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Product listing: XRN1 Antibody, UniProt ID Q8IZH2 #70205 to Annexin A2 (D11G2) Rabbit mAb (PE Conjugate), UniProt ID P07355 #15161

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: 5’-3’ exoribonuclease 1 (XRN1) is a cytoplasmic exonuclease that degrades RNA containing a 5’-monophosphate to component mononucleotides. XRN1 is the primary exonuclease associated with ribosomes in the cytoplasm and is responsible for mRNA turnover (1,2). This turnover is facilitated in discrete structures in the cytoplasm called P-bodies that contain decapping and deadenylation proteins (3). XRN1 also plays a role in RISC-mediated mRNA degradation, as it associates with 3’ mRNA fragments generated by RISC cleavage. This process does not require uncapping or deadenylation (4). XRN1 plays a significant role in viral RNA degradation (5). As such, many viral genomes, including hepatitis C, Dengue, and West Nile, encode for XRN1-resistant long non-coding RNA that affect innate immunity and viral replication (6).

$305
50 assays
100 µl
This Cell Signaling Technology antibody was conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for immunofluorescence in cells transfected with Myc-tagged protein.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Formins are a family of large multidomain actin nucleation/polymerization proteins characterized by their catalytic FH2 domains. The mammalian diaphanous-related formin (mDia/diap) subfamily, including mDia1/diap1, mDia2/diap3 and mDia3/diap2, are effectors of Rho family small GTPases. In response to Rho, mDia/diap proteins are involved in the regulation of multiple cell functions including cytoskeletal dynamics, migration, adhesion, polarity and cell shape (reviewed in 1,2).mDia1/diap1 is activated by GTP-bound Rho, leading to Rho-associated kinase (ROCK)-dependent stress fiber formation (3,4). Rho activation of mDia1 has also been shown to regulate serum response factor (SRF)-dependent transcription (5), and has been implicated in human cancer phenotypes such as ras-mediated transformation, metastasis and invasion (reviewed in 6).mDia3/diap2, activated by the Rho family small GTPase cdc42, regulates the attachment of microtubules to the kinetochore during mitosis in mammalian cells (7).Rho-dependent activation of mDia2/diap3 is important in assembly of the contractile ring during cytokinesis (8,9).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Translation initiation requires a set of factors to facilitate the association of the 40S ribosomal subunit with mRNA. The eIF4F complex, consisting of eIF4E, eIF4A, and eIF4G, binds to the 5' cap structure of mRNA. eIF4F and eIF4B unwind the secondary structure of mRNA at its 5' untranslated region. The 40S ribosomal subunit, along with some initiation factors including eIF3, then binds to the 5' mRNA cap and searches along the mRNA for the initiation codon. eIF3 is a large translation initiation complex with 10 to 13 different subunits. eIF3A, eIF3B, eIF3C, eIF3E, eIF3F, and eIF3H are the core subunits critical for the function of this complex. eIF3 physically interacts with eIF4G, which may be responsible for the association of the 40S ribosomal subunit with mRNA (1). eIF3 also stabilizes the binding of Met-tRNAf.eIF2.GTP to the 40S ribosomal subunit and helps keep the integrity of the resulting complex upon addition of the 60S ribosomal subunit (2). Studies have shown that mTOR interacts with eIF3 directly (3,4). When cells are stimulated by hormones or mitogenic signals, mTOR binds to the eIF3 complex and phosphorylates S6K1 (3). This process results in the dissociation of S6K1 from eIF3 and S6K1 activation. The activated S6K1 then phosphorylates its downstream targets including ribosomal protein S6 and eIF4B, resulting in stimulation of translation. Further findings demonstrated that activated mTOR signaling induces the association of eIF3 with eIF4G upon stimulation with insulin (3).

