Methyl-CpG Binding Domain Protein 3, Methyl-CpG-Binding Domain Protein 3, Methyl-CpG-Binding Protein MBD3.
Methyl-CpG-binding domain protein 3 (MBD3), belongs to the MBD family of transcriptional repressors. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 includes a family of nuclear proteins related by the presence of a methyl-CpG binding domain (MBD) in each protein. Nevertheless, not like the other family members, MBD3 is not capable of binding to methylated DNA. MBD3 is a subunit of the NuRD, a multisubunit complex having nucleosome remodeling and histone deacetylase activities. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex.
MBD3 Human Recombinant produced in E. coli is a single polypeptide chain containing 314 amino acids (1-291) and having a molecular mass of 35.2 kDa. MBD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Sterile Filtered colorless solution.
The MBD3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT, 1mM EDTA and 40% glycerol.
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Greater than 85% as determined by SDS-PAGE.
Amino acid sequence
MGSSHHHHHH SSGLVPRGSH MGSMERKRWE CPALPQGWER EEVPRRSGLS AGHRDVFYYS PSGKKFRSKP QLARYLGGSM DLSTFDFRTG KMLMSKMNKS RQRVRYDSSN QVKGKPDLNT ALPVRQTASI FKQPVTKITN HPSNKVKSDP QKAVDQPRQL FWEKKLSGLN AFDIAEELVK TMDLPKGLQG VGPGCTDETL LSAIASALHT STMPITGQLS AAVEKNPGVW LNTTQPLCKA FMVTDEDIRK QEELVQQVRK RLEEALMADM LAHVEELARD GEAPLDKACA EDDDEEDEEE EEEEPDPDPE MEHV.
Safety Data Sheet
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.