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Product listing: FAM134B Antibody, UniProt ID Q9H6L5 #61011 to CD200 (E2K4C) Rabbit mAb, UniProt ID P41217 #69858

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: FAM134B (family with sequence similarity 134, member B), also referred to as JK-1 and RETREG1, is a cis-Golgi endoplasmic reticulum (ER) transmembrane protein that plays a role in ER homeostasis and may contribute to several human diseases (1). FAM134B contains a conserved LC3 interacting domain (LIR) that facilitates binding to LC3 and GABARAP family members and targets impaired ER to the autophagsome for degradation by ER-phagy (2). Deletion of FAM134B leads to ER expansion and stress-induced apoptosis (2). Expression of FAM134B has been linked to a number of pathological conditions, including viral infection, cancer, and neuronal disorders (1). FAM134B can potentially inhibit viral infection, as demonstrated by studies of FAM134B knockouts that resulted in significantly higher rates of Ebola virus replication (3). Mutations in FAM134B that lead to an accumulation of mis-folded proteins have also been associated with neuronal sensory disorders (2, 4, 5). The expression and mutational state of FAM134B can also have varying effects on cancer. Oncogenic effects of FAM134B were described in esophageal squamous carcinoma; whereas, it appears to have tumor suppressor activity in colorectal cancer (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Western Blotting

Background: L-asparaginase (ASRGL1) catalyzes the conversion of L-asparagine to L-aspartate. Research studies have shown that intracellular asparagine can suppress apoptosis in a large number of human tumors (1). In addition, acute lymphocytic leukemia cells frequently depend upon serum asparagine for their viability, as they lack asparagine synthetase (ASNS). Deprivation of asparagine by L-asparaginase has therefore been developed as a therapeutic treatment for acute lymphocytic leukemia (2-3). In KRAS mutant non-small cell lung carcinoma (NSCLC) cells, PI3K/Akt signaling was shown to be required for ASNS expression, suggesting combinatorial Akt inhibition and L-asparaginase treatment as a therapeutic strategy for NSCLC (3). Research studies on a breast cancer model have furthermore shown that restriction of asparagine can suppress cancer metastasis (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: RALY is a member of the large family of heterogeneous nuclear ribonucleoproteins (hnRNPs). RALY was initially discovered in lethal yellow mice, a condition where heterozygotes display an all yellow coat, obesity, diabetes, and tumors. In this condition, mRNA to the 5’ untranslated region of RALY fuses to the agouti transcript (1,2). RALY binds to U-rich elements in coding and non-coding mRNAs undergoing translation (3). RALY has been implicated certain cancer types, as it can control transcriptional regulation and splicing of E2F1 and PRMT1 mRNAs (4,5).

The B Cell Signaling Antibody Sampler Kit II provides an economical means to examine key signaling proteins commonly associated with B cell activation. The provided antibodies allow monitoring of both total protein levels and the phosphorylation state. The kit includes enough antibody to perform two western blot experiments with each primary antibody.
The ULK1 Substrate Antibody Sampler Kit provides an economical means of detecting the activity of ULK1 using phospho-specific and control antibodies. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