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

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

Background: The ubiquitin-conjugating (UBC) enzymes HR6A and HR6B are the mammalian orthologues of the Saccharomyces cerevisiae Rad6 gene products (1). In S. cerevisiae, Rad6 facilitates cell cycle progression and ubiquitinates histone H2B (2,3). In vivo phosphorylation of HR6A Ser120 by cyclin-dependent kinases is thought to be important for the coordination and timing of ubiquitination events involved in cell cycle progression (4). In response to DNA damage, HR6A is known to interact physically with p53 and p14ARF, but knockout mice lacking HR6A or HR6B exhibit normal DNA damage responses (5,6). HR6B knockout males exhibit defective spermatogenesis, while HR6A knockout females fail to produce viable offspring (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain, and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience-dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Atlastin proteins are highly conserved members of the dynamin superfamily of membrane GTPases that are involved in the formation of vesicles for the endocytotic and secretory processes (1). Atlastins are required to establish and maintain the morphology of the tubular endoplasmic reticulum (ER) and are therefore important in ER function (2). GTP hydrolysis and dimerization are required for atlastin-dependent ER membrane fusion (3).Atlastin GTPase 1 (ATL1) is primarily expressed in brain, while the related atlastin 2 and atlastin 3 proteins are ubiquitously expressed (4). Mutations in the atlastin 1 gene SPG3A and the ER defects that result are thought to cause one form of hereditary spastic paraplegia (HSP), a group of heterogeneous neurological disorders characterized by severe progressive spasticity of the lower limbs (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Adherens junctions are dynamic structures that form cell-cell contacts and are important in development, differentiation, tissue integrity, morphology and cell polarity. They are composed of the transmembrane proteins, cadherins, which bind cadherins on adjacent cells in a calcium-dependent manner. On the cytoplasmic side of adherens junctions, the classic model states that cadherins are linked to the cytoskeleton through β- and α-catenin. α-E-catenin is ubiquitously expressed, α-N-catenin is expressed in neuronal tissue, and α-T-catenin is primarily expressed in heart tissue. Research studies have demonstrated that loss of E-cadherin and α-E-catenin occurs during the progression of several human cancers, indicating that the breakdown of adherens junctions is important in cancer progression (reviewed in 1).Research studies also suggest that, rather than acting as a static link between cadherins and actin, α-catenin regulates actin dynamics directly, possibly by competing with the actin nucleating arp2/3 complex (2,3). α-catenin also plays a role in regulating β-catenin-dependent transcriptional activity, affecting differentiation and response to Wnt signaling. α-catenin binds to β-catenin in the nucleus, preventing it from regulating transcription, and levels of both proteins appear to be regulated via proteasome-dependent degradation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: ROR1 and ROR2 are orphan receptor tyrosine kinases that are most closely related to MuSK and the Trk family of neurotrophin receptors. They are characterized by the presence of extracellular frizzled-like cysteine-rich domains and membrane-proximal kringle domains, both of which are assumed to mediate protein-protein interactions (1-3). The ROR family RTKs are evolutionarily conserved among Caenorhabditis elegans, Drosophila, mice, and humans (1,4). Although the functions of ROR kinases are unknown, similarities between ROR and MuSK and Trk kinases have led to speculation that ROR kinases regulate synaptic development. CAM-1, a C. elegans ortholog of the ROR family RTKs, plays several important roles in regulating cellular migration, polarity of asymmetric cell divisions, and axonal outgrowth of neurons during nematode development (4). mROR1 and mROR2 may play differential roles during the development of the nervous system (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: CD133, also known as Prominin, was first described as a cell surface marker recognized by monoclonal antibody AC133 on putative hematopoietic stem cells (1). Subsequent cDNA cloning indicated that CD133 is a five-transmembrane protein with a predicated molecular weight of 97 kDa. Due to heavy glycosylation, its apparent molecular weight is 130 kDa as determined by SDS-PAGE analysis (2). Besides blood stem cells, CD133 is expressed on and used to isolate other stem cells, including cancer stem cells (3-7). A deletion mutation in CD133 produces aberrant protein localization and may result in retinal degeneration in humans (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Mastermind-like (MAML) family of proteins are homologs of Drosophila Mastermind. The family is composed of three members in mammals: MAML1, MAML2, and MAML3 (1,2). MAML proteins form complexes with the intracellular domain of Notch (ICN) and the transcription factor CSL (RBP-Jκ) to regulate Notch target gene expression (3-5). MAML1 also interacts with myocyte enhancer factor 2C (MEF2C) to regulate myogenesis (6). MAML2 is frequently found to be fused with Mucoepidermoid carcinoma translocated gene 1 (MECT1, also know as WAMTP1 or TORC1) in patients with mucoepidermoid carcinomas and Warthin's tumors (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Tensin 2 belongs to the Tensin family of cytoskeletal proteins that includes Tensin 1-3 and Cten, which couple integrins to the actin cytoskeleton (1). Tensin proteins contain SH2 and phosphotyrosine binding (PTB) domains, which enable interaction with diverse signaling molecules and proteins. Tensin family proteins play important roles in signal transduction, cell proliferation, and motility (2-5).Tensin 2 is localized to focal adhesions of various tissues with highest expression in the heart, kidney, and liver (6,7). Tensin 2 inhibits Akt/PKB signaling via a phosphatase tensin-type domain (8). However, Tensin 2 also mediates thrombopoietin/c-Mpl signaling, which promotes Akt signaling (9). Interaction with Tensin 2 is essential for the tumor suppressor function of Deleted in Cancer 1 (DLC1) (10-12).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The yeast nucleotide excision repair (NER) radiation sensitive protein 23 (rad23) and its human homologs Rad23A (hHR23A) and Rad23B (hHR23B) are critical components of the cellular machinery that recognize DNA lesions and serve as receptors that target ubiquitinated substrates to the proteasome for degradation (1).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: SLFN11 is a nuclear protein that belongs to the Schlafen (SLFN) family of genes involved in cell cycle regulation and growth inhibition (1, 2). Expression of SLFN11 predicts sensitivity of cancer cell lines to DNA-damaging agents (1, 3). Evidence suggests that in the presence of DNA-targeted therapies, SLFN11 is recruited to stressed replication forks where it blocks replication leading to cell death (4). SLFN11 is being explored as a predictive biomarker for response to DNA-targeted therapies (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Mouse, Rat

