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M7318

Sigma-Aldrich

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

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-DMTase, Anti-NY-CO-41

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Specificity

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

Immunogen

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

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Pablo Gómez-Del Arco et al.
Cell metabolism, 23(5), 881-892 (2016-05-12)
Heart muscle maintains blood circulation, while skeletal muscle powers skeletal movement. Despite having similar myofibrilar sarcomeric structures, these striated muscles differentially express specific sarcomere components to meet their distinct contractile requirements. The mechanism responsible is still unclear. We show here
Methyl-CpG binding proteins in the nervous system
Guoping F and Hutnick L
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Epigenetic silencing of serine protease HTRA1 drives polyploidy
Schmidt N, et al.
BMC Cancer, 16(1), 399-399 (2016)
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
Nina Schmidt et al.
BMC cancer, 16, 399-399 (2016-07-09)
Increased numbers and improperly positioned centrosomes, aneuploidy or polyploidy, and chromosomal instability are frequently observed characteristics of cancer cells. While some aspects of these events and the checkpoint mechanisms are well studied, not all players have yet been identified. As

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