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AB271787

重组人 CUL-2 + Elongin-B + Elongin-C + RBX1 + VHL 蛋白 (6x His N-Term, DDDDK N-Term)

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.

查看别名

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.

关键信息

纯度

>80% SDS-PAGE

表达系统

HEK 293 cells

标签

Tag free

应用

FuncS, SDS-PAGE

applications

生物活性

Yes

生物学活性

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.

访问

Q13617

不含动物源

No

不含载体蛋白

No

种属

Human

存储溶液

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

反应性数据

{ "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>" } } }

序列信息

[{"linker":null,"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"}]},{"linker":null,"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"}]},{"linker":null,"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"}]},{"linker":null,"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"}]},{"linker":null,"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"}]}]

性能和储存信息

形式
Liquid
运输条件
Dry Ice
推荐的短期储存条件
-80°C
推荐的长期储存条件
-80°C
储存信息
Avoid freeze / thaw cycle
True

常规信息

功能

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).

序列相似性

Belongs to the cullin family.

翻译后修饰

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).

产品实验方案

靶点信息

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

其他靶点

ELOB,ELOC,RBX1,VHL

文献 (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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