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

Background: PZR (Protein zero related) is an immunoglobulin superfamily protein that specifically binds the tyrosine phosphatase SHP-2 through its intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIMs) (1,2). PZR is phosphorylated by c-Src, c-Fyn, c-Lyn, Csk, and c-Abl (3). PP1, a Src family kinase inhibitor, inhibits PZR phosphorylation (4,5). There are three alternatively spliced isoforms, designated as PZR, PZRa, and PZRb; both PZRa and PZRb lack ITIMs (6,7). PZR is the main receptor of ConA and has an important role in cell signaling via c-Src (4). PZR is expressed in many cell types and is localized to cell contacts and intracellular granules in BAECs and mesothelioma (REN) cells. PZR has been implicated as a cell adhesion protein that may be involved in SHP-2-dependent signaling at interendothelial cell contacts (3). Hypertyrosine phosphorylation of PZR was observed during embryogenesis in a mouse model of Noonan syndrome (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Retinoic acid-induced protein 2 (RAI2) is a 530 amino acid protein, encoded by the RAI2 gene on XP22.3 (1). RAI2 contains a central, proline-rich domain that is hypothesized to play a role in protein-protein interactions, and is expressed in a variety of embryonic and adult tissues (2). Beyond that, little is known about the biological functions of RAI2. Notably, a 2015 research study reported that suppressing RAI2 led to increased hematogenous dissemination of breast cancer cells to bone marrow, suggesting that RAI2 may function to negatively regulate tumor metastasis (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Tousled-like kinases (TLK1 and TLK2) are nuclear serine/threonine kinases named for their homology to the Tousled gene from Arabidopsis thaliana, essential for flower development (1). The kinase activities of the TLKs are cell cycle regulated, with maximal activity during S phase (1). TLK appears to play a role in chromatin assembly and DNA damage checkpoint regulation (1,2). In C. elegans, TLK1 is essential for appropriate transcription during embryonic development (3). Substrates for TLK include the human chromatin assembly factor Asf, which functions in DNA replication- and repair-coupled chromatin assembly (2). DNA damage during S phase, when TLK is maximally active, leads to inhibition of TLK activity (1). This inhibition requires ataxia mutated kinase (ATM) and Chk1 (4,5). ATM and the related kinase ATR are activited by DNA damage during S phase, phosphorylate Chk1/Chk2, and block the transition into mitosis (6). Chk1 phosphorylates TLK1 on Ser743 in vitro and in vivo, leading to inhibition of TLK1 activity (4). This process likely provides a mechanism to slow the chromatin assembly processes controlled by TLK in the event of DNA damage.

