M7318
Anti-MBD2a,b (RA-18) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
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Synonym(s):
Anti-DMTase, Anti-NY-CO-41
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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.
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Certificates of Analysis (COA)
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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
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
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)
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
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
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