SUMO2 Antibody (YA10060)
(Synonyms: SMT3B, SMT3H2, SUMO2, Small ubiquitin-related modifier 2, SUMO-2, HSMT3, SMT3 homolog 2, SUMO-3, Sentrin-2, Ubiquitin-like protein SMT3B, Smt3B)SUMO2 Antibody (YA10060) is a Mouse-derived and non-conjugated IgG2b Monoclonal antibody, targeting to SUMO2.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, ICC/IF
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Reactivity :
Human, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:10-50 |
Product Details
SUMO2 Antibody (YA10060) is a Mouse-derived and non-conjugated IgG2b Monoclonal antibody, targeting to SUMO2.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Rat
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Observed Molecular WeightObserved band size: 17 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: 10 kDa
Purified recombinant protein of human SUMO2.
Endogenous
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, and 0.01% 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
SUMO2 is an Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2, CBX4 or ZNF451. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Plays a role in the regulation of sumoylation status of SETX[1][2][3][4][5][6].
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Subcellular Localization
Nucleus; Nucleus, PML body
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Expression
Tissue_Specificity: Broadly expressed. -
Isoforms & Post-Translational Modification
SUMO2 has 2 isoforms, P61956-1: amino acid length is 95, molecular weight is 10871 Da (predicted); P61956-2: amino acid length is 71, molecular weight is 8111 Da (predicted).
Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4. -
Subunit
Interacts with SAE2 and UBE2I.
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SwissProt ID
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Synonyms
SMT3B, SMT3H2, SUMO2, Small ubiquitin-related modifier 2, SUMO-2, HSMT3, SMT3 homolog 2, SUMO-3, Sentrin-2, Ubiquitin-like protein SMT3B, Smt3B
Documentation
[1]. Cappadocia L, et al. Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase. Nat Struct Mol Biol. 2015 Dec;22(12):968-75. [Content Brief]
[2]. Tatham MH, et al. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol. 2008 May;10(5):538-46. [Content Brief]
[3]. Meulmeester E, et al. Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol Cell. 2008 Jun 6;30(5):610-9. [Content Brief]
[4]. Cong L, et al. SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function. J Biol Chem. 2011 Dec 23;286(51):43793-43808. [Content Brief]
[5]. Kamitani T, et al. Characterization of a second member of the sentrin family of ubiquitin-like proteins. J Biol Chem. 1998 May 1;273(18):11349-53. [Content Brief]
[6]. Richard P, et al. A SUMO-dependent interaction between Senataxin and the exosome, disrupted in the neurodegenerative disease AOA2, targets the exosome to sites of transcription-induced DNA damage. Genes Dev. 2013 Oct 15;27(20):2227-32. [Content Brief]