Recombinant Human Methyl-Cpg-Binding Domain Protein 2 (MBD2) Protein (hFc)

Name: Recombinant Human Methyl-Cpg-Binding Domain Protein 2 (MBD2) Protein (hFc)
Brand: Beta LifeScience
SKU: BLC-06476P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Methyl-Cpg-Binding Domain Protein 2 (MBD2) Protein (hFc) is produced by our Yeast expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9UBB5
Target Symbol	MBD2
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	C-hFc
Target Protein Sequence	ESGKRMDCPALPPGWKKEEVIRKSGLSAGKSDVYYFSPSGKKFRSKPQLARYLGNTVDLSSFDFRTGKMMPSKLQKNKQRLRNDPLNQNKGKPDLNTTLPIRQTASIFKQPVTKVTNHPSNKVKSDPQRMNEQPRQLFWEKRLQGLSASDVTEQIIKTMELPKGLQGVGPGSNDETLLSAVASALHTSSAPITGQVSAAVEKNPAVWLNTSQPLCKAFIVTDEDIRKQEERVQQVRKKLEEALMADILSRAADTEEMDIEMDSGDEA
Expression Range	145-411aa
Protein Length	Partial
Mol. Weight	56.3 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binds hemimethylated DNA as well. Recruits histone deacetylases and DNA methyltransferases. Acts as transcriptional repressor and plays a role in gene silencing. Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression. May enhance the activation of some unmethylated cAMP-responsive promoters.
Subcellular Location	Nucleus. Note=Nuclear, in discrete foci. Detected at replication foci in late S phase.
Database References	HGNC: 6917 OMIM: 603547 KEGG: hsa:8932 STRING: 9606.ENSP00000256429 UniGene: PMID: 29535511 knockdown of MBD2 by siRNA attenuated vancomycin-induced apoptosis, caspase activity, and the expression of BAX and cleaved caspase 3. PMID: 29022913 CpG and methylation-dependent DNA binding and dynamics of the MBD2 protein at the single-molecule level have been reported. PMID: 28637186 Results show that MBD2 mediates epigenetic silencing of Htra1. PMID: 27388476 MBD2 has a critical role in 'rewriting' the cancer methylome at specific regulatory regions. PMID: 27593931 MBD2 expression was elevated in HCC tissue, which suggesting MBD2 as a candidate prognostic marker of HCC. PMID: 27315121 downregulation of miR-221 inhibits cell migration and invasion at least partially through targeting MBD2 in the human OSCC cell line UM1. PMID: 26788506 Specifically, methyl-CpG-binding domain protein 2 (MBD2) is revealed to be recruited to DNA damage sites after laser microirradiation, which was mediated through MBD domain and MBD2 C-terminus. PMID: 26827827 MBD2 targets short interspersed nuclear elements, but does not exclude RNA Polymerase III. PMID: 25798578 The dynamics of MBD2 deposition across methylated DNA regions was associated with the oncogenic transformation of human mammary cells. PMID: 26007656 Data suggest that MBD2 binds primarily at highly methylated regions, with a strong preference for CpG islands and highlights that MBD2 binding sites display increased methylation in primary breast cancer tissues as compared to normal mammary cells. PMID: 24927503 Biophysical analyses show that the MBD2IDR is an intrinsically disordered region (IDR). However, despite this inherent disorder, MBD2IDR increases the overall binding affinity of MBD2 for methylated DNA. PMID: 25753662 This study investigates the genetic association between methyl-CpG-binding domain (MBD) gene polymorphisms and schizophrenia. PMID: 24849540 alternatively spliced isoforms support pluripotency of stem cells PMID: 24813856 The methylated-DNA binding protein MBD2 enhances NGFI-A (egr-1)-mediated transcriptional activation of the glucocorticoid receptor. PMID: 25135974 These data point to a potential new approach in targeting the DNA methylation machinery by combination of MBD2 and DNMT inhibitors. PMID: 25178277 MBD2 seems to play a selective role in gene repression depending on the CpG content of the promoter region PMID: 23888954 Methylated DNA binding domain protein 2 (MBD2) coordinately silences gene expression through activation of the microRNA hsa-mir-496 promoter in breast cancer cell line. PMID: 24204564 reduced mRNA expression of MBD2 and MBD3 is implicated in gastric carcinogenesis. PMID: 24338710 global DNA hypomethylation is one of the possible epigenetic variations associated with the complex etiology of TOF and significantly correlates with the aberrant expression of MBD2 mRNA in patients with TOF. PMID: 23820632 MBD2 binds a significant fraction of the hypomethylated genes. PMID: 23955541 Abnormal expression levels of DNA (cytosine-5-)-methyltransferase 1 and MBD2 mRNA may be important causes of the global hypomethylation observed in CD4+T cells in systemic lupus erythematosus. PMID: 23127209 In metastatic colorectal cancer cells, reduced levels of miR-221* and miR-224 increase levels of MBD2, thereby decreasing expression of the metastasis suppressor maspin. PMID: 23770133 MBD3 is enriched at active promoters, whereas MBD2 is bound at methylated promoters and enriched at exon sequences of active genes. PMID: 23361464 These factors lead to a binding affinity hierarchy of p66alpha for the different MBD2 homologues (MBD2 approximately MBD3 > MBD3L1 approximately MBD3L2). PMID: 23239876 repressive functions of MBD2-containing NuRD complexes are dependent on cooperative interactions between the major domains of CHD4 with histones and DNA and on binding of methylated DNA by MBD2 PMID: 23071088 MiR-373 behaves as a direct transcriptional target and negative regulator of MBD2 activity through a feedback loop of CpG island methylation in hilar cholangiocarcinoma PMID: 22876037 The association between MBD2 binding and transcriptional repression weakened as the distance between binding site and TSS increased, suggesting that MBD2 represses transcriptional initiation PMID: 22048253 A two-stage association study identifies methyl-CpG-binding domain protein 2 gene polymorphisms as candidates for breast cancer susceptibility. PMID: 22258532 These results show a role for MBD2 in cancer progression and provide support for the prospect of targeting MBD2 therapeutically in aggressive breast cancers. PMID: 21693597 MBD2 overexpression during gliomagenesis may drive tumor growth by suppressing the antiangiogenic activity of a key tumor BAI1. PMID: 21724586 human epsilon-globin gene is subject to multilayered silencing mediated in part by MBD2 PMID: 21296012 In hilar cholangiocarcinoma, down-expression of miR-373 leads to increase of MBD2, which in turn suppresses the methylation-mediated gene such as RASSF1A. PMID: 21086164 This study demonstrated that patients with SLE had a significantly lower level of DNA methylation than the controls, and that expression of both DNMT1 and MBD2 mRNA was significantly increased in the SLE patients compared with controls. PMID: 21078759 Expression level of MBD2 is significantly lower in endometriotic lesions compared with disease-free controls. PMID: 21316665 miR-373 is a methylation-mediated gene and the implication of MBD2 in methylation-mediated suppression of miR-373 plays an important role in tumourigenesis and development in hilar cholangiocarcinoma. PMID: 21165562 The anti-TNFalpha biological agents do not seem to affect DNA methylation and mRNA expressions of DNMT1 and MBD2 in RA PMID: 20937307 MBD2 and ERalpha drive opposite effects on pS2 expression, which are associated with specific steady state levels of histone H3 acetylation and methylation marks PMID: 20300195 Methyl-CpG binding domain protein 2 represses transcription from hypermethylated pi-class glutathione S-transferase gene promoters in hepatocellular carcinoma cells PMID: 11960994 MBD2 protein activates CpG sites within the promoter region of reporter genes PMID: 12177048 interaction with two highly related p66 proteins PMID: 12183469 interacts with latency-associated nuclear antigen of Kaposi's Sarcoma-associated herpesvirus (KSHV)to tether KSHV to cell chromosomes PMID: 12388720 MBDin relieves MBD2 repression potential and reactivates transcription from methylated promoters PMID: 12588985 Results show that methyl-CpG binding domain protein 1 (MBD1) is expressed in tumor cells, but methyl-CpG binding domain protein 2 (MBD2) and methyl CpG binding protein 2 (MeCP2) are not. PMID: 12646234 MBD2a and RNA helicase A cooperatively enhanced CREB-dependent gene expression. PMID: 12665568 MBD2 has a role in the methylation-mediated inhibition of ribosomal RNA gene expression PMID: 14610093 Antisenses oligoDNA suppresses tumor growth in nude mice, a potential anticaner therapy approach. PMID: 14688029 MBD2 gene expression may be significant factor in tumorigenesis. PMID: 15112265 role of MBD3L1 as a methylation-dependent transcriptional repressor that may interchange with MBD3 as an MBD2-interacting component of the NuRD complex PMID: 15456747 MBD3L2 interacts with MBD3 and components of the NuRD complex and can oppose MBD2-MeCP1-mediated methylation silencing PMID: 15701600

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.