL

2 Images
Functional Studies - Recombinant Human CUL-2 + Elongin-B + Elongin-C + RBX1 + VHL protein (6x His N-Term, DDDDK N-Term) (AB271787)
  • FuncS

Supplier Data

Functional Studies - Recombinant Human CUL-2 + Elongin-B + Elongin-C + RBX1 + VHL protein (6x His N-Term, DDDDK N-Term) (AB271787)

Functional studies of ab271787.

SDS-PAGE - Recombinant Human CUL-2 + Elongin-B + Elongin-C + RBX1 + VHL protein (6x His N-Term, DDDDK N-Term) (AB271787)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human CUL-2 + Elongin-B + Elongin-C + RBX1 + VHL protein (6x His N-Term, DDDDK N-Term) (AB271787)

SDS-PAGE analysis of ab271787.

Key facts

Purity

>80% SDS-PAGE

Expression system

HEK 293 cells

Tags

Tag free

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Assay Conditions: ARV-771-mediated binding of VHL to BET bromodomain was assessed using A-screen technology. Various amounts of VHL were incubated in 10-ul reaction with ARV-771 and GSTBRD3 (BD2) at room temperature for one hour. After this, FLAG-acceptor beads and GSH-donor beads were added followed by detection of A-counts.

Accession

Q13617

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.02% Potassium chloride

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"AAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH","proteinLength":"Full Length","predictedMolecularWeight":"13 kDa","actualMolecularWeight":null,"aminoAcidEnd":108,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P62877","tags":[{"tag":"6x His","terminus":"N-Terminus"}]},{"sequence":"DGEEKTYGGCEGPDAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC","proteinLength":"Fragment","predictedMolecularWeight":"13 kDa","actualMolecularWeight":null,"aminoAcidEnd":112,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q15369","tags":[{"tag":"6x His","terminus":"N-Terminus"}]},{"sequence":"DVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGECGFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ","proteinLength":"Fragment","predictedMolecularWeight":"14 kDa","actualMolecularWeight":null,"aminoAcidEnd":118,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q15370","tags":[{"tag":"DDDDK","terminus":"N-Terminus"}]},{"sequence":"PRRAENWDEAEVGAEEAGVEEYGPEEDGGEESGAEESGPEESGPEELGAEEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD","proteinLength":"Fragment","predictedMolecularWeight":"25 kDa","actualMolecularWeight":null,"aminoAcidEnd":212,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P40337","tags":[{"tag":"DDDDK","terminus":"N-Terminus"}]},{"sequence":"SLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYTETKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQFIKKNKLTEADLQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQAILIRMLLREIKNDRGGEDPNQKVIHGVINSFVHVEQYKKKFPLKFYQEIFESPFLTETGEYYKQEASNLLQESNCSQYMEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHAECHNIIRQEKKNDMANMYVLLRAVSTGLPHMIQELQNHIHDEGLRATSNLTQENMPTLFVESVLEVHGKFVQLINTVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDRLTSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHRMYTDMSVSADLNNKFNNFIKNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEKSVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMNFSSKRTKFKITTSMQKDTPQEMEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKKCIEVLIDKQYIERSQASADEYSYVA","proteinLength":"Fragment","predictedMolecularWeight":"88 kDa","actualMolecularWeight":null,"aminoAcidEnd":745,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q13617","tags":[{"tag":"DDDDK","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
True

Specifications

Form

Liquid

General info

Function

Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins (PubMed : 11384984, PubMed : 26138980, PubMed : 29775578, PubMed : 29779948, PubMed : 38326650). CUL2 serves as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the E2 ubiquitin-conjugating enzyme (PubMed : 10973499, PubMed : 11384984, PubMed : 12609982, PubMed : 24076655, PubMed : 9122164, PubMed : 38326650). The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (PubMed : 12609982, PubMed : 24076655, PubMed : 27565346, PubMed : 38326650). The functional specificity of the ECS complex depends on the substrate recognition component (PubMed : 10973499, PubMed : 26138980, PubMed : 29775578, PubMed : 29779948, PubMed : 9122164, PubMed : 38326650). ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF) (PubMed : 10973499, PubMed : 9122164). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed : 26138980, PubMed : 29775578, PubMed : 29779948). ECS complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (PubMed : 27565346). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity).

Sequence similarities

Belongs to the cullin family.

Post-translational modifications

Neddylated; which enhances the ubiquitination activity of ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes (PubMed:24076655, PubMed:27565346, PubMed:38326650). Neddylation leads to structural rearrangment in the complex that allows interaction between the E2 ubiquitin-conjugating enzyme and the acceptor ubiquitin (PubMed:38326650). CBC(VHL) complex formation seems to promote neddylation. Deneddylated via its interaction with the COP9 signalosome (CSN) complex (By similarity).

Product protocols

Target data

Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins (PubMed : 11384984, PubMed : 26138980, PubMed : 29775578, PubMed : 29779948, PubMed : 38326650). CUL2 serves as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the E2 ubiquitin-conjugating enzyme (PubMed : 10973499, PubMed : 11384984, PubMed : 12609982, PubMed : 24076655, PubMed : 9122164, PubMed : 38326650). The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1 (PubMed : 12609982, PubMed : 24076655, PubMed : 27565346, PubMed : 38326650). The functional specificity of the ECS complex depends on the substrate recognition component (PubMed : 10973499, PubMed : 26138980, PubMed : 29775578, PubMed : 29779948, PubMed : 9122164, PubMed : 38326650). ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF) (PubMed : 10973499, PubMed : 9122164). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed : 26138980, PubMed : 29775578, PubMed : 29779948). ECS complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (PubMed : 27565346). ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity).
See full target information CUL2

Additional targets

ELOB,ELOC,RBX1,VHL

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

The Journal of cell biology 221: PubMed35674692

2022

SARS-CoV-2 ORF10 impairs cilia by enhancing CUL2ZYG11B activity.

Applications

Unspecified application

Species

Unspecified reactive species

Liying Wang,Chao Liu,Bo Yang,Haotian Zhang,Jian Jiao,Ruidan Zhang,Shujun Liu,Sai Xiao,Yinghong Chen,Bo Liu,Yanjie Ma,Xuefeng Duan,Yueshuai Guo,Mengmeng Guo,Bingbing Wu,Xiangdong Wang,Xingxu Huang,Haitao Yang,Yaoting Gui,Min Fang,Luo Zhang,Shuguang Duo,Xuejiang Guo,Wei Li
View all publications

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