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Product listing: VGLUT2 (D7D2H) Rabbit mAb, UniProt ID Q9P2U8 #71555 to Protein G Magnetic Beads #70024

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Glutamatergic neurons release glutamate, the most common excitatory neurotransmitter. Their synaptic vesicles are filled with glutamate by vesicular glutamate transporters, VGLUTs (1). VGLUT1, also called solute carrier family 17 member 7 (SLC17A7), was first identified as an inorganic phosphate transporter (2). Despite the absence of homology with neurotransmitter transporters, VGLUT1 was later demonstrated to be a glutamate transporter (1) specific to glutamatergic neurons (3). Closely related to VGLUT1, VGLUT2 and VGLUT3 are also involved in glutamate uptake into synaptic vesicles, but define different neuronal subpopulations (4,5). VGLUT1 and VGLUT2 are the most abundant isoforms. VGLUT1 is expressed in the cortex, hippocampus, and cerebellar cortex, while VGLUT2 is mostly found in the thalamus (6,7). VGLUT3 is expressed in hair cells of the auditory system (8).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Btk (D6T2C) Mouse mAb #56044.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: Bruton's tyrosine kinase (Btk) is a member of the Btk/Tec family of cytoplasmic tyrosine kinases. Like other Btk family members, it contains a pleckstrin homology (PH) domain and Src homology SH3 and SH2 domains. Btk plays an important role in B cell development (1,2). Activation of B cells by various ligands is accompanied by Btk membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate (3-5). The membrane-localized Btk is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinases, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation (6,7). The activation of Btk is negatively regulated by PKCβ through phosphorylation of Btk at Ser180, which results in reduced membrane recruitment, transphosphorylation, and subsequent activation (8). The PKC inhibitory signal is likely to be a key determinant of the B cell receptor signaling threshold to maintain optimal Btk activity (8).

$348
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 DC-SIGN (D7F5C) XP® Rabbit mAb #13193.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: DC-SIGN (CD209, CLEC4L) is a C-type lectin receptor expressed by dendritic cells (DCs) (1,2). The DC-SIGN transcript can undergo several splicing events to generate at least thirteen different transmembrane and soluble isoforms (3). DC-SIGN responds to a broad range of pathogens due to its ability to recognize both mannose and fructose carbohydrates, and is well studied for its role in HIV infection. Recognition of the HIV envelope glycoprotein gp120 by DC-SIGN leads to internalization of HIV by DCs and facilitates transmission of the virus to CD4+ T cells (2,4). DC-SIGN also mediates adhesion to T cells through interaction with ICAM-3, as well as transmigration across the endothelium by binding to ICAM-2 (1,5). The DC-SIGN receptor can modulate TLR signaling by activating the kinase Raf-1 (6,7). The closely related molecule DC-SIGNR (L-SIGN, CLEC4M) is 77% homologous to DC-SIGN and likely arose through a gene duplication event (8). Like DC-SIGN, DC-SIGNR binds mannose carbohydrates on the surface of pathogens (8,9). However, the expression patterns of the two receptors differ, as DC-SIGNR expression is restricted to endothelial cells of the liver, lymph node, and placenta (10). Murine cells contain a set of related molecules, SIGNR1-SIGNR8 (11). Based on sequence analysis, there is no clear murine ortholog to human DC-SIGN, however SIGNR3 is the most functionally similar due to its ability to recognize both mannose and fructose structures (11).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Focal adhesion kinase (FAK) is a widely expressed cytoplasmic protein tyrosine kinase involved in integrin-mediated signal transduction. It plays an important role in the control of several biological processes, including cell spreading, migration, and survival (1). Activation of FAK by integrin clustering leads to autophosphorylation at Tyr397, which is a binding site for the Src family kinases PI3K and PLCγ (2-5). Recruitment of Src family kinases results in the phosphorylation of Tyr407, Tyr576, and Tyr577 in the catalytic domain, and Tyr871 and Tyr925 in the carboxy-terminal region of FAK (6,7).