PTMScan® IAP Buffer is used to reconstitute lyophilized peptides prior to immunoaffinity purification (IAP).
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Macrophage-colony stimulating factor (M-CSF, CSF-1) receptor is an integral membrane tyrosine kinase encoded by the c-fms proto-oncogene. M-CSF receptor is expressed in monocytes (macrophages and their progenitors) and drives growth and development of this blood cell lineage. (1-3). Binding of M-CSF to its receptor induces receptor dimerization, activation, and autophosphorylation of cytoplasmic tyrosine residues used as docking sites for SH2-containing signaling proteins (4). There are at least five major tyrosine autophosphorylation sites. Tyr723 (Tyr721 in mouse) is located in the kinase insert (KI) region. Phosphorylated Tyr723 binds the p85 subunit of PI3 kinase as well as PLCγ2 (5). Phosphorylation of Tyr809 provides a docking site for Shc (5). Overactivation of this receptor can lead to a malignant phenotype in various cell systems (6). The activated M-CSF receptor has been shown to be a predictor of poor outcome in advanced epithelial ovarian carcinoma (7) and breast cancer (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: XPB and XPD are ATPase/helicase subunits of the TFIIH complex that are involved in nucleotide excision repair (NER) to remove lesions and photoproducts generated by UV light (1). XPB and XPD are 3’-5’ and 5’-3’ DNA helicases, respectively, that play a role in opening of the DNA damage site to facilitate repair (2,3). XPB and XPD both play an important role in maintaining genomic stability, and researchers have linked mutations of these proteins to Xeroderma Pigmentosum (XP) and Trichothiodystrophy (TTD). XP patients have abnormalities in skin pigmentation and are highly susceptible to skin cancers, while TTD patients exhibit symptoms such as brittle hair, neurological abnormalities, and mild photosensitivity (4). In addition to their role in NER, XPB and XPD are involved in transcription initiation as part of the TFIIH core complex (5). The helicase activity of XPB unwinds DNA around the transcription start site to facilitate RNA polymerase II promoter clearance and initiation of transcription (6). XPD plays a structural role linking core TFIIH components with the cdk-activating kinase (CAK) complex that phosphorylates the C-terminus of the largest subunit of RNA polymerase II, leading to transcription initiation (7).

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster

Application Methods: Western Blotting

Background: Cell death in the fruit fly Drosophila melanogaster is regulated by many of the same stimuli as mammalian cell death (1). The Drosophila genome contains seven caspase genes; three encode initiator caspases and four encode effector caspases (reviewed in 2). drICE is a cysteine protease that cleaves baculovirus p35 and lamin DmO in vitro and acts downstream of rpr (3). drICE is proteolytically processed during apoptosis into active p21 and p12 subunits. Comparison of the in vivo activity between drICE and Dcp-1 has shown that drICE is a more effective inducer of apoptosis than Dcp-1, which plays a role in determining the rate of cell death (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: HLA-F adjacent transcript 10 (FAT10/Ubiquitin D) belongs to the ubiquitin-like modifier (Ubl) family of proteins. The 18 kDa FAT10 protein contains two tandem Ubl domains that are oriented in a head-to-tail fashion and a free C-terminal di-glycine motif, which is available for isopeptide bond formation with target proteins via an E1-E2-E3 enzymatic cascade (1). Indeed, FAT10 provides a ubiquitin-independent signal for proteasomal degradation (2). Research studies have demonstrated that FAT10 expression is enriched in lymphoid organs and that its expression is transiently upregulated via the NF-kB pathway in response to pro-inflammatory cytokines such as TNFα and IFNγ (1,3-5). In solid tumors that possess inflammatory microenviroments, research studies have shown that FAT10 is overexpressed and may serve as a biomarker for inflamed tumors (6,7).