Background: Two related serine/threonine kinases, UNC-51-like kinase 1 and 2 (ULK1, ULK2), were discovered as mammalian homologs of the C. elegans gene UNC-51 in which mutants exhibited abnormal axonal extension and growth (1-4). Both proteins are widely expressed and contain an amino-terminal kinase domain followed by a central proline/serine rich domain and a highly conserved carboxy-terminal domain. The roles of ULK1 and ULK2 in axon growth have been linked to studies showing that the kinases are localized to neuronal growth cones and are involved in endocytosis of critical growth factors, such as NGF (5). Yeast two-hybrid studies found ULK1/2 associated with modulators of the endocytic pathway, SynGAP and syntenin (6). Structural similarity of ULK1/2 has also been recognized with the yeast autophagy protein Atg1/Apg1 (7). Knockdown experiments using siRNA demonstrated that ULK1 is essential for autophagy (8), a catabolic process for the degradation of bulk cytoplasmic contents (9,10). It appears that Atg1/ULK1 can act as a convergence point for multiple signals that control autophagy (11), and can bind to several autophagy-related (Atg) proteins, regulating phosphorylation states and protein trafficking (12-16).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: BTB/POZ domain-containing protein KCTD5 is a member of the potassium channel tetramerization domain family of proteins that play a role in transcriptional repression, cytoskeletal regulation, and ion channel gating (1). KCTD5 interacts with bound ubiquitin proteins and cullin3, and acts as a dependent E3 ligase substrate adaptor through interactions with its BTB domain (2). KCTD5 has been identified as a negative regulator of the AKT pathway by acting as an off switch for G-protein coupled receptor signaling by triggering proteolysis of Gβγ heterodimers dissociated from the Gα subunit (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Calcium/Calmodulin-dependent Protein Kinase Kinase 2 (CaMKK2) is a member of the CaMK family that contains a central Ser/Thr kinase domain followed by a regulatory domain consisting of overlapping autoinhibitory and CaM-binding regions (1). CaMKK2 can be distinguished from other CaMK family members by the presence of a unique Pro/Arg/Gly-rich insert following the ATP-binding domain (2). CaMKK2 phosphorylates CaMKI at Thr177 and CaMKIV at Thr200 (3). CaMKK2 also phosphorylates AMPKα in response to calcium (4). CaMKK2 has been implicated in long-term memory formation (5) and adipocyte development (6). CaMKK2 is phosphorylated at Ser511 by death-associated protein kinase (DAPK) in a signaling cascade thought to be involved in neuronal death (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Proteins in the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex are integral membrane proteins involved in vesicle transport and membrane fusion by pairing of vesicular SNAREs (v-SNAREs) with cognate target SNAREs (t-SNAREs) (reviewed in 1,2). Vesicle associated membrane protein 3 (VAMP3), also known as cellubrevin, has a broad tissue distribution and localizes to endosomal compartments (3). VAMP3 interacts with the t-SNAREs syntaxin1, syntaxin4, SNAP23, and SNAP25 (4,5). Research studies indicate that VAMP3 is involved in transferrin receptor recycling to the plasma membrane (6) and in T-cell receptor recycling to immunological synapses (7). Inhibition of VAMP3 with tetanus toxin impairs membrane trafficking during cell migration (8).

The Polycomb Group 2 (PRC2) Antibody Sampler Kit provides an economical means of evaluating total levels of Polycomb Group 2 Proteins. The kit contains enough primary and secondary antibodies to perform two western blot experiments.

Background: The polycomb group (PcG) proteins are involved in maintaining the silenced state of multiple developmentally regulated genes and contribute to the maintenance of cell identity, cell cycle regulation, and oncogenesis (1-4). Enhancer of zest homolog 1 (Ezh1) and enhancer of zest homolog 2 (Ezh2) are members of this large protein family and are subunits of the polycomb repressor complex 2 (PRC2), also known to contain SUZ12, EED, JARID2, and AEBP2. Ezh1 and its paralog Ezh2 are mutually exclusive catalytic subunits of the PRC2 complex, which functions to mono-, di-, and tri-methylate Lys27 on histone H3, all marks that are associated with transcriptional repression. SUZ12 and EED proteins are also absolutely required for methyltransferase activity (5). JARID2 and AEBP2 are both accessory proteins that function to recruit the PRC2 complex to target genes and enhance methyltransferase activity by binding to DNA and histone proteins in nucleosomes (6-14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Retinoids (vitamin A and its active retinoic acid derivatives) are non-steroid hormones that regulate cell proliferation, differentiation and apoptosis. Retinoic acid receptors (RARalpha, -beta and -gamma) and retinoid X receptors (RXRalpha, -beta and -gamma) are nuclear receptors that function as RAR-RXR heterodimers or RXR homodimers (1-2). In response to retinoid binding, these dimers control gene expression by binding to specific retinoic acid response elements, by recruiting cofactors and the transcriptional machinery, and by indirectly regulating chromatin structure. Finally, ligand binding and phosphorylation of RARalpha by JNK at Thr181, Ser445 and Ser461 controls the stability of RAR-RXR through the ubiquitin-proteasome pathway (3-4). At least four distinct genetic lesions affect RARalpha and result in acute promyelocytic leukemia (APL). The t(15;17) translocation that results in the PML-RARalpha fusion protein is responsible for more than 99% of APL cases, and the fusion protein inhibits PML-dependent apoptotic pathways in a dominant negative fashion. In addition PML-RARalpha inhibits transcription of retinoic acid target genes by recruiting co-repressors, attenuating myeloid differentiation (5-6).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse tissue and cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PD-1 (D7D5W) XP® Rabbit mAb (Mouse Specific) #84651.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry)

