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M7318

Sigma-Aldrich

Anti-MBD2a,b (RA-18) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-DMTase, Anti-NY-CO-41

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About This Item

Numéro MDL:
MFCD06798469
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

mouse, human

Technique(s)

indirect immunofluorescence: 6-8 μg/mL using NIH3T3 cells
microarray: suitable
western blot: 0.5-1.0 μg/mL using nuclear extracts of HeLa cells

Numéro d'accès UniProt

Q9UBB5

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... MBD2(8932)
mouse ... Mbd2(17191)

Description générale

Anti-MBD2a,b (RA-18) is developed in rabbit using as immunogen a synthetic peptide corresponding human MBD2a conjugated to KLH. MBD2 consists of two isoforms, MBD2a and MBD2b, which are generated from a single gene; MBD2a is a 414 amino acids protein, whereas MBD2b lacks the 152 amino acids N-terminal extension. MBD2a is a component of the MeCP1 corepressor complex, which is a 400-800 kDa complex containing as components MBD2, Mi-2, MTA2, MBD3, and HDAC1/2.
The gene encoding methyl-CpG binding domain protein 2 (MBD2a) is localized on chromosome 18.

Spécificité

The antibody recognizes MBD2a (~45 kDa) and MBD2b (~29 kDa). In immunoblotting, an unidentified band at ~43 kDa may also be detected.

Immunogène

synthetic peptide corresponding to amino acids 294-411 of human MBD2a conjugated to KLH via an N-terminal added lysine residue. This sequence is conserved in MBD2a and MBD2b of human origin, and is not found in MBD3.

Application

Anti-MBD2a,b (RA-18) antibody produced in rabbit has been used:
  • for chromatin immunoprecipitation and western blotting
  • immunofluorescence
  • immunoblotting

Actions biochimiques/physiologiques

MBD2 binds to methylated DNA in vitro or in vivo, suggesting that MBD2 targets the MeCP1 complex to methylated DNA. MBD2a interacts with RNA Helicase A (RHA). MBD2 protein appear to protect against some cancers.
Methyl-CpG binding domain protein 2 (MBD2a) acts as a repressor during transcription.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

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

MiR-520b inhibits the development of glioma by directly targeting MBD2
Cui S, et al.
American Journal of Cancer Research, 7(7), 1528-1528 (2017)
Sitong Cui et al.
American journal of cancer research, 7(7), 1528-1539 (2017-07-27)
MicroRNAs play important roles in the process of cancer, which microRNA-520b (miR-520b) has been reported to play critical roles in tumor progression in many types of cancers. However, its role in glioma remains unknown. In this study, we found that
Jin Young Kim et al.
Molecular cell, 56(6), 738-748 (2014-12-03)
Mammalian circadian rhythms are generated by a negative feedback loop in which PERIOD (PER) proteins accumulate, form a large nuclear complex (PER complex), and bind the transcription factor CLOCK-BMAL1, repressing their own expression. We found that mouse PER complexes include
Ukrae H Cho et al.
eLife, 12 (2023-09-04)
During apoptosis, caspases degrade 8 out of ~30 nucleoporins to irreversibly demolish the nuclear pore complex. However, for poorly understood reasons, caspases are also activated during cell differentiation. Here, we show that sublethal activation of caspases during myogenesis results in
C Stirzaker et al.
Oncogene, 36(10), 1328-1338 (2016-09-07)
Cancer is characterised by DNA hypermethylation and gene silencing of CpG island-associated promoters, including tumour-suppressor genes. The methyl-CpG-binding domain (MBD) family of proteins bind to methylated DNA and can aid in the mediation of gene silencing through interaction with histone
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