$118
10 western blots
200 µl
Nonphosporylated MEK1/2 Control Cell Extracts: Total cell extracts from HeLa cells, serum starved overnight serve as a negative control. Supplied in SDS Sample Buffer.Phosphorylated MEK1/2 Control Cell Extracts: Total cell extracts from HeLa cells, serum starved overnight then treated with 200 nM TPA #4174 for 15 minutes to serve as a positive control. Supplied in SDS Sample Buffer.
APPLICATIONS

Application Methods: Western Blotting

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: ABHD6 (α/β-Hydrolase domain-containing 6) is a monoacylglycerol lipase, ubiquitously expressed with the highest expression in brown adipose tissue, small intestine, and brain (1). A high-fat diet upregulates ABHD6 mRNA expression in small intestine and liver, and ABHD6 knockdown protects against high-fat diet-induced obesity, hepatic steatosis, and systemic insulin resistance (2). In addition, it has been shown that ABHD6 is a negative modulator of glucose-stimulated insulin secretion (3). In the central nervous system, ABHD6 is expressed postsynptically and degrades the endocannabinoid 2-arachidonoylglycerol (2-AG), an endogenous activator of cannabinoid receptors (4,5). Inhibitors of α/β-hydrolase domain 6 (ABHD6) have been actively pursued as a promising approach to treat inflammation, metabolic disorders, and epilepsy (2,6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Rab27 is a member of the Ras superfamily of small Rab GTPases implicated in exocytosis (1-2). The protein is localized in secretory lysosomes, such as melanosomes in melanocyte or lytic granules in cytotoxic T cells to control exosome secretion pathway (3-5). Rab27 has two isoforms, Rab27a and Rab27b. Rab27a colocalizes with part of CD63 staining vesicles, and Rab27b shows perinuclear distribution. Target knock out studies indicate that the isoforms control different steps of the exosome secretion pathway (6). Rab27a interacts with a wide range of effectors and is involved in multiple steps of exocytosis depending on the effector it associated with and the cell type that is involved (1,2). Rab27a has been shown to be an important player in leukocyte function, cancer metastasis and invasion, and insulin secretion (7-11)

$348
400 µl
This Cell Signaling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. Mer (D21F11) XP® Rabbit mAb (Sepharose® Bead Conjugate) is useful for the immunoprecipitation of Mer. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Mer (D21F11) XP® Rabbit mAb #4319.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation

Background: Mer tyrosine kinase belongs to a receptor tyrosine kinase family with Axl and Tyro3. This family is characterized by a common NCAM (neural adhesion molecule)-related extracellular domain and a common ligand, GAS6 (growth arrest-specific protein 6). Mer protein has an apparent molecular weight of 170-210 kDa due to different glycosylation patterns generated in different cell types. Mer can be activated by dimerization and autophosphorylation through ligand binding or homophilic cell-cell interaction mediated by its NCAM-like motif (1). The downstream signaling components of activated Mer include PI3 kinase, PLCγ, and MAP kinase (2). Family members are prone to transcriptional regulation and carry out diverse functions including the regulation of cell adhesion, migration, phagocytosis, and survival (3). Mer regulates macrophage activation, promotes apoptotic cell engulfment, and supports platelet aggregation and clot stability in vivo (4). Investigators have found that overexpression of Mer may play a cooperative role in leukemogenesis and may be an effective target for biologically based leukemia/lymphoma therapy (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

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

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

Background: The methylation state of lysine residues in histone proteins is a major determinant of the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (1,2). Jumonji C (JmjC) domain-containing proteins represent the largest class of potential histone demethylase proteins (3). The JmjC domain of several proteins has been shown to catalyze the demethylation of mono-, di-, and tri-methyl lysine residues via an oxidative reaction that requires iron and α-ketoglutarate (3). Based on homology, both humans and mice contain at least 30 such proteins, which can be divided into seven separate families (3). The JMJD1 (Jumonji domain-containing protein 1) family, also known as JHDM2 (JmjC domain-containing histone demethylation protein 2) family, contains four members: hairless (HR), JMJD1A/JHDM2A, JMJD1B/JHDM2B, and JMJD1C/JHDM2C. Hairless is expressed in the skin and brain and acts as a co-repressor of the thyroid hormone receptor (4-6). Mutations in the hairless gene cause alopecia in both mice and humans (4,5). JMJD1A is expressed in meiotic and post-meiotic male germ cells, contributes to androgen receptor-mediated gene regulation, and is required for spermatogenesis (7-9). It has also been identified as a downstream target of OCT4 and STAT3 and is critical for the regulation of self-renewal in embryonic stem cells (10,11). JMJD1B is a more widely expressed family member and is frequently deleted in myeloid leukemia (12). JMJD1C (also known as TRIP8) is a co-factor of both the androgen and thyroid receptors and has a potential link to autism (13-15). Members of the JMJD1/JHDM2 family have been shown to demethylate mono-methyl and di-methyl histone H3 (Lys9) (3,8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Glucocorticoid hormones control cellular proliferation, inflammation, and metabolism through their association with the glucocorticoid receptor (GR)/NR3C1, a member of the nuclear hormone receptor superfamily of transcription factors (1). GR is composed of several conserved structural elements, including a carboxy-terminal ligand-binding domain (which also contains residues critical for receptor dimerization and hormone-dependent gene transactivation), a neighboring hinge region containing nuclear localization signals, a central zinc-finger-containing DNA-binding domain, and an amino-terminal variable region that participates in ligand-independent gene transcription. In the absence of hormone, a significant population of GR is localized to the cytoplasm in an inactive form via its association with regulatory chaperone proteins, such as HSP90, HSP70, and FKBP52. On hormone binding, GR is released from the chaperone complex and translocates to the nucleus as a dimer to associate with specific DNA sequences termed glucocorticoid response elements (GREs), thereby enhancing or repressing transcription of specific target genes (2). It was demonstrated that GR-mediated transcriptional activation is modulated by phosphorylation (3-5). Although GR can be basally phosphorylated in the absence of hormone, it becomes hyperphosphorylated upon binding receptor agonists. It has been suggested that hormone-dependent phosphorylation of GR may determine target promoter specificity, cofactor interaction, strength and duration of receptor signaling, receptor stability, and receptor subcellular localization (3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Annexin A2 (D11G2) Rabbit mAb #8235.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Flow Cytometry

Background: Annexin A2 (ANXA2), also known as lipocortin II or calpactin-1 heavy chain, is a 36 kDa member of the annexin superfamily that binds phospholipids and other proteins in a calcium-dependent manner via annexin repeats (1). Annexin A2 contains four such repeats through which it mediates protein-protein and protein-lipid interactions (1-4). It forms a constitutive heterotetramer with S100A10, acting as a bridge between the actin cytoskeleton, plasma membrane, and endocytotic vesicle machinery (5-7). Originally identified as a protein inhibitor of phospholipase A2, annexin A2 has subsequently been shown to interact with an array of protein and non-protein partners, including F-actin, spectrin, SNARE complexes, RNA, and virus particles (4,6,8,9). Annexin A2 has also been shown to have receptor-like activity and is detected on the surface of macrophages and vascular endothelial cells where it mediates macrophage activation and Factor Xa signaling, respectively (10-13). Upregulation of annexin A2 at the cell surface is thought to be modulated by phosphorylation at Tyr23 by Src (14-18). Interestingly, phosphorylation at Tyr23 has recently been shown to be required for cell surface expression of annexin A2 where it mediates motility, invasiveness, and overall metastatic potential of certain pancreatic cancer cells (19,20). Annexin A2 has also been shown to be heavily phosphorylated on serine residues in response to PKC activation via a pleiotropic mechanism (21-23). For a complete list of curated phosphorylation sites on annexin A2, please see PhosphoSitePlus® at www.phosphosite.org.