Microsize antibodies for $99 | Learn More >>

Product listing: γ-Catenin (D9M1Q) Rabbit mAb, UniProt ID P14923 #75550 to VPS29 (D2H7G) Rabbit mAb, UniProt ID Q9UBQ0 #73540

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Also known as plakoglobin, γ-catenin is a member of the Armadillo family of signaling molecules, which includes β-catenin and the Drosophila protein armadillo (1). This family of proteins is involved in Wnt signaling, which is important in embryonic development and in tumorigenesis (2-3). Although the two vertebrate proteins β- and γ-catenin display sequence homology, γ-catenin likely plays a role distinct from that of β-catenin (1, 4-6). γ-catenin localizes to desmosomes and adherens junctions, both sites of intercellular adhesion, and interacts with the cytoplasmic domains of classical and desmosomal cadherins. Interaction of γ- or β-catenin with α-catenin, desmoplakin and other junction proteins provides a link between intercellular junctions and the actin and intermediate filament cytoskeleton. Maintenance and/or modification of this link is vital for control of cell adhesion and migration (1). γ-catenin is modified by phosphorylation, affecting both adhesion and β-catenin dependent transcription (7), and by and O-glycosylation, affecting adhesion (8). Recent evidence suggests that γ-catenin regulates desmosomal adhesion in response to growth factor stimulation (9).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-4 is expressed by dendritic cells and macrophages (1). Like TIM-1, TIM-4 is a receptor for phosphatidylserine (2). Interaction of TIM-4 with phosphatidylserine exposed by cells undergoing apoptosis leads to uptake of apoptotic cells (2,3). In this way, TIM-4 regulates adaptive immunity by removing apoptotic antigen-specific T cells following clearance of infection. Peritoneal macrophages from mice deficient in TIM-4 fail to effectively clear apoptotic cells leading to hyperactive T and B cells and autoimmunity (4). In addition, TIM-4 expressed by tumor-associated macrophages and dendritic cells leads to autophagy-mediated degradation of dying tumor cells, resulting in reduced antigen presentation and T cell responses (5). TIM-4 was also identified as a ligand for TIM-1, and interaction between these proteins regulates T cell proliferation (1). Finally, TIM-4 is expressed by a subset of proinflammatory B cells that produce IFN-γ and promote Th1 cell differentiation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Oct-4 (POU5F1) is a transcription factor highly expressed in undifferentiated embryonic stem cells and embryonic germ cells (1). A network of key factors that includes Oct-4, Nanog, and Sox2 is necessary for the maintenance of pluripotent potential, and downregulation of Oct-4 has been shown to trigger cell differentiation (2,3). Research studies have demonstrated that Oct-4 is a useful germ cell tumor marker (4). Oct-4 exists as two splice variants, Oct-4A and Oct-4B (5). Recent studies have suggested that the Oct-4A isoform has the ability to confer and sustain pluripotency, while Oct-4B may exist in some somatic, non-pluripotent cells (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Ectonucleotide pyrophosphatase/phosphodiesterase 3 (ENPP3/CD203c/PD-Ιbeta) is a type-II transmembrane glycoprotein that contains a large extracellular domain, an α-helical transmembrane segment, and a short cytoplasmic domain containing the N-terminus. ENPP3 has been shown to be overexpressed in colon carcinoma and is thought to play a role in tumor initiation and tumor cell invasiveness (1-3). Within the hematopoietic cell compartment, ENPP3 is a cell surface marker of basophil and mast cell lineages (4,5). Indeed, ENPP3 is overexpressed on transformed mast cells in patients with systemic mastocytosis (6). Recently, ENPP3 has been identified as being highly overexpressed in renal cell carcinoma (RCC) and may have potential as a novel therapeutic target for this disease (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: BCL11A is a zinc finger-containing transcriptional repressor that is important for normal hematopoiesis (1). Alternative splicing of the BCL11A transcript results in several isoforms of the protein (2). BCL11A is required for the early stages of B lineage commitment and mice lacking BCL11A fail to develop B cells (1). Mice deficient in BCL11A also fail to develop plasmacytoid dendritic cells (3). In addition, BCL11A regulates the switch from fetal to adult hemoglobin by repressing expression of fetal hemoglobin in adult erythroid cells (4). Since expression of fetal hemoglobin can decrease the severity of hemoglobin disorders in adults, BCL11A is a potential therapeutic target for these diseases (4). BCL11A was also recently identified as a component of the mammalian SWI/SNF complex (5). BCL11A is required for morphogenesis and terminal differentiation of dorsal spinal neurons (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Modulation of chromatin structure plays a critical role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure (1). There are five major variants of histone H2A: canonical H2A (most abundant), H2A.X, MacroH2A, H2ABbd and H2A.Z (2). Histone H2A.Z, the most conserved variant across species, functions as both a positive and negative regulator of transcription and is important for chromosome stability (2). Several homologous protein complexes, such as SWR-C (S. cerevisiae), TIP60 (D. melanogaster) and SRCAP (mammals), have been shown to catalyze the ATP-dependent exchange of H2A.Z for H2A in the nucleosome (3,4,5). This exchange of histone H2A variants changes histone-histone interactions in the nucleosome core and alters an acidic patch on the surface of the nucleosome, resulting in changes in nucleosome stability and binding of non-histone proteins such as HP1α (6,7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CD14 is a leucine-rich repeat-containing pattern recognition receptor with expression largely restricted to the monocyte/macrophage cell lineage (1). Research studies have shown that CD14 is a bacterial lipopolysaccharide (LPS) binding glycoprotein, expressed as either a GPI-linked membrane protein or a soluble plasma protein (2). LPS induces an upregulation of GPI-linked CD14 expression, which facilitates TLR4 signaling and macrophage activation in response to bacterial infection (3-5).

$327
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 Phospho-p44/42 MAPK (Erk1) (Tyr204)/(Erk2) (Tyr187) (D1H6G) Mouse mAb #5726.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs, such as cell proliferation, differentiation, motility, and death. The p44/42 MAPK (Erk1/2) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines (1-3), and research investigators consider it an important target in the diagnosis and treatment of cancer (4). Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK or MAP3K), a MAP kinase kinase (MAPKK or MAP2K), and a MAP kinase (MAPK). Multiple p44/42 MAP3Ks have been identified, including members of the Raf family, as well as Mos and Tpl2/COT. MEK1 and MEK2 are the primary MAPKKs in this pathway (5,6). MEK1 and MEK2 activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187, respectively. Several downstream targets of p44/42 have been identified, including p90RSK (7) and the transcription factor Elk-1 (8,9). p44/42 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases, known as DUSPs or MKPs (10), along with MEK inhibitors, such as U0126 and PD98059.

$263
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to PerCP-Cy5.5® and tested in-house for direct flow cytometry analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Members of the Janus family of tyrosine kinases (Jak1, Jak2, Jak3, and Tyk2) are activated by ligands binding to a number of associated cytokine receptors (1). Upon cytokine receptor activation, Jak proteins become autophosphorylated and phosphorylate their associated receptors to provide multiple binding sites for signaling proteins. These associated signaling proteins, such as Stats (2), Shc (3), insulin receptor substrates (4), and focal adhesion kinase (FAK) (5), typically contain SH2 or other phospho-tyrosine-binding domains.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Diffuse intrinsic pontine glioma (DIPG) is an aggressive brainstem astrocyte tumor arising mostly in children, leading to a long-term survival rate of less than 10%. Multiple whole-genome sequencing studies of DIPG patients identified commonly occurring mutations in the H3F3A gene encoding histone H3.3. One of these mutations, a lysine to methionine amino acid substitution (K27M), is found in up to 78% of DIPGs and 22% of non-brainstem pediatric gliomas (1-3). This mutation is associated with poor prognosis, with a mean survival time of 0.73 years for patients with the K27M mutation versus 4.6 years for patients without the mutation (1-3). Expression of the K27M mutant histone H3 is accompanied by a dramatic reduction in the levels of polycomb repressive complex 2 (PRC2)-mediated trimethylation of histone H3, changes in the distribution of PRC2 on the genome, and altered expression of genes associated with various cancer pathways (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Sigma non-opioid intracellular receptor 1 (SIGMAR1) is an endoplasmic reticulum (ER) membrane chaperone that forms raft-like microdomains on the ER, where it interacts with mitochondria at the mitochondria-associated ER membrane domain (MAM). At MAM, SIGMAR1 maintains proper ER-mitochondrion Ca2+ signaling, regulates mitochondria function, and enhances cellular survival upon ER stress (1-4). When activated, SIGMAR1 translocates to ER and plasma membrane, where it interacts with a plethora of membrane proteins, including ion channels, neurotransmitter receptors, and kinases. SIGMAR1 also modulates a variety of neuronal functions, such as neuronal excitability, neuroplasticity, neuroprotection, and neurorestoration (5-7). SIGMAR1 binds to many anti-psychotic drugs and it is implicated in addiction, pain, neurodegenerative diseases, and depression (8-11). Recently, mutations in the SIGMAR1 gene have been reported to be associated with amyotrophic lateral sclerosis (12,13). Besides its important roles in central nervous system and peripheral nervous system, SIGMAR1 also enhances cancer cell migration and invasion (14,15).

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

Application Methods: Chromatin IP, Western Blotting

Background: Reptin/RuvBL2 and Pontin/RuvBL1 are closely related members of the AAA+ (ATPase associated with diverse cellular activities) superfamily of proteins, and are putatively homologous to bacterial RuvB proteins that drive branch migration of Holliday junctions (1). Reptin and Pontin function together as essential components of chromatin remodeling and modification complexes, such as INO80, TIP60, SRCAP, and Uri1, which play key roles in regulating gene transcription (1,2). In their capacity as essential transcriptional co-regulators, Reptin and Pontin have both been implicated in oncogenic transformations, including those driven by c-Myc, β-catenin, and E1A (2-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Kv4.2 is a voltage-gated potassium channel that belongs to the Shal-related subfamily. Kv4.2 mediates K+ transport in excitable membranes primarily in the brain, where it regulates neuronal excitability, synaptic plasticity, and the circadian rhythm of locomotor activity (1-6). In rodent heart, Kv4.2 mediates the transient outward current (Ito), which contributes to early repolarization and the cardiac action potential (7). Kv4.2 can form homotetramers or heterotetramers with other members of the Shal-related subfamily. Interaction with modulating β subunits such as KChIP family proteins modulates Kv4.2 expression at cell surface and its channel activity (8-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Transducing β-like protein 1 (TBL1X/TBL1) and TBL1-related protein 1 (TBL1XR1/TBLR1) were originally identified as subunits of the co-repressor silencing mediator for retinoic and thyroid hormone receptor (SMRT) and nuclear receptor co-repressor (NCoR) complexes (1-3). These two factors are required for the exchange of co-repressor complexes for co-activators by acting as adaptors to recruit the ubiquitin/proteasome machinery that degrades the co-repressor proteins during ligand mediated activation of transcription (4,5). Co-factor exchange driven by TBL1X/TBL1 and TBL1XR1/TBLR1 appears to be the mechanism by which c-Jun and NF-κB mediated transcription is activated and is therefore likely to be the mechanism employed by other signal-dependent transcription factors as well (4,6). In addition, both TBL1X/TBL1 and TBL1XR1/TBLR1 have essential roles in regulating the Wnt-signaling pathway by recruiting β-catenin to Wnt target genes to activate transcription. Depletion of TBL1X-TBL1XR1 significantly inhibited Wnt-beta-catenin- induced gene expression and oncogenic growth in vitro and in vivo (7). Research studies have shown that upregulation of TBL1XR/TBLR1 is observed in a variety of solid tumors, and is correlated with advanced tumor stage, metastasis and poor prognosis (1).

$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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EpCAM (D4K8R) XP® Rabbit mAb #36746.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$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 SP1 (D4C3) Rabbit mAb #9389.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

Background: Specificity protein 1 (SP1) is a ubiquitously expressed transcription factor belonging to the family of C2H2-type zinc finger containing DNA-binding proteins. SP1 binds GC-rich motifs with high affinity and regulates the expression of numerous mammalian genes (1,2). It interacts with many other transcription factors, such as c-Myc, EGR1, and Stat1, and with basal transcription machinery components. SP1 interacts with chromatin-modifying factors, such as histone deacetylases (HDACs) and p300 in chromatin remodeling. Transcriptional activity and stability of SP1 are regulated by post-translational modification, including phosphorylation, acetylation, ubiquitination, and glycosylation (3). Glycosylation of SP1 following insulin treatment leads to increased nuclear localization, while glucagon treatment increases cytoplasmic SP1 levels (4-6). Investigators have found high levels of SP1 in patients with Alzheimer's disease (7).

$285
