biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
MTA2-276, monoclonal
form
buffered aqueous solution
mol wt
antigen ~73 kDa
species reactivity
mouse, human, bovine, rat, hamster, canine, monkey
technique(s)
immunocytochemistry: suitable, immunoprecipitation (IP): suitable, indirect ELISA: suitable, microarray: suitable, western blot: 1-2 μg/mL using 293T total cell extract
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... MTA2(9219)
mouse ... Mta2(23942)
rat ... Mta2(361724)
General description
Metastasis associated 1 family member 2 (MTA2) is part of the nucleosome remodeling and histone deacetylation complex. This 668 amino acid protein possesses four different domains.
Monoclonal Anti-MTA2 (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells (NS1 cells) and splenocytes from BALB/c mice immunized with a synthetic peptide of human MTA2, conjugated to KLH. Human metastasis-associated protein 2 (MTA2) shares 58% homology to human MTA1 and MTA3 proteins, the C-terminus being more divergent than the N-terminus. MTA2 comprises N-terminal bromo-adjacent homology (BAH) and MTA1 homology 2 (ELM2) domain, SANTand zinc finger (ZnF) domain. It also has the nuclear localization region at C-terminus.
Immunogen
synthetic peptide corresponding to amino acids 626-641of human MTA2, conjugated to KLH.
Application
Monoclonal Anti-MTA2 antibody produced in mouse has been used in:
- enzyme linked immunosorbent assay (ELISA)
- immunoprecipitation
- immunocytochemistry
- Western blotting
- antibody microarray
Biochem/physiol Actions
Human metastasis-associated protein 2 (MTA2) interacts with the histone deacetylase-1 HDAC1 and within the nuclear remodeling and deacetylation complexes ATP-dependent helicase -nucleosome remodelling and histone deacetylation (Mi2/NuRD), suggests that these proteins are involved in transcriptional repression. In the p53 pathway, MTA2/MTA1L1 is better known as protein in the deacetylase complexes p53 target protein in the deacetylase complexes (PID). It inhibits p53-dependent transcriptional activation and its growth arrest and apoptosis functionality. showing that deacetylation and functional interaction by the PID/MTA2/MTA1L1 associated nucleosome remodeling deacetylase (NuRD) complex may represent an important pathway to regulated p53 function.
Metastasis associated 1 family member 2 (MTA2) has been associated with tumor progression and metastasis.
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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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
新产品
此项目有
Epigenetic reactivation of LINE-1 retrotransposon disrupts Nu RD corepressor functions and induces oncogenic transformation in human bronchial epithelial cells
Bojang Jr P and Ramos KS
Molecular Oncology, 12(8), 1342-1357 (2018)
Deacetylation of p53 modulates its effect on cell growth and apoptosis
Luo J, et al.
Nature, 408(6810), 377-377 (2000)
Validation of a novel shotgun proteomic workflow for the discovery of protein-protein interactions: Focus on ZNF521
Bernaudo F, et al.
Journal of Proteome Research, 14(4), 1888-1899 (2015)
Overexpression of MTA1 inhibits the metastatic ability of ZR-75-30 cells in vitro by promoting MTA2 degradation
Zhang L, et al.
Cell communication and signaling : CCS, 17(1), 4-4 (2019)
Kyle R Covington et al.
Cancer metastasis reviews, 33(4), 921-928 (2014-11-15)
Metastasis is the ultimate cause of death for most cancer patients. While many mechanisms have been delineated for regulation of growth and tumor initiation of the primary tumor, very little is known about the process of metastasis. Metastasis requires dynamic
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