Polyclonal Rabbit BAZ2A Antibody
- Known as:
- Polyclonal Rabbit BAZ2A Antibody
- Catalog number:
- KA0391
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit BAZ2A Antibody
Related genes to: Polyclonal Rabbit BAZ2A Antibody
- Gene:
- BAZ2A NIH gene
- Name:
- bromodomain adjacent to zinc finger domain 2A
- Previous symbol:
- -
- Synonyms:
- KIAA0314, TIP5, WALp3
- Chromosome:
- 12q13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-09-06
- Date modifiied:
- 2015-11-13
Related products to: Polyclonal Rabbit BAZ2A Antibody
Related articles to: Polyclonal Rabbit BAZ2A Antibody
- Establishment of correct chromatin configuration in male meiosis is essential for sperm formation and male fertility. However, how chromatin remodeling contributes to meiotic progression in male germ cells is not well understood. Here, we find that the ISWI family ATP-dependent chromatin remodeling factor SMARCA5 (SNF2H) plays a critical role in regulating meiotic prophase progression during spermatogenesis in mice. Male mice with germ cell-specific depletion of SMARCA5 are infertile and unable to form sperm. Conditional knockout of results in meiotic progression failure, with abnormal spermatocytes appearing at the pachytene stage of meiosis I and subsequent accumulation of defects in chromosome synapsis, DNA repair, and transposon control, along with elevated rates of apoptosis. SMARCA5 interacts with known cofactors BAZ1A/ACF and BAZ2A/TIP5, as well as numerous DNA repair and recombination factors, in the testis. Single cell RNA sequencing confirmed failure to achieve a normal transcriptional state in premeiotic spermatogonia and during meiotic prophase, with reduced levels of meiotic gene transcripts and increasingly aberrant transcriptional states at later stages of spermatogenic development. Transcriptional misregulation in meiotic prophase was preceded by a widespread increase in chromatin accessibility in spermatogonia at promoters and repeat elements. Our findings suggest that SMARCA5 restricts chromatin accessibility in male germ cells to guide appropriate chromatin remodeling during meiotic recombination, contrasting with its role promoting chromatin accessibility during female meiosis. - Source: PubMed
Publication date: 2025/07/31
Kataruka ShubhanginiMalla Aushaq BRainsford Shannon RWalters Benjamin WilliamHeuer Rachel AMarshall Kira LLesch Bluma J - There is increasing evidence that the methyl-binding domain (MBD) is a protein-protein interaction motif that can function independently of methylated DNA binding. The MBD proteins found throughout plants and invertebrates duplicated into multiple vertebrate DNA and non-DNA-binding members (MBD1, MBD2, MBD3, MBD4, MBD5, MBD6, MECP2, BAZ2A, BAZ2B, SETDB1, and SETDB2). Although many invertebrate species possess MBD proteins that can bind and recognize DNA methylation, the DNA-binding function has been independently lost multiple times, with only minor alterations to the protein interaction residues. The nucleosome remodeling and deacetylase (NuRD) complex, which interacts with MBD2/3 and is colocalized with MBD1/4 ChIP-Seq, is maintained in species where MBD2/3 cannot bind to DNA. NuRD ChIP-seq data from HepG2 cell line, human induced pluripotent stem cells (iPSCs), and human iPSC-derived liver cells suggest that the NuRD complex is highly localized to nonmethylated CpG-rich housekeeping gene promoter elements, which are essential in organogenesis and maintained within the MBD2/3 non-DNA-binding system. Integration of MBD interaction proteins and NuRD gene expression from >115 million cells of single-cell RNA-seq, along with thousands of bulk tissue profiles, highlights a critical role of MBD3, MECP2, and GATAD2B in brain development and intellectual disability syndromes that is maintained throughout invertebrate neural development and likely involves evolutionary expanded entanglement as the vertebrate MBD proteins expanded. This work suggests that MBD has a largely unexplored role as a critical protein interaction motif that is evolutionarily conserved for regulating enhancers and promoters. The evolution of the methyl-binding domain (MBD) suggests a shared function in gene regulation, from plants to humans, with the conservation of non-DNA-interacting amino acids critical for protein-protein interactions. The MBD-regulated NuRD complex localizes to promoters of housekeeping genes with hypomethylated CpG islands. Expression profiles suggest a shared role for NuRD complex components in neurodevelopment, where the MBD3 and GATAD2B subcomplex of NuRD may be underexplored due to its non-DNA-binding biology. - Source: PubMed
Publication date: 2025/07/25