Background: The programmed cell death 1 protein (PD-1, PDCD1, CD279) is a member of the CD28 family of immunoreceptors that regulate T cell activation and immune responses (1-3). The PD-1 protein contains an extracellular Ig V domain, a transmembrane domain, and a cytoplasmic tail that includes an immunoreceptor tyrosine-based inhibitory motif (ITIM) and an immunoreceptor tyrosine-based switch motif (ITSM). PD-1 is activated by the cell surface ligands PD-L1 and PD-L2 (4). Upon activation, PD-1 ITIM and ITSM phosphorylation leads to the recruitment of the protein tyrosine phosphatases SHP-1 and SHP-2, which suppress TCR signaling (5-7). In addition to activated T-cells, PD-1 is expressed in activated B-cells and monocytes, although its function in these cell types has not been fully characterized (8). The PD-1 pathway plays an important role in immune tolerance (3); however, research studies show that cancer cells often adopt this pathway to escape immune surveillance (9). Consequently, blockade of PD-1 and its ligands is proving to be a sound strategy for neoplastic intervention (10).

$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: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: TAZ is a transcriptional co-activator with a PDZ-binding motif that is regulated by its interaction with 14-3-3 proteins (1). TAZ shares homology with the WW domain of Yes-associated protein (YAP) (1). TAZ is proposed to modulate the switch between proliferation and differentiation of mesenchymal stem cells (MSC) via interaction with transcription factors Runx2 and PPARγ. This process is critical to normal tissue development and the prevention of tumor formation. Due to its role in determination of MSC fate, TAZ may have clinical relevance to several human diseases caused by an imbalance of MSC differentiation (2,3). TAZ is negatively regulated via phosphorylation by LATS1/2, core kinases in the Hippo signaling pathway that controls stem cell development, tissue growth and tumor development (4).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis in mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated VCAM-1 (D8U5V) Rabbit mAb (Mouse Specific) #39036.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: VCAM-1 (vascular cell adhesion molecule-1) is a transmembrane glycoprotein containing multiple amino-terminal extracellular Ig-like domains, a transmembrane domain, and a short carboxy-terminal cytoplasmic domain (1). Alternative splicing generates two isoforms of VCAM-1 (2). The role of VCAM-1 during infection and inflammatory diseases is well characterized. Expression of VCAM-1 is induced in endothelial cells by inflammatory cytokines including TNF-α and IL-1β (1). VCAM-1 on endothelial cells interacts with the integrin VLA-4 (α4β1) on leukocytes to mediate migration of circulating leukocytes from the blood across the endothelium and into tissues (3).

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

Application Methods: Western Blotting

Background: The pyruvate dehydrogenase complex catalyzes the conversion of pyruvate and CoA into acetyl-CoA and CO2 in the presence of NAD+. Acetyl-CoA then goes into the citric acid cycle where it reacts with oxaloacetate to form citrate. Acetyl-CoA is also used for fatty acid and cholesterol biosynthesis. The reaction of oxidative decarboxylation of pyruvate therefore serves as a critical link between glycolysis and the citric acid cycle and lipid metabolism. In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix (1). This complex is comprised of three enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3). Pyruvate dehydrogenase (E1) consists of two subunits: α and β. This enzyme catalyzes the removal of CO2 from pyruvate. Mutations in the α subunits of pyruvate dehydrogenase (E1) lead to congenital defects that are usually associated with lactic acidosis, neurodegeneration and early death (2).

