ERCC8 Antibody (YA9761)
(Synonyms: ERCC8, ERCC Excision Repair 8, CSA Ubiquitin Ligase Complex Subunit, CSA, CKN1, Excision Repair Cross-Complementing Rodent Repair Deficiency, Complementation Group 8, Excision Repair Cross-Complementation Group 8, Cockayne Syndrome WD Repeat Protein CSA, DNA Excision Repair Protein ERCC-8, Cockayne Syndrome WD-Repeat Protein CSA, Cockayne Syndrome 1 (Classical), UVSS2)ERCC8 Antibody (YA9761) is a Rabbit-derived and non-conjugated IgG Monoclonal, Recombinant antibody, targeting to ERCC8.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, FC, ICC/IF
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Reactivity :
Human
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Formulation:
Supplied in PBS (pH 7.4) containing 50% glycerol, 0.05% BSA and 0.02% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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FC
FC: Flow Cytometry
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|---|
| Dilution Ratio | 1:1000-5000 | 1:200-2000 | 1:100-1000 |
Product Details
ERCC8 Antibody (YA9761) is a Rabbit-derived and non-conjugated IgG Monoclonal, Recombinant antibody, targeting to ERCC8.
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Host Rabbit
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 44 kDaNote: 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: 44 kDa
A synthesized peptide derived from human ERCC8
affinity purified.
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4) containing 50% glycerol, 0.05% BSA and 0.02% sodium azide.
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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
ERCC8 is a Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair (TC-NER), a process during which RNA polymerase II-blocking lesions are rapidly removed from the transcribed strand of active genes. Following recruitment to lesion-stalled RNA polymerase II (Pol II), the CSA complex mediates ubiquitination of Pol II subunit POLR2A/RPB1 at 'Lys-1268', a critical TC-NER checkpoint, governing RNA Pol II stability and initiating DNA damage excision by TFIIH recruitment. The CSA complex also promotes the ubiquitination and subsequent proteasomal degradation of ERCC6/CSB in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. Also plays a role in DNA double-strand breaks (DSSBs) repair by non-homologous end joining (NHEJ)[1][2][3][4][5][6][7][8][9][10].
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Subcellular Localization
Nucleus; Chromosome; Nucleus matrix
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Isoforms & Post-Translational Modification
ERCC8 has 2 isoforms, Q13216-1: amino acid length is 396, molecular weight is 44055 Da (predicted); Q13216-2: amino acid length is 205, molecular weight is 23182 Da (predicted).
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Subunit
Part of the CSA complex (also named DCX(ERCC8) complex), a DCX E3 ubiquitin-protein ligase complex containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II.
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SwissProt ID
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Synonyms
ERCC8, ERCC Excision Repair 8, CSA Ubiquitin Ligase Complex Subunit, CSA, CKN1, Excision Repair Cross-Complementing Rodent Repair Deficiency, Complementation Group 8, Excision Repair Cross-Complementation Group 8, Cockayne Syndrome WD Repeat Protein CSA, DNA Excision Repair Protein ERCC-8, Cockayne Syndrome WD-Repeat Protein CSA, Cockayne Syndrome 1 (Classical), UVSS2
Documentation
References
[1]. Groisman R, et al. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell. 2003 May 2;113(3):357-67. [Content Brief]
[2]. Groisman R, et al. CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome. Genes Dev. 2006 Jun 1;20(11):1429-34. [Content Brief]
[3]. Angers S, et al. Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. Nature. 2006 Oct 5;443(7111):590-3. [Content Brief]
[4]. Nakazawa Y, et al. Ubiquitination of DNA Damage-Stalled RNAPII Promotes Transcription-Coupled Repair. Cell. 2020 Mar 19;180(6):1228-1244.e24. [Content Brief]
[5]. Kokic G, et al. Structural basis of human transcription-DNA repair coupling. Nature. 2021 Oct;598(7880):368-372. [Content Brief]
[6]. 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]
[7]. Carnie CJ, et al. Transcription-coupled repair of DNA-protein cross-links depends on CSA and CSB. Nat Cell Biol. 2024 May;26(5):797-810. [Content Brief]
[8]. van Sluis M, et al. Transcription-coupled DNA-protein crosslink repair by CSB and CRL4(CSA)-mediated degradation. Nat Cell Biol. 2024 May;26(5):770-783. [Content Brief]
[9]. 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]
[10]. Pascucci B, et al. CSA and CSB play a role in the response to DNA breaks. Oncotarget. 2018 Feb 20;9(14):11581-11591. [Content Brief]