Bilinovich Stephanie MChhetri Surya BMitchell Jackson TLeighton Gage OJdanov VladislavZieba Jacob KCook Taylor WEngel Krysta LVaughan Robert MBhatti HumzaHeeringa Sadie LWilstermann Amy MVanderweele SophieDas Akansha SSherry Emily CDuncan Stephen AUhl Katie LHinds David CMackiewicz MarkMeadows Sarah KNewberry Kimberly MPartridge E ChristopherCline Sara GShepard C JoySmith D CaseyBradley AntonioVogt DanielCampbell Daniel BPozzo-Miller LucasBupp Caleb PGoodyke Austin JRajasekaran SurenderKnickmeyer Rebecca CBlair BenjieKrawczyk Connie MTriche Timothy JMyers Richard MMendenhall Eric MWilliams David CProkop Jeremy W - Methyl-CpG-binding proteins are crucial epigenetic regulators associated with inborn genetic and neurodevelopmental disorders such as Rett Syndrome, Autism Spectrum Disorder, and Angelman Syndrome, as well as various malignancies, including colorectal, prostate, brain, breast, and endometrial cancers. The proteins that belong to Methyl Binding Domain (MBD) superfamily, have eleven members: SETDB1, SETDB2, MECP2, MBD1-6, BAZ2A, and BAZ2B. This research utilized both sequence-based and structure-based methodologies to ascertain the most detrimental mutation in MBD proteins. The W104C mutation in MECP2 was recognized as the most damaging alteration. Structure prediction and stereochemical evaluation were succeeded by 500 ns all-atom molecular dynamics simulation to evaluate conformational alterations. The docking of wild type and W104C mutant MECP2 onto the targeted gene BDNF, demonstrated variations in docking geometry. Parameters including RMSD and R, indicated structural divergence and decreased DNA-binding efficacy in the mutant, coupled with solvent exposure. W104C disrupts stable DNA binding by MECP2 via inducing conformational instability and impairing hydrogen bond donor-acceptor activity, leading to fluctuating rotation angles and inconsistent binding energies throughout the simulation. Analysis of the interaction profile indicated the loss of critical residues (Y121, R133) and acquisition of new residues (R115, A117 and R168) in the mutant, hence modifying electrostatic equilibrium. Electrostatic surface mapping revealed an almost consistent surface potential within wild type binding cavity but the mutant demonstrated a fluctuating surface charge distribution, indicating less affinity. The severity of deregulation of wild type MECP2 activity by W104C, prompting inborn genetic diseases, Rett syndrome, could further be experimentally tested. - Source: PubMed
Publication date: 2025/06/27
Saha MowmitaPaul IshaniRay SoumyadeepRoy AlankarPyne SoumiliRay Sujay - Bromodomain adjacent to zinc finger 2A and 2B (BAZ2A and BAZ2B) are homologous proteins that serve as regulatory subunits in different initiation switch complexes. Despite their structural similarity, BAZ2A/B seem to play different roles in disease development. However, reported BAZ2A/B inhibitors bind similarly to both homologues. Here we report the discovery of and , first-in-class Proteolysis Targeting Chimeras (PROTACs) degrading BAZ2A/B and BAZ2B, respectively. induces BAZ2A/B degradation with a ≥ 97% (BAZ2A_DC = 180 nM; BAZ2B_DC = 250 nM), while selectively degrades BAZ2B with a DC = 19 nM and ≥ 97%. Degradation by and is almost complete within 2 h, is maintained for at least 3 days, and occurs in PC3 and MM1S cells, demonstrating the potential of these compounds as chemical probes to decipher the distinct biological functions of BAZ2A/B. - Source: PubMed
Publication date: 2025/01/07
Palaferri LeonardoCheng-Sánchez IvánGosselé KatherineZielinska DominikaNevado Cristina - Arsenic exposure has been known to be associated with male reproduction injury. Exploring the antidote of arsenic and ascertaining proper dose of antidote are important for detoxifying the male reproductive toxicity of arsenic. Selenium, which is essential for the male reproduction and spermatogenesis, can alleviate the toxicity of many environmental toxins, such as metals, and fluoride (F). Selenium relieves arsenic-induced reductions in spermatogenesis index and testicular function marker enzymes via promoting the antioxidative ability of rats. Our previous study has found that arsenic can induce male reproductive toxicity by affecting the level of H3K14ac in the testis, so we further investigate whether selenium can antagonize arsenic-induced male reproductive toxicity through the H3K14ac pathway and ascertain the appropriate dose of selenium. The results show that selenium intervention reduces the accumulation of arsenic in rat testis probably attributing to promote the excretion of arsenic from rat, then improves the testis injury induced by arsenic. Selenium intervention enhances sperm quality, testosterone level, and expression of steroidogenic genes by regulating H3K14ac level and expression of its associated enzymes (KAT2A, BAZ2A, and HDAC6), and thus alleviates the male reproductive toxicity of arsenic, and the proper dose of Se for mitigating arsenic male reproductive toxicity is 1 mg/kg. - Source: PubMed
Publication date: 2024/10/01
Yuan DunxuanShen KainaDong XiuxiaYang YanWang BoheFeng XiaojuanLi FangZhao XinruiTian FangzhouQuan JinrouWang JunlingLi Xiangli