$499
96 assays
1 Kit
The FastScan™ Phospho-Vimentin (Ser56) ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of vimentin when phosphorylated at Ser56. To perform the assay, sample is incubated with a capture antibody conjugated with a proprietary tag and a second detection antibody linked to HRP, forming a sandwich with phospho-vimentin (Ser56) in solution. This entire complex is immobilized to the plate via an anti-tag antibody. The wells are then washed to remove unbound material. TMB is then added. The magnitude of observed signal is proportional to the quantity of phospho-vimentin (Ser56). Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse, Rat

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are distinguished by their cell-specific expression: cytokeratins (epithelial cells), glial fibrillary acidic protein (GFAP) (glial cells), desmin (skeletal, visceral, and certain vascular smooth muscle cells), vimentin (mesenchyme origin), and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Research studies have shown that vimentin is present in sarcomas, but not carcinomas, and its expression is examined in conjunction with that of other markers to distinguish between the two (3). Vimentin's dynamic structural changes and spatial re-organization in response to extracellular stimuli help to coordinate various signaling pathways (4). Phosphorylation of vimentin at Ser56 in smooth muscle cells regulates the structural arrangement of vimentin filaments in response to serotonin (5,6). Remodeling of vimentin and other intermediate filaments is important during lymphocyte adhesion and migration through the endothelium (7).During mitosis, CDK1 phosphorylates vimentin at Ser56. This phosphorylation provides a PLK binding site for vimentin-PLK interaction. PLK further phosphorylates vimentin at Ser82, which might serve as memory phosphorylation site and play a regulatory role in vimentin filament disassembly (8,9). Additionally, studies using various soft-tissue sarcoma cells have shown that phosphorylation of vimentin at Ser39 by Akt1 enhances cell migration and survival, suggesting that vimentin could be a potential target for soft-tissue sarcoma targeted therapy (10,11).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Eukaryotic initiation factor 4E (eIF4E) binds to the mRNA cap structure to mediate the initiation of translation (1,2). eIF4E interacts with eIF4G, a scaffold protein that promotes assembly of eIF4E and eIF4A into the eIF4F complex (2). eIF4B is thought to assist the eIF4F complex in translation initiation. Upon activation by mitogenic and/or stress stimuli mediated by Erk and p38 MAPK, Mnk1 phosphorylates eIF4E at Ser209 in vivo (3,4). Two Erk and p38 MAPK phosphorylation sites in mouse Mnk1 (Thr197 and Thr202) are essential for Mnk1 kinase activity (3). The carboxy-terminal region of eIF4G also contains serum-stimulated phosphorylation sites, including Ser1108, Ser1148, and Ser1192 (5). Phosphorylation at these sites is blocked by the PI3 kinase inhibitor LY294002 and by the FRAP/mTOR inhibitor rapamycin.

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CRACC/SLAMF7/CD319 (also known as CS1) is a member of the signaling lymphocytic activation molecule (SLAM) family. It is a single-pass type l transmembrane glycoprotein expressed on NK cells, subsets of mature dendritic cells, activated B and T lymphocytes, but not in promyelocytic B or T cell lines. Expression of this protein has been detected in the spleen, lymph node, peripheral blood leukocytes, bone marrow, small intestine, stomach, appendix, lung, and trachea (1-6). Homophilic interactions of CRACC/SLAMF7/CD319 modulate the activity and differentiation of immune cells. CRACC/SLAMF7/CD319 may function as an inhibitory or activating receptor in immune cells depending on cellular context and availability of adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2 (5-9). In the presence of SH2D1B/EAT-2, CRACC/SLAMF7/CD319 activates NK cells and B cells (5-7). T cells lack SH2D1B/EAT-2 expression, and therefore CRACC/SLAMF7/CD319 acts as an inhibitory receptor (8). In LPS-activated monocytes, CRACC/SLAMF7/CD319 negatively regulates production of proinflammatory cytokines (9). CRACC/SLAMF7/CD319 is upregulated in multiple myeloma and is implicated in the uncontrolled proliferation of these cells, and thus has become the target for therapeutic intervention (10, 11). Seven isoforms of CRACC/SLAMF7/CD319 produced by alternative splicing have been identified.