$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 PD-L1 (D8T4X) Rabbit mAb #86744.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Programmed cell death 1 ligand 1 (PD-L1, B7-H1, CD274) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses. The PD-L1 ligand binds the PD-1 transmembrane receptor and inhibits T cell activation. PD-L1 was discovered following a search for novel B7 protein homologs and was later shown to be expressed by antigen presenting cells, activated T cells, and tissues including placenta, heart, and lung (1-3). Similar in structure to related B7 family members, PD-L1 protein contains extracellular IgV and IgC domains and a short, cytoplasmic region. Research studies demonstrate that PD-L1 is expressed in several tumor types, including melanoma, ovary, colon, lung, breast, and renal cell carcinomas (4-6). Expression of PD-L1 in cancer is associated with tumor infiltrating lymphocytes, which mediate PD-L1 expression through the release of interferon gamma (7). Additional research links PD-L1 expression to cancers associated with viral infections (8,9).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Sox9 (D8G9H) Rabbit mAb #82630.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Sox9 is a transcription factor with an HMG-box DNA binding domain that has homology to the HMG domain of the mammalian testis-determining factor, SRY (1). Sox9 regulates several important processes during embryonic development including chondrogenesis, during which it contributes to skeletal formation and digit specification (2,3). Sox9 also coordinates with steroidogenic factor-1 to direct Sertoli cell-specific expression of anti-Mullerian hormone during embryogenesis, thereby contributing to male sex determination (4). In addition, Sox9 is reportedly involved in the maintenance of adult stem cell populations, including multipotent neural stem cells (5), hair follicle stem cells (6), and mammary stem cells (7). Recent interest has focused on the role of Sox9 in tumor biology. For example, research studies have shown that Sox9 expression in lung adenocarcinoma induces a mesenchymal phenotype in tumor cells (8). Other research studies have shown that YAP1 induced upregulation of Sox9 confers cancer stem cell like properties on esophageal cancer cells (9). Moreover, Sox9 expression has been linked with several other tumor types including ovarian, prostate, and pancreatic malignancies (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors, and adhesion molecules (1). Among the family members, MMP-2, MMP-3, MMP-7, and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (2-4). Research studies have shown that MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: SS18 is a protein that has been shown to be a part of the SWI/SNF complex (1, 2). The SS18-SSX fusion proteins are a result of in-frame fusions that fuse the SS18 gene on chromosome 18 with X chromosome genes SSX1, SSX2, and to a lesser extent SSX4 (3). Human synovial sarcoma (SS) accounts for 8-10% of all soft tissue malignancies and 95% of these malignancies express the recurrent translocation of the SS18 gene on chromosome 18 (3). The N-terminal SNH domain (SYT N-terminal homology domain) of the SS18 protein interacts with SWI/SNF chromatin remodeling complexes via the N terminal region of BRM and BRG1 subunits (4). Studies of the SS18-SSX fusion in SS suggest that endogenous SS18 competes with the mutant SS18-SSX fusion for occupancy in the SWI/SNF complexes resulting in the displacement of SNF5 (BAF47) subunit. Displacement of the SNF5 subunit results in altered function of the SWI/SNF complex that leads to deregulated expression of genes such as Sox2 in SS (3).

$348
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 RING1B (D22F2) XP® Rabbit mAb #5694.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell-cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, Eed-Ezh2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyltransferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Methylation of Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinates histone H2A on Lys119 (6). PRC1 is composed of Bmi1 and RING1A (also RING1 or RNF1), both of which act to enhance the E3 ubiquitin ligase activity of an additional catalytic subunit RING1B (also RING2 or RNF2) (7). PcG proteins play an important role in the regulation of cell proliferation and senescence through repression of the p16 INK4A and p19 ARF genes and are required for maintenance of adult hematopoietic and neural stem cells, as well as embryonic stem cells (3,4,8-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: SH2 domain-containing leukocyte protein of 76 kDa (SLP-76) is a hematopoietic adaptor protein that is important in multiple biochemical signaling pathways and necessary for T cell development and activation (1). ZAP-70 phosphorylates SLP-76 and LAT as a result of TCR ligation. SLP-76 has amino-terminal tyrosine residues followed by a proline rich domain and a carboxy-terminal SH2 domain. Phosphorylation of Tyr113 and Tyr128 result in recruitment of the GEF Vav and the adapter protein Nck (2). TCR ligation also leads to phosphorylation of Tyr145, which mediates an association between SLP-76 and Itk, which is accomplished in part via the proline rich domain of SLP-76 and the SH3 domain of ITK (3). Furthermore, the proline rich domain of SLP-76 binds to the SH3 domains of Grb2-like adapter Gads (3,4). In resting cells, SLP-76 is predominantly in the cytosol. Upon TCR ligation, SLP-76 translocates to the plasma membrane and promotes the assembly of a multi-protein signaling complex that includes Vav, Nck, Itk and PLCγ1 (1). The expression of SLP-76 is tightly regulated; the protein is detected at very early stages of thymocyte development, increases as thymocyte maturation progresses, and is reduced as cells mature to CD4+ CD8+ double-positive thymocytes (5).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated ASC (D2W8U) Rabbit mAb (Mouse Specific) #67824.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: TMS1 (target of methylation-induced silencing)/ASC (apoptosis-associated speck-like protein containing a CARD), also referred to as PYCARD and CARD5, is a 22-kDa pro-apoptotic protein containing an N-terminal pyrin domain (PYD) and a C-terminal caspase recruitment domain (CARD) (1-2). The ASC/TMS1 gene was originally found to be aberrantly methylated and silenced in breast cancer cells (2), and has since been found to be silenced in a number of other cancers, including ovarian cancer (3), glioblastoma (4), melanoma (5), gastric cancer (6), lung cancer (7), and prostate cancer (8). Expression of ASC/TMS1 can be induced by pro-apoptotic/inflammatory stimuli (9). During apoptosis ASC/TMS1 is re-distributed from the cytosol to the mitochondria and associates with mitochondrial Bax to trigger cytochrome c release and subsequent apoptosis (10). ASC/TMS1 has also been found to be a critical component of inflammatory signaling where it associates with and activates caspase-1 in response to pro-inflammatory signals (11).

The Autophagy Vesicle Nucleation Antibody Sampler Kit provides an economical means of detecting target proteins involved in autophagosome formation and maturation. The kit contains enough antibody to perform two western blot experiments per primary antibody.
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Argininosuccinate synthetase (ASS1) catalyzes the formation of argininosuccinate from citrulline and aspartate, the rate-limiting step in the urea cycle that is responsible for the synthesis of arginine and the clearance of nitrogenous waste (1). ASS1 is ubiquitously and differentially expressed in different cell types and tissues. Mutations in ASS1 are associated with citrullinemia type I, an autosomal recessive disease characterized primarily by elevated serum and urine citrulline levels in human patients (2, 3).Loss of ASS1 expression is one of the common metabolic alterations observed in many cancers, and it is a prognostic biomarker of reduced metastasis-free survival. ASS1 deficiency leads to the dependence of extracellular arginine for survival, proliferation, and cell growth. Ariginine starvation induces autophagy and apoptosis in ASS1 deficient cells and this has been exploited as a therapeutic intervention for the tumors with loss of ASS1 expression (4, 5). Pegylated arginine deiminase (ADI-PEG20), an enzyme that degrades arginine into citrulline, causes significant growth inhibition in tumors that have lost ASS1 expression, such as hepatocellular carcinoma, breast cancer, and sarcoma (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: P2X purinergic receptors are ATP-gated ion channels involved in physiological processes that include inflammation, afferent sensory signaling, and sympathetic motor nerve activity. Seven different vertebrate genes (P2RX1-P2RX7) encode for individual receptor protein subunits (1). All P2X subunit proteins share similar protein domain structure, but can differ in overall protein length from 384 to 595 amino acids. Each P2X subunit is composed of amino- and carboxy-terminal intracellular domains, two transmembrane domains, and a large extracellular loop that contains ten evenly spaced cysteines and multiple glycosylation sites (2). P2X receptors are found in a variety of cell types and tissues, including central and peripheral nervous system neurons and glial cells, autonomic and sensory neurons, bone, muscle, and hematopoietic tissues (1).

$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 HSP90 (C45G5) Rabbit mAb #4877.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Bone morphogenetic proteins (BMPs) were first identified as molecules that can induce ectopic bone and cartilage formation (1,2). BMPs belong to the TGF-β superfamily, playing many diverse functions during development (3). BMPs are synthesized as precursor proteins and then processed by cleavage to release the C-terminal mature BMP. BMPs initiate signaling by binding to a receptor complex containing type I and type II serine/threonine receptor kinases that then phosphorylate Smad (mainly Smad1, 5, and 8), resulting in the translocation of Smad into the nucleus. BMP was also reported to activate MAPK pathways in some systems (3,4).

$305
400 µl
This Cell Signaling Technology (CST) antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. It is useful for the immunoprecipitation of DYKDDDDK-tagged proteins. CST expects that DYKDDDDK Tag (D6W5B) Rabbit mAb (Binds to same epitope as Sigma's Anti-Flag® M2 Antibody) (Sepharose® Bead Conjugate) will display the same species cross-reactivity as the unconjugated antibody DYKDDDDK Tag (D6W5B) Rabbit mAb # 14793.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunoprecipitation

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

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

Background: Translocator protein (TSPO) is an 18 kDa mitochondrial drug- and cholesterol-transporting protein involved in steroid hormone synthesis and mitochondrial homeostasis in a variety of cell types (1,2). Originally thought to play a role exclusively in steroid synthesis in steroidogenic cells, subsequent research studies have implicated TSPO in a variety of pathologies in a broad range of tissues including progression of breast cancer, neuroinflammation, and neurological disorders (1,3-5). TSPO was first identified by its ability to bind benzodiazepines in peripheral tissues and glial cells, hence its alternate name Peripheral Benzodiazepine Receptor (PBR).TSPO has been shown to modulate an array of cellular functions; it is critical for steroidogenesis, modulates mitochondrial function and metabolism, and plays a role in both cell proliferation and apoptosis (6-8). TSPO is found in the outer mitochondrial membrane where it coordinates with Steroidogenic Acute Regulatory Factor (StAR) to transport cholesterol into the mitochondria and is critical for steroidogenesis and tumor progression (9,10). This is illustrated by studies that show the non-aggressive, hormone-dependent cell line, MCF7, expresses low levels of TSPO whereas the more aggressive, metastatic, and hormone-independent cell line, MDA-MB-231, expresses high levels of TSPO (10). This study, and others, suggest that TSPO may be an important regulator of hormone-dependent tumor progression. Numerous investigations have concluded that due to its high affinity for pharmacological compounds and up-regulation in disease, TSPO is an attractive target for diagnosis and treatment of tumor progression, neuroinflammation, neurodegeneration, and neurological/psychiatric disorders (11-15).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: CAD is essential for the de novo synthesis of pyrimidine nucleotides and possesses the following enzymatic activities: glutamine amidotransferase, carbamoyl-phosphate synthetase, aspartate transcarbamoylase, and dihydroorotase. Thus, the enzyme converts glutamine to uridine monophosphate, a common precursor of all pyrimidine bases, and it is necessary for nucleic acid synthesis (1). In resting cells, CAD is localized mainly in the cytoplasm where it carries out pyrimidine synthesis. As proliferating cells enter S phase, MAP Kinase (Erk1/2) phosphorlyates CAD at Thr456, resulting in CAD translocation to the nucleus. As cells exit S phase, CAD is dephosphorylated at Thr456 and phosphorylated at Ser1406 by PKA, returning the pathway to basal activity (2). Various research studies have shown increased expression of CAD in several types of cancer, prompting the development of pharmacological inhibitors such as PALA. Further studies have identified CAD as a potential predictive early marker of prostate cancer relapse (3).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin)

Background: Cluster of Differentiation 8 (CD8) is a disulphide-linked heterodimer consisting of the unrelated α and β subunits. Each subunit is a glycoprotein composed of a single extracellular Ig-like domain, a polypeptide linker, a transmembrane part and a short cytoplasmic tail. On T cells, CD8 is the coreceptor for the T cell receptor (TCR), and these two distinct structures recognize the Antigen–Major Histocompatibility Complex (MHC). Specifically, the Ig-like domain of CD8α interacts with the α3-domain of the MHC class I molecule. CD8 ensures specificity of the TCR–antigen interaction, prolongs the contact between the T cell and the antigen presenting cell, and the α chain recruits the tyrosine kinase Lck, which is essential for T cell activation (1).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: La-related protein 1 (LARP1) is a ubiquitously expressed RNA binding protein that promotes both global and specific mRNA translation in cells (1). LARP1 belongs to the La-related protein family and contains two RNA binding domains, a La motif (LAM), and a neighboring RNA recognition motif-like (RRM-L) domain (1). Research studies indicate that LARP1 acts downstream of mTORC1 to facilitate cell proliferation and growth by promoting global mRNA translation and translation of mRNAs containing a 5'Terminal Oligo-Pyrimidine (5'TOP) motif, which code for translational machinery components (2,3). At the molecular level, LARP1 associates with 5'TOP mRNAs and multiple translation machinery components to positively regulate translation (2,4). Additional studies show that LARP1 expression is upregulated in hepatocellular carcinoma (HCC) patients and that high LARP1 expression in HCC negatively correlates with survival rate (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The adducins (ADD) are cytoskeleton-associated proteins that help cap the ends of actin filaments, promote association between spectrin and actin, and participate in synapse assembly. The three closely related genes ADD1, ADD2, and ADD3 encode the α-adducin, β-adducin, and γ-adducin proteins (1). Research studies indicate that β-adducin is found at high levels in brain and hematopoietic tissues, whereas both α-adducin and γ-adducin are ubiquitously expressed (2). Adducin protein function is regulated by phosphorylation at a number of sites. Both PKA and PKC can phosphorylate α-adducin at Ser726 and β-adducin at Ser713, which inhibits calmodulin binding and adducin activity (3-5). Additionally, PKA (but not PKC) can phosphorylate β-adducin at Ser408, Ser436, and Ser481, which negatively affects spectrin-actin interactions (3). Phosphorylation of α-adducin at Thr445 and Thr480 by Rho-kinase regulates cell motility and membrane ruffling (6). Finally, CDK-1 phosphorylation of α-adducin at Ser12 and Ser355 during mitosis leads to association of α-adducin with the mitotic spindle, suggesting that α-adducin may play a role in mitotic regulation (7). Because α-adducin plays a role in regulating renal sodium reabsorption, it is not surprising that a number of studies show a relationship between ADD1 genetic polymorphisms and the development of hypertension (8-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Chromatin IP, Chromatin IP-seq, 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).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Notch signaling is activated upon engagement of the Notch receptor with its ligands, the DSL (Delta, Serrate, Lag2) proteins of single-pass type I membrane proteins. The DSL proteins contain multiple EGF-like repeats and a DSL domain that is required for binding to Notch (1,2). Five DSL proteins have been identified in mammals: Jagged1, Jagged2, Delta-like (DLL) 1, 3 and 4 (3). Ligand binding to the Notch receptor results in two sequential proteolytic cleavages of the receptor by the ADAM protease and the γ-secretase complex. The intracellular domain of Notch is released and then translocates to the nucleus where it activates transcription. Notch ligands may also be processed in a way similar to Notch, suggesting a bi-directional signaling through receptor-ligand interactions (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CBP (CREB-binding protein) and p300 are highly conserved and functionally related transcriptional co-activators that associate with transcriptional regulators and signaling molecules, integrating multiple signal transduction pathways with the transcriptional machinery (1,2). CBP/p300 also contain histone acetyltransferase (HAT) activity, allowing them to acetylate histones and other proteins (2). Phosphorylation of p300 at Ser89 by PKC represses its transciptional acitivity, and phosphorylation at the same site by AMPK disrupts the association of p300 with nuclear receptors (3,4). Ser1834 phosphorylation of p300 by Akt disrupts its association with C/EBPβ (5). Growth factors induce phosphorylation of CBP at Ser437, which is required for CBP recruitment to the transcription complex (6). CaM kinase IV phosphorylates CBP at Ser302, which is required for CBP-dependent transcriptional activation in the CNS (7). The role of acetylation of CBP/p300 is of particular interest (2,8). Acetylation of p300 at Lys1499 has been demonstrated to enhance its HAT activity and affect a wide variety of signaling events (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Heme oxygenase (HO) is the rate-limiting enzyme in the catabolism of heme that results in the release of carbon monoxide, iron, and biliverdin (1). The products of this enzymatic reaction play important biological roles in antioxidant, anti-inflammatory and cytoprotective functions (2). Heme oxygenase comprises two isozymes, including the constitutively expressed HO-2 isozyme and the inducible HO-1 isozyme (3). Inducible HO-1 is expressed as an adaptive response to several stimuli, including heme, metals, and hormones (4). The induction of HO-1 has been implicated in numerous disease states, such as transplant rejection, hypertension, atherosclerosis, Alzheimer disease, endotoxic shock, diabetes, inflammation, and neurological disorders (1,5).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: F4/80 (EMR1) is a heavily glycosylated G-protein-coupled receptor and is a well-established marker for mouse macrophages (1-3). Expression of F4/80 has also been observed in microglia and subset populations of dendritic cells (4).

$364
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 and immunofluorescence analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Non-phospho (Active) β-Catenin (Ser45) (D2U8Y) XP® Rabbit mAb #19807.
APPLICATIONS
REACTIVITY
Dog, Human, Monkey, Mouse, Rat, Zebrafish

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$180
1 ml
$676
5 x 1ml
5 ml
Protein G Magnetic Beads are an affinity matrix for the small-scale isolation of immunocomplexes from immunoprecipitations (IP assays). Protein G is covalently coupled to a magnetic particle.Protein G exhibits high affinity for subclasses of IgG from many species (including human, rabbit, mouse, rat, and sheep) and can be used for immunoprecipitation assays with these antibodies. Beads can be separated from solution using our 6-Tube Magnetic Separation Rack #7017 or 12-Tube Magnetic Separation Rack #14654 which concentrates the beads to the side of the tube instead of the bottom. This eliminates centrifugation steps, minimizes sample loss, increases washing efficiency, and saves time.The 1mL and 5mL size is enough material for 25 and 125 immunoprecipitations, respectively, when following our recommended protocol.Product Specifications: Bead Diameter: ~1.5 μmBinding Capacity: > 0.2 μg Rabbit IgG/μl bead slurry
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunoprecipitation