Recombinant Human Chromodomain-Helicase-Dna-Binding Protein 4 (CHD4) Protein (His&His)

Name: Recombinant Human Chromodomain-Helicase-Dna-Binding Protein 4 (CHD4) Protein (His&His)
Brand: Beta LifeScience
SKU: BLC-08520P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Chromodomain-Helicase-Dna-Binding Protein 4 (CHD4) Protein (His&His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q14839
Target Symbol	CHD4
Synonyms	ATP dependent helicase CHD4; ATP-dependent helicase CHD4; CHD 4; CHD-4; CHD4; CHD4_HUMAN; Chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4; Mi 2 autoantigen 218 kDa protein; Mi 2b; Mi-2 autoantigen 218 kDa protein; Mi2 beta; Mi2-beta
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His&C-6His
Target Protein Sequence	MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEEDPEEDLSETETPKLKKKKKPKKPRDPKIPKSKRQKKERMLLCRQLGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFKGSSGASVAAAAAAAVAVVES
Expression Range	1-239aa
Protein Length	Partial
Mol. Weight	31.8 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	Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.
Subcellular Location	Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families	SNF2/RAD54 helicase family
Database References	HGNC: 1919 OMIM: 603277 KEGG: hsa:1108 STRING: 9606.ENSP00000349508 UniGene: PMID: 29305962 the N-terminal part of CHD4 interacts with an unstructured A-rich region in promoter and pre-rRNA antisense "), a long noncoding RNA that is transcribed in an orientation antisense to pre-rRNA PMID: 29907651 RNA interference identifies CHD4 as an essential gene in regulating breast cancer growth. PMID: 27779108 Data suggest TCF19 interacts with histone 3 lysine 4 trimethylation through its plant homeodomain finger; TCF19 expression appears to regulate gluconeogenesis in hepatocytes; TCF19 interacts with CHD4 causing NuRD complex recruitment to gene promoters of enzymes involved in gluconeogenesis. (TCF19 = transcription factor 19; CHD4 = chromodomain helicase DNA binding protein 4; NuRD = nucleosome-remodeling-deacetylase) PMID: 29042441 Mutation in CHD4 gene is associated with congenital heart defects. PMID: 27479907 this work identifies CHD4 as an epigenetic coregulator of PAX3-FOXO1 activity, providing rational evidence for CHD4 as a potential therapeutic target in alveolar rhabdomyosarcoma. PMID: 27760049 CHD4 recruits repressive chromatin proteins to sites of DNA damage repair, including DNA methyltransferases where it imposes de novo DNA methylation. At TSGs, CHD4 retention helps maintain DNA hypermethylation-associated transcriptional silencing. PMID: 28486105 this study identifies the Chd4-Tbx3 axis in controlling ESC fate and a role of H2A.Z in maintaining the stability of Chd4 proteins. PMID: 28298436 report provides evidence for the role of CHD4 in human development and expands an increasingly recognized group of Mendelian disorders involving chromatin remodeling and modification PMID: 27616479 complex lacking CHD4 that has HDAC activity can exist as a stable species. The addition of recombinant CHD4 to this nucleosome deacetylase complex reconstitutes a NuRD complex with nucleosome remodeling activity. PMID: 27235397 CHD4 plays a pivotal role in chemoresistance and the maintenance of stemness in liver cancer stem cells and is therefore a good target for the eradication of hepatocellular carcinoma. PMID: 26095183 Acetyltransferase p300 collaborates with chromodomain helicase DNA-binding protein 4 (CHD4) to facilitate DNA double-strand break repair PMID: 26546801 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 these data build on our understanding of how CHD4-NuRD acts to regulate gene expression and participates in the DNA-damage response. PMID: 26565020 CHD4 depletion modulates expression of acute myeloid leukemia cell genes that regulate tumor formation in vivo and colony formation in vitro. PMID: 26265695 Also discovered a novel causative role for CHD4, a helicase involved in the histone deacetylase complex that is associated with poor clinical outcome. PMID: 26296641 D140E SNP was associated with lung cancer, malignant lymphoma and rectum cancer and may interact with smoking habit to increase the risk. PMID: 25407497 CHD4 modulates therapeutic response in BRCA2 mutant cancer cells. PMID: 25737278 Endogenous Mta1/2 forms a complex with chromodomain helicase (Chd)4, histone deacetylases (Hdac)1/2, RbAp46/48, and Mbd3 in rat cerebellum PMID: 24991957 CHD4 and HDAC1 occupy the promoters of several of these hypermethylated tumor suppressor genes and physically and functionally interact to maintain their silencing. PMID: 23708667 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 a three-dimensional structural model describing the overall shape and domain interactions of CHD4 and discuss the relevance of these for regulating the remodeling of chromatin by the NuRD complex. PMID: 22575888 Concerted action of the PHD, chromo and motor domains regulates the human chromatin remodelling ATPase CHD4 PMID: 22749909 Chd4 is necessary to guide proper terminal differentiation of Schwann cells; the nucleosome remodeling and deacetylase (NURD) complex is a requisite factor in timely and stable peripheral chromatin remodeling. PMID: 22302795 CHD4 could bind to two H3 N-terminal tails on the same nucleosome or on two separate nucleosomes simultaneously, presenting exciting implications for the mechanism by which CHD4 and the NuRD complex could direct chromatin remodeling. PMID: 21278251 PU.1 directs Mi2beta to erase an established DNase I-hypersensitive site, in an ATP-dependent reaction subsequent to PU.1 binding to chromatin, whereas ACF will not support erasure PMID: 19158090 the amino-terminal and carboxyl-terminal regions of Mi-2 beta have distinct transcriptional activities and bind to BRG1 and the RET finger protein, forming a multiprotein supercomplex involved in transcriptional regulation. PMID: 14530259 Mi-2beta and RFP, known to be involved in transcriptional repression in the nucleus, co-localize with MCRS1 in the nucleolus and appear to activate the rRNA transcription. PMID: 16186106 The known subunits of the Mi-2/NuRD complex , their connections to signaling networks, and their association with cancer are reviewed. PMID: 17694084 Data show that Mi-2/NuRD constitutes an enzymatic component of a pathway for assembly and maturation of chromatin utilized by rapidly proliferating lymphoid cells for replication of constitutive heterochromatin. PMID: 19296121 The PHD2 finger plays a role in targeting of the CHD4/NuRD complex to chromatin. PMID: 19624289

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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.