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: The protein product of the DEK oncogene is a nuclear phosphoprotein that is highly conserved among higher eukaryotic organisms and preferentially expressed in actively proliferating and/or malignant cells (1,2). DEK is an abundant, non-histone chromosomal protein that establishes and maintains heterochromatin by interacting with HP1a, enhancing HP1a binding to tri-methyl histone H3 Lys9 and stabilizing local tri-methyl histone H3 Lys9 levels (3). DEK localized to euchromatin represses transcription by interacting with transcription factors such as RelA/p65 (4). The DEK protein also associates with mRNA processing factors to regulate splicing and nuclear export (5,6).The DEK proto-oncogene functions as a negative regulator of cellular differentiation, senescence, and apoptosis. DEK is translocated and/or over-expressed in a number of different cancers, including acute myeloid leukemia, breast cancer, cervical cancer, hepatocellular carcinoma, melanoma, and small cell lung cancer (1,2). In addition to the role of DEK in cancer biology, which is mainly related to its intracellular functions, extracellular DEK is implicated in the pathogenesis of autoimmune disorders (1,2). Circulating autoantibodies to DEK have been identified in the serum of patients with autoimmune diseases, including juvenile idiopathic arthritis, sarcoidosis, and systemic lupus erythematosus. DEK is secreted by human monocyte-derived macrophages and apoptotic T-lymphocytes and can act as a chemotactic, pro-inflammatory factor (7,8). Exogenous DEK can penetrate neighboring cells, and translocate to the nucleus to carry out its endogenous nuclear functions (9). IL-8 induced secretion of DEK from macrophages serves as a chemoattractant for peripheral blood leukocytes (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Decay-accelerating factor (DAF/CD55) is a GPI-linked plasma membrane glycoprotein normally expressed on the surface of vascular endothelial and hematopoietic cells, which are continuously exposed to autologous complement components. In conjunction with other membrane complement regulatory proteins (CD35, CD46, and CD59), DAF/CD55 protects healthy cells from inappropriate complement-mediated lysis (1). DAF/CD55 inhibits activation of the complement cascade by promoting membrane dissociation and inactivation of C3 convertase, which inhibits amplification of the classical and alternative complement cascades (2). Research studies have demonstrated that DAF/CD55 is overexpressed in a variety of solid and liquid tumors, which functions to protect tumor cells from complement-mediated attack (3,4). Given its ability to disable the complement cascade and facilitate immune evasion by tumor cells, DAF/CD55 has received attention as a potential therapeutic target for the treatment of human malignancies. CD55 deficiency is also linked to human disease. The inability to express CD55 on the surface of erythrocytes renders them highly susceptible to complement-mediated lysis, which contributes to the development of paroxymal noctural hemoglobinuria (PNH). PNH is characterized by hemolytic anaemia, pancytopenia, and venous thrombosis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MAFB belongs to the musculoaponeurotic fibrosarcoma (MAF) family of basic leucine-zipper transcription factors (1). In mouse embryo, MAFB expression is first detected at E10.5 (2, 3). Early in development, MAFB drives differentiation of both glucagon-producing α-cells and insulin-producing β-cells in the pancreas, but later plays a more decisive role in the maturation and maintenance of functional α-cells (4, 5). Consistent with MAFB playing a critical role in mature α-cells, MAFB is enriched in α-cells within 2 weeks of birth in the pancreas (6). Glucagon and insulin secretion is tightly regulated, and imbalances in these hormones contribute to metabolic conditions. Therefore, understanding the role of MAFB in α-cell development, maintenance, and physiological function may contribute to developing deeper insights into how these cells contribute to metabolic diseases like diabetes. MAFB also regulates monocyte differentiation, indicating MAFB functions beyond the pancreas (7).

$309
100 µg
This Cell Signaling Technology antibody is conjugated to APC and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).FoxP3 is crucial for the development of T cells with regulatory properties (Treg) (6). Mutations in FoxP3 are associated with immune dysregulation, polyendocrinopathy, enteropathy, and X-linked syndrome (IPEX) (7), while overexpression in mice causes severe immunodeficiency (8). Research studies have shown that FoxP3 functions as a tumor suppressor in several types of cancer (9-11).

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

Application Methods: Western Blotting

Background: Lysine-specific demethylase 2 (LSD2; also known as AOF1) is a nuclear amine oxidase homolog that acts as a histone demethylase and transcription cofactor protein (1,2). LSD2 functions as a co-repressor protein by demethylating mono-methyl and di-methyl histone H3 Lys4, two marks associated with actively transcribed genes (1,2). LSD2-mediated demethylation of histone H3 Lys4 is required for establishing proper DNA methylation imprints during oogenesis (3). In addition, LSD2 appears to be overexpressed in malignant breast cancers, where it contributes to DNA methylation and repression of multiple tumor suppressor genes (4,5). Furthermore, LSD2 also contains E3 ubiquitin ligase activity that targets O-GlcNac transferase (OGT) for proteosomal degradation (6). A549 lung cancer cell growth is dependent on this E3 ubiquitin ligase activity, suggesting that this function of LSD2 is also important for proper gene regulation (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: RPA70 (HSSB, REPA1, RF-A, RP-A, p70) is a component of a heterotrimeric complex, composed of 70, 32/30 and 14 kDa subunits, collectively known as RPA. RPA is a single stranded DNA binding protein, whose DNA binding activity is believed to reside entirely in the 70 kDa subunit. The complex is required for almost all aspects of cellular DNA metabolism such as DNA replication (1-3), recombination, cell cycle and DNA damage checkpoints, and all major types of DNA repair including nucleotide excision, base excision, mismatch and double-strand break repairs (4-7). In response to genotoxic stress in eukaryotic cells, RPA has been shown to associate with the Rad9/Rad1/Hus1 (9-1-1) checkpoint complex (8). RPA is hyperphosphorylated upon DNA damage or replication stress by checkpoint kinases including ataxia telangiectasia mutated (ATM), ATM and Rad3-related (ATR), and DNA-dependent protein kinase (DNA-PK) (9-11). Phosphorylation of RPA32 occurs at serines 4, 8 and 33 (11). Hyperphosphorylation may alter RPA-DNA and RPA-protein interactions. In addition to the checkpoint partners, RPA interacts with a wide variety of protein partners, including proteins required for normal replication such as RCF, PCNA and Pol α, and also proteins involved in SV40 replication, such as DNA polymerase I and SV40 large T antigen (10,12).

$499
96 assays
1 Kit
The FastScan™ Total Tau ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Tau. To perform the assay, sample is incubated with a capture antibody conjugated with a proprietary tag and a second detection antibody linked to HRP, forming a sandwich with Tau in solution. This entire complex is immobilized to the plate via an anti-tag antibody. The wells are then washed to remove unbound material. TMB is then added. The magnitude of observed signal is proportional to the quantity of Tau. Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse, Rat

Background: Tau is a heterogeneous microtubule-associated protein that promotes and stabilizes microtubule assembly, especially in axons. Six isoforms with different amino-terminal inserts and different numbers of tandem repeats near the carboxy terminus have been identified, and tau is hyperphosphorylated at approximately 25 sites by Erk, GSK-3, and CDK5 (1,2). Phosphorylation decreases the ability of tau to bind to microtubules. Neurofibrillary tangles are a major hallmark of Alzheimer's disease; these tangles are bundles of paired helical filaments composed of hyperphosphorylated tau. In particular, phosphorylation at Ser396 by GSK-3 or CDK5 destabilizes microtubules. Furthermore, research studies have shown that inclusions of tau are found in a number of other neurodegenerative diseases, collectively known as tauopathies (1,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Glucose-6-phosphate isomerase (GPI) is a multi-functional protein belonging to the glucose phosphate isomerase family (1,2). As an intracellular metabolic enzyme, GPI plays a pivotal role in glycolysis and gluconeogenesis by catalyzing the interconversion of D-glucose-6-phosphate and D-fructose-6-phosphate (3). GPI is also secreted, where it functions as a cytokine (referred to as Autocrine Motility Factor, AMF), acting via the E3-ubiquitin-protein ligase AMFR/gp78 (4). In normal tissues, GPI/AMF has been shown to promote both immune cell maturation and neuronal cell survival (5,6). It is also secreted in abundance by some tumor cells (7), where it has been shown to promote tumor cell migration and metastasis (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Jumonji domain-containing protein 6 (JMJD6) is a bifunctional metalloenzyme belonging to the large family of JmjC domain-containing proteins. These proteins are ferrous iron- and 2-oxoglutarate-dependent enzymes (Fe2+/2OG) that catalyze hydroxylation and demethylation reactions on a wide variety of protein and nucleic acid substrates (1). JMJD6 is thought to act as both a lysyl-hydroxylase and an arginine demethylase, although the latter activity remains controversial. Specifically, JMJD6 has been shown to catalyze 5-hydroxylation of Lys15 and Lys276 residues on the protein U2AF2 / U2AF65 in vivo, affecting pre-mRNA splicing activity (2). It has also been reported that JMJD6 hydroxylates the Lys382 residue of p53, preventing acetylation and promoting association of p53 with MDMX, resulting in inhibition of p53 transcriptional activity (3). In addition to hydroxylase activity, JMJD6 also acts as an arginine demethylase by targeting histone H3 at Arg2 (H3R2me) and histone H4 at Arg3 (H4R3me). Unlike other members of the JmjC family, JMJD6 appears to have no lysine demethylase activity (4). Studies have shown that JMJD6 colocalizes with BRD4 at a subset of enhancers to demethylate H3R2me2 repressor marks (5). It has also been reported to demethylate non-histone substrates, such as estrogen receptor (ERα) (6), heat shock protein 70 (HSP70) (7), RNA helicase A (8), and the TRAF6 E3 ubiquitin ligase following activation of toll-like receptors (9).Although mutations in the sequence of JMJD6 have not been observed in cancer, its overexpression is identified in various cancers and is associated with aggressive disease progression and poor prognosis (10). This holds true for certain types of colon (3), lung (11), and breast cancers (12, 13). Based on these findings, JMJD6 has drawn interest as a potential therapeutic target and biomarker for certain cancer types.

$309
100 µg
This Cell Signaling Technology antibody is conjugated to PE and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).FoxP3 is crucial for the development of T cells with regulatory properties (Treg) (6). Mutations in FoxP3 are associated with immune dysregulation, polyendocrinopathy, enteropathy, and X-linked syndrome (IPEX) (7), while overexpression in mice causes severe immunodeficiency (8). Research studies have shown that FoxP3 functions as a tumor suppressor in several types of cancer (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: CD200 (OX2) and CD200R (OX2R) are membrane glycoprotein members of the Ig superfamily (1-3). CD200 is expressed by a range of cells, including neurons, epithelial cells, endothelial cells, fibroblasts, and lymphoid cells, while its receptor, CD200R, is found on myeloid and T cells (1-5). Interaction between CD200 and CD200R downregulates macrophage function and plays a role in immunosuppression and regulation of anti-tumor immune responses (3-7).