MAD2L2 Antibody (YA9683)
(Synonyms: Homolog of REV7 S cerevisiae, hREV7, MAD2 (mitotic arrest deficient yeast, homolog) like 2, MAD2 homolog, MAD2 like 2, MAD2 mitotic arrest deficient like 2, MAD2-like protein 2, MAD2B, Mad2l2, MD2L2_HUMAN)MAD2L2 Antibody (YA9683) is a Rabbit-derived and non-conjugated IgG Recombinant,Monoclonal antibody, targeting to MAD2L2.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, FC, IP
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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IP
IP: Immunoprecipitation
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|---|---|---|---|
| Dilution Ratio | 1:500 | 1:50-200 | 1-2 μg/sample |
Product Details
MAD2L2 Antibody (YA9683) is a Rabbit-derived and non-conjugated IgG Recombinant,Monoclonal antibody, targeting to MAD2L2.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Calculated Molecular Weight Predicted band size: 24 kDa;
Synthetic peptide of Human Mad2L2 (aa 162-211).
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% 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
MAD2L2 is an Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation[1][2][3][4][5][6][7][8].
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Subcellular Localization
Nucleus; Cytoplasm, cytoskeleton, spindle; Cytoplasm; Chromosome
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Expression
Tissue_Specificity: Ubiquitously expressed. -
Isoforms & Post-Translational Modification
MAD2L2 has an amino acid length of 211, molecular weight is 24334 Da.
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Subunit
Homooligomer (Probable).
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SwissProt ID
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Synonyms
Homolog of REV7 S cerevisiae, hREV7, MAD2 (mitotic arrest deficient yeast, homolog) like 2, MAD2 homolog, MAD2 like 2, MAD2 mitotic arrest deficient like 2, MAD2-like protein 2, MAD2B, Mad2l2, MD2L2_HUMAN
Documentation
[1]. Pfleger CM, et al. Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: a novel mechanism for regulating Cdh1. Genes Dev. 2001 Jul 15;15(14):1759-64. [Content Brief]
[2]. Chen J, et al. MAD2B is an inhibitor of the anaphase-promoting complex. Genes Dev. 2001 Jul 15;15(14):1765-70. [Content Brief]
[3]. Zhang L, et al. Rev7/MAD2B links c-Jun N-terminal protein kinase pathway signaling to activation of the transcription factor Elk-1. Mol Cell Biol. 2007 Apr;27(8):2861-9. [Content Brief]
[4]. Iwai H, et al. A bacterial effector targets Mad2L2, an APC inhibitor, to modulate host cell cycling. Cell. 2007 Aug 24;130(4):611-23. [Content Brief]
[5]. Hong CF, et al. MAD2B, a novel TCF4-binding protein, modulates TCF4-mediated epithelial-mesenchymal transdifferentiation. J Biol Chem. 2009 Jul 17;284(29):19613-22. [Content Brief]
[6]. Gupta R, et al. DNA Repair Network Analysis Reveals Shieldin as a Key Regulator of NHEJ and PARP Inhibitor Sensitivity. Cell. 2018 May 3;173(4):972-988.e23. [Content Brief]
[7]. Hara K, et al. Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1. J Biol Chem. 2010 Apr 16;285(16):12299-307. [Content Brief]
[8]. Xie W, et al. Structural insights into the assembly of human translesion polymerase complexes. Protein Cell. 2012 Nov;3(11):864-74. [Content Brief]