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Polyclonal Antibody Atp-Dependent Protein Binding

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: The UAP56 gene is found in the central MHC region and encodes a member of the DEAD-box family of RNA helicases (1). Also known as DDX39B and BAT1, UAP56 functions as an ATP-dependent splicing factor and RNA helicase in the evolutionary conserved transcription/export (TREX) complex. The TREX complex is recruited to sites of active transcription, where it travels along the length of the gene with RNA polymerase II and exports resulting mRNAs to the cytoplasm (2-8). Both UAP56 and its paralog DDX39A are hijacked by various viral replication machineries to enable viral reproduction and mRNA export (9-11). UAP56 and DDX39A have also been implicated in promoting the AR-V7 splice variant in advanced prostate cancers (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The process of SUMO conjugation to target proteins is similar to the molecular chain of events observed with ubiquitin (1). SUMO is conjugated to target proteins through the coordinated action of the cellular SUMO conjugation machinery, which consists of the E1, E2, and E3 enzymes (2). The canonical SUMO E1 activating enzyme is a heterodimer consisting of Ubiquitin-like 1-activating enzyme E1A (UBLE1A, SAE1) and UBLE1B (SAE2, UBA2) subunits. Mature SUMO is activated by E1 in an ATP-dependent reaction that generates adenylated SUMO, which functions as a high-energy intermediate in the formation of a thioester linkage between SUMO and Cys173 of SAE2 (3,4). SUMO is subsequently transferred from SAE2 to the SUMO E2 conjugating enzyme UBE2I (5). Research studies indicate that UBLE1A (SAE1) is a nuclear protein and c-Myc transcriptional target whose expression is required for Myc-driven tumorigenesis (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunoprecipitation, Western Blotting

Background: Myosin Va is a molecular motor protein involved in the transport of organelles, vesicles and other cellular cargo along actin filaments (reviewed in 1). The molecule consists of two identical heavy chains, which dimerize via helical domains in a coiled coil structure. The amino-terminal motor domains of the heavy chains contain both the ATPase and the actin-binding activities of myosin Va. The globular tail domains act in a regulatory capacity, binding the myosin Va cargo (2) or inhibiting motor activity by binding the head domains and preventing ATP consumption (3). Mutation of the murine dilute gene, which encodes myosin Va, causes defects in coat pigmentation as well as severe neurological defects (4). In melanocytes, the coiled coil structure of myosin Va is important in regulating the trafficking of melanosomes in conjunction with melanophilin and Rab27a (5). Myosin Va regulates trafficking and exocytosis of secretory granules in neuroendocrine cells (reviewed in 6) as well as RNA transport and distribution (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: DDX5 (DEAD box polypeptide 5), also known as p68, was first identified as a 68 kDa nuclear protein with similarity to translation initiation factor eIF-4A (1). DDX5 is a member of the DEAD box family of putative RNA helicases, defined by the presence of a conserved DEAD (Asp-Glu-Ala-Asp) motif that appears to function primarily in the regulation of RNA secondary structure. DDX5 exhibits ATP-dependent RNA helicase activity (2) and has been identified as a critical subunit of the DROSHA complex that regulates miRNA and rRNA processing (3,4). DDX may also regulate mRNA splicing (5) and has been shown to interact with HDAC1, where it can regulate promoter-specific transcription (6). DDX5 interacts with a diverse group of proteins, including Runx2, p53, Smad3, CBP, and p300 (7-10), suggesting an important role for DDX5 in a multitude of developmental processes. Notably, DDX5 may be involved in growth factor-induced epithelial mesechymal transition (EMT). Phosphorylation of DDX5 at Tyr593 following PDGF stimulation was shown to displace Axin from β-catenin; this prevented phosphorylation of β-catenin by GSK-3β, leading to Wnt-independent nuclear translocation of β-catenin (11) and increased transcription of c-Myc, cyclin D1, and Snai1 (12,13).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: FKBP4 (also known as FKBP52) is a member of the immunophilin protein family. FKBP4 does not demonstrate appreciable immunosuppressant activity typical of this family, despite its ability to bind the immunosuppressants FK506 and rapamycin (1,2). While FKBP4 plays an important role in immunoregulatory gene expression in B and T lymphocytes, its role in regulating steroid hormone receptor signaling and cytoskeletal dynamics is garnering significant interest. FKBP4 contains two petidyl-prolyl cis-trans isomerase (PPIase) domains, the first of which is implicated in steroid receptor signaling while the second interacts with tubulin and other cytoskeletal components. The maturation of cytoplasmic steroid hormone receptors into a functional conformation requires multiple chaperone and co-chaperone components, including HSP90, p23, and FKBP4 (3,4). FKBP4 interacts with HSP90 to facilitate the folding of androgen, glucocorticoid, and progesterone steroid hormone receptors. Indeed, the functionality of these receptors is impaired in the absence of FKBP4, and research studies have found that null mice demonstrate signs of androgen insensitivity syndrome (5). In addition, FKBP4, which is expressed at high levels in the brain, interacts with hyperphosphorylated Tau and antagonizes Tau's ability to promote microtubule polymerization (6). FKBP4 can also suppress amyloid β toxicity in Drosophila by processing APP (Alzheimer's Amyloid Precursor Protein) to unfold aggregates (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: YTH domain-containing protein 1 (YTHDC1) and YTH domain-containing protein 2 (YTHDC2) both belong to a family of proteins that bind to RNA. YTHDC1 and YTHDC2 both recognize and bind to N6-methyladenosine(m6A)-containing RNAs; binding is mediated through the YTH domains (1-3). m6A is a modification that is present at internal sites of mRNAs and some non-coding RNAs and plays a role in regulating mRNA splicing, processing, and stability. YTHDC1, also known as splicing factor YT521, regulates alternative splicing by functioning as a key regulator of exon-inclusion or exon-skipping. YTHDC1 promotes exon-inclusion by recruiting pre-mRNA splicing factor SRSF3 to regions containing m6A, while repressing exon-skipping by blocking SRSF10 binding to these same regions (2). Increased expression of YTHDC1 promotes malignant endometrial carcinoma (EC) through alternative splicing of vascular endothelial growth factor A (VEGF-A), resulting in an increase in VEGF-165 isoform and increased EC cell invasion (4). YTHDC2 functions to enhance the translation efficiency of target mRNAs and may play a role in spermatogenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The minichromosome maintenance (MCM) 2-7 proteins are a family of six related proteins required for initiation and elongation of DNA replication. MCM2-7 bind together to form the heterohexameric MCM complex that is thought to act as a replicative helicase at the DNA replication fork (1-5). This complex is a key component of the pre-replication complex (pre-RC) (reviewed in 1). Cdc6 and CDT1 recruit the MCM complex to the origin recognition complex (ORC) during late mitosis/early G1 phase forming the pre-RC and licensing the DNA for replication (reviewed in 2). Licensing of the chromatin permits the DNA to replicate only once per cell cycle, thereby helping to ensure that genetic alterations and malignant cell growth do not occur (reviewed in 3). Phosphorylation of the MCM2, MCM3, MCM4, and MCM6 subunits appears to regulate MCM complex activity and the initiation of DNA synthesis (6-8). CDK1 phosphorylation of MCM3 at Ser112 during late mitosis/early G1 phase has been shown to initiate complex formation and chromatin loading in vitro (8). Phosphorylation of MCM2 at serine 139 by cdc7/dbf4 coincides with the initiation of DNA replication (9). MCM proteins are removed during DNA replication, causing chromatin to become unlicensed through inhibition of pre-RC reformation. Studies have shown that the MCM complex is involved in checkpoint control by protecting the structure of the replication fork and assisting in restarting replication by recruiting checkpoint proteins after arrest (reviewed in 3,10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: PNK (polynucleotide kinase) is a DNA repair enzyme that participates in single strand break repair and non-homologous end rejoining (NHEJ) for double strand breaks. PNK possesses a 5'-DNA kinase activity and a 3'-DNA phosphatase activity (1,2). It has three domains, a C-terminal kinase domain, a central phosphatase domain, and an N-terminal forkhead associated (FHA) domain that is responsible for protein-protein interactions. Reduction in expression of PNK by RNAi sensitizes cells to ionizing radiation and topoisomerase I inhibitors (3)

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Nonmuscle myosin is an actin-based motor protein essential to cell motility, cell division, migration, adhesion, and polarity. The holoenzyme consists of two identical heavy chains and two sets of light chains. The light chains (MLCs) regulate myosin II activity and stability. The heavy chains (NMHCs) are encoded by three genes, MYH9, MYH10, and MYH14, which generate three different nonmuscle myosin II isoforms, IIa, IIb, and IIc, respectively (reviewed in 1). While all three isoforms perform the same enzymatic tasks, binding to and contracting actin filaments coupled to ATP hydrolysis, their cellular functions do not appear to be redundant and they have different subcellular distributions (2-5). The carboxy-terminal tail domain of myosin II is important in isoform-specific subcellular localization (6). Research studies have shown that phosphorylation of myosin IIa at Ser1943 contributes to the regulation of breast cancer cell migration (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: SMARCA1 (SNF2L) is one of the two orthologs of the ISWI (imitation switch) ATPases encoded by the mammalian genome (1). The ISWI chromatin remodeling complexes were first identified in Drosophila and have been shown to remodel and alter nucleosome spacing in vitro (2). SMARCA1 is the catalytic subunit of the nucleosome remodeling factor (NURF) and CECR2-containing remodeling factor (CERF) complexes (3-5). The NURF complex plays an important role in neuronal physiology by promoting neurite outgrowth and regulation of Engrailed homeotic genes that are involved in neuronal development in the mid-hindbrain (3). NURF is also thought to be involved in the maturation of T cells from thymocytes by regulating chromatin structure and expression of genes important for T cell development (6). The largest subunit of the NURF complex, BPTF, is required for proper development of mesoderm, endoderm, and ectoderm tissue lineages, suggesting a role for SMARCA1 in the development of the germ layers in mouse embryo (7). Disruption of the CERF complex by deletion of CECR2, an interacting partner of SMARCA1, is associated with the neural tube defect exencephaly, linking the CERF complex with regulation of neurulation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The minichromosome maintenance (MCM) 2-7 proteins are a family of six related proteins required for initiation and elongation of DNA replication. MCM2-7 bind together to form the heterohexameric MCM complex that is thought to act as a replicative helicase at the DNA replication fork (1-5). This complex is a key component of the pre-replication complex (pre-RC) (reviewed in 1). Cdc6 and CDT1 recruit the MCM complex to the origin recognition complex (ORC) during late mitosis/early G1 phase forming the pre-RC and licensing the DNA for replication (reviewed in 2). Licensing of the chromatin permits the DNA to replicate only once per cell cycle, thereby helping to ensure that genetic alterations and malignant cell growth do not occur (reviewed in 3). Phosphorylation of the MCM2, MCM3, MCM4, and MCM6 subunits appears to regulate MCM complex activity and the initiation of DNA synthesis (6-8). CDK1 phosphorylation of MCM3 at Ser112 during late mitosis/early G1 phase has been shown to initiate complex formation and chromatin loading in vitro (8). Phosphorylation of MCM2 at serine 139 by cdc7/dbf4 coincides with the initiation of DNA replication (9). MCM proteins are removed during DNA replication, causing chromatin to become unlicensed through inhibition of pre-RC reformation. Studies have shown that the MCM complex is involved in checkpoint control by protecting the structure of the replication fork and assisting in restarting replication by recruiting checkpoint proteins after arrest (reviewed in 3,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Western Blotting

Background: DDX6, also known as RCK and p54, was identified as a proto-oncogene product and is a member of the ATP-dependent DEAD box helicase family (1,2). This protein interacts with translation initiation factor eIF4E in the cytoplasmic P-bodies (3) and represses mRNA translation (4). DDX6 is a component of the miRNA induced silencing complex (miRISC) and interacts with Argonaute 1 (Ago1) and Argonaute 2 (Ago2) proteins in vitro and in vivo (5), functioning in miRNA-mediated translational repression (5). Depletion of DDX6 leads to the disruption of cytoplasmic P-bodies indicating that it is required for P-body formation (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Western Blotting

Background: The Ca2+/calmodulin-dependent kinase (CaMK) family, which is activated in response to elevation of intracellular Ca2+, includes CaMKI, CaMKII, CaMKIV and CaMK-kinases (CaMKKs) (1,2). CaMKI is a downstream substrate of CaMKK and has 4 isoforms: CaMKI-α, CaMKI-β, CaMKI-γ and CaMKI-δ. CaMKI is present in most cell types and may be involved in cellular functions including transcription, cytoskeletal organization, axonal growth cone motility and long-term potentiation in neurons (3-6). CaMKII is also ubiquitously expressed in most cell types. While muscular CaMKII has been linked to activation of mitochondrial biogenesis in muscle hypertrophy response, neuronal CaMKII regulates important neuronal functions, including neurotransmitter synthesis, neurotransmitter release, modulation of ion channel activity, cellular transport, cell morphology and neurite extension, synaptic plasticity, learning and memory and gene expression (7). Like CaMKI, CaMKIV is also a substrate of CaMKKs and is primarily restricted to the nucleus of neurons. CaMKIV regulates gene transcription in neurons through phosphorylation of transcription factors such as CREB and is required for fear memory (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Chromodomain-helicase-DNA-binding domain (CHD) proteins have been identified in a variety of organisms (1,2). This family of proteins, which consists of nine members, has been divided into three separate subfamilies: subfamily I (CHD1 and CHD2), subfamily II (CHD3 and CHD4), and subfamily III (CHD5, CHD6, CHD7, CHD8, and CHD9). All of the CHD proteins contain two tandem N-terminal chromodomains, a SWI/SNF-related ATPase domain, and a C-terminal DNA binding domain (1,2). The chromodomains facilitate binding to methylated lysine residues of histone proteins and confer interactions with specific regions of chromatin. The SWI/SNF-related ATPase domain utilizes the energy from ATP hydrolysis to modify chromatin structure. CHD1 is a euchromatic protein that associates with the promoters of active genes, and is required for the maintenance of open chromatin and pluripotency in embryonic stem cells (3-6). The two chromodomains of CHD1 facilitate its recruitment to active genes by binding to methyl-lysine 4 of histone H3, a mark associated with transcriptional activation (4-6). Yeast CHD1 is a component of the SAGA and SLIK histone acetyltransferase complexes, and is believed to link histone methylation with histone acetylation during transcriptional activation (6). The CHD2 protein is not well characterized; however, mouse knockout studies suggest important functions in development and tumor suppression. Homozygous CHD2 knockout mice exhibit delayed growth and perinatal lethality (7). Heterozygous knockout mice show increased mortality and gross organ abnormalities, in addition to increased extramedullary hematopoiesis and susceptibility to lymphomas (7,8). CHD2 mutant cells are defective in hematopoietic stem cell differentiation and exhibit aberrant DNA damage responses (8).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Chromodomain-helicase-DNA-binding domain (CHD) proteins have been identified in a variety of organisms (1,2). This family of nine proteins is divided into three separate subfamilies: subfamily I (CHD1 and CHD2), subfamily II (CHD3 and CHD4), and subfamily III (CHD5, CHD6, CHD7, CHD8, and CHD9). All CHD proteins contain two tandem amino-terminal chromodomains, a SWI/SNF-related ATPase domain, and a carboxy-terminal DNA-binding domain (1,2). The chromodomains facilitate binding to methylated lysine residues of histone proteins and confer interactions with specific regions of chromatin. The SWI/SNF-related ATPase domain utilizes energy from ATP hydrolysis to modify chromatin structure. CHD proteins are often found in large, multiprotein complexes with their transcriptional activation or repression activity governed by other proteins within the complex. CHD3 (also known as Mi2-α) and CHD4 (also known as Mi2-β) are central components of the nucleosome remodeling and histone deacetylase (NuRD) transcriptional repressor complex, which also contains HDAC1, HDAC2, RBAP48, RBAP46, MTA1, MTA2, MTA3, and MBD3 (3-8). Both CHD3 and CHD4 contain two plant homeodomain (PHD) zinc finger domains that bind directly to HDAC1 and HDAC2.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: ATP-dependent chromatin remodeling complexes play an essential role in the regulation of various nuclear processes, such as gene expression, DNA replication, and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits with a single molecule of the ATPase catalytic subunit BRM or BRG1, but not both. The activities of these two subunits drive the disruption of histone-DNA contacts that lead to changes in accessibility of crucial regulatory elements within chromatin (2-5). The BRM/BRG1 containing SWI/SNF complexes are recruited to target promoters by transcription factors, such as nuclear receptors, p53, RB, and BRCA1 to regulate gene activation, cell growth, the cell cycle, and differentiation processes (1,6-9). BRM and BRG1 are also considered to be tumor suppressors and their expression levels are severely reduced in several cancer cell lines (10-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Upf1 was identified as an active component in nonsense-mediated decay (NMD), an mRNA surveillance mechanism in eukaryotic cells that degrades mRNAs containing premature termination codons (1). Upf1 was found to be an ATP-dependent RNA helicase in the cytoplasm (2) and was later shown to be a component of cytoplasmic P-bodies (3). Upf1 phosphorylation mediates the repression of translation that accompanies NMD, allowing mRNA accessibility to the NMD machinery (4). Two other active components of NMD, Upf2 and Upf3, were also identified and described as having perinuclear and nucleocytoplasmic localization, respectively (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: A variety of factors contribute to the important biological event of initiation of translation. The eIF4F complex of translation initiation factors binds to the 5' m7 GTP cap to open up the mRNA secondary structure and allow small ribosome subunit binding (1). eIF4A, an eIF4 complex component that acts as an ATP-dependent RNA helicase, unwinds the secondary structure of the 5' mRNA untranslated region to mediate ribosome binding (2,3). In addition, eIF4A has recently been shown to repress Dpp/BMP signalling in a translation-independent manner in Drosophila (4,5).