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Key Documents

07-2167

Sigma-Aldrich

Anti-SUMO 2/3 Antibody

from rabbit, purified by affinity chromatography

Synonyme(s) :

SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae), Ubiquitin-like protein SMT3B, SMT3 homolog 2, SMT3 (suppressor of mif two 3, yeast) homolog 2, SMT3 suppressor of mif two 3 homolog 2 (yeast), small ubiquitin-related modifier 2, small ubiquitin-lik

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702

Source biologique

rabbit

Niveau de qualité

Type de produit anticorps

primary antibodies

Clone

polyclonal

Produit purifié par

affinity chromatography

Espèces réactives

pig, human, mouse, rat

Réactivité de l'espèce (prédite par homologie)

bovine (based on 100% sequence homology), porcine (based on 100% sequence homology), rhesus macaque (based on 100% sequence homology), opossum (based on 100% sequence homology), chimpanzee (based on 100% sequence homology)

Technique(s)

immunoprecipitation (IP): suitable
western blot: suitable

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... SUMO2(6613)
mouse ... Sumo2(170930)
opossum ... Sumo2(123244757)
rat ... Sumo2(690244)

Description générale

Small ubiquitin-related modifier 2 (UniProt P61956; also known as HSMT3, Sentrin-2, SMT3 homolog 2, Smt3B, SUMO-2, Ubiquitin-like protein SMT3B) and 3 (UniProt P55854; also known as SMT3 homolog 1, Smt3A, SUMO-3, Ubiquitin-like protein SMT3A) are encoded by the SUMO2 (also known as SMT3B, SMT3H2; Gene ID 6613) and SUMO3 (also known as SMT3A, SMT3H1; Gene ID 6612) genes in human. SUMOylation, protein post-translation modification by small ubiquitin-like modifier (SUMO), is a signaling event in many cellular processes. SUMO proteins are translated as immature precursors and subsequently converted to their mature forms through the activity of sentrin/SUMO-specific proteases (SENPs). SUMOylation is a reversible process. SUMO E1 activating enzyme, E2 conjugating enzyme, and E3 ligase mediate SUMOylation of substrate proteins, while SENPs are responsible for the de-SUMOylation. SUMOylation usually occurs at lysine residues in the consensus KxD/E motif, although not all such lysines become SUMOylated and SUMOylation can also occur on lysine residues outside of this motif. SUMO2 and 3 share 97% identity at the amino acid level, while SUMO1 shares only about 50% sequence homology with SUMO-2 and 3. In addition to difference in their target substrates, SUMO2/3 can be SUMOylated and form chains, whereas SUMO1 cannot and may serve as chain terminator. SUMO-2 can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Its covalent attachment to its substrate via an isopeptide bond 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. Although SUMO-2 functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system, however, unlike ubiquitin which targets proteins for degradation, SUMO-2 is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last two amino acids of the carboxy-terminus (aa 94-95; propeptide) have been cleaved off.

Spécificité

This antibody recognizes SUMO 2/3 at the N-terminus.

Immunogène

Epitope: N-terminus
KLH-conjugated linear peptide corresponding to the first 15 amino acids from the N-terminal region of human SUMO-2/3.

Application

Research Category
Signaling
Research Sub Category
Ubiquitin & Ubiquitin Metabolism
This SUMO 2/3 antibody is validated for use in WB & IP for the detection of the SUMO 2/3 protein.
Western Blot (Snap i.d.) Analysis: 5 µg/mL from a previous lot detected SUMO 2/3 on 10 µg of HeLa nuclear extract.
Immunoprecipitation Analysis: A previous was used by an independent laboratory in IP. (Li, T., et al. (2006). The Journal of Biological Chemistry. 281(47):36221-36227.)

Qualité

Evaluated by Western Blot in HeLa nuclear extract.
Western Blot Analysis: 1 µg/mL of this antibody detected SUMO 2/3 on 10 µg of HeLa nuclear extract.

Description de la cible

~12 kDa observed; 10.87 for SUMO-2 and 11.64 for SUMO-3 calculated. Uncharacterized bands may be observed in some lysate(s).

Forme physique

Affinity purified
Purified rabbit polyclonal antibody in buffer containing 0.1M Tris-Glycine, 0.15M NaCl, 0.05% sodium azide, pH7.4 without azide.

Stockage et stabilité

Stable for 1 year at 2-8°C from date of receipt.

Remarque sur l'analyse

Control
HeLa nuclear extract

Autres remarques

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Nan Zhao et al.
Nature structural & molecular biology, 25(9), 885-893 (2018-09-05)
Viral infection perturbs host cells and can be used to uncover regulatory mechanisms controlling cellular responses and susceptibility to infections. Using cell biological, biochemical, and genetic tools, we reveal that influenza A virus (IAV) infection induces global transcriptional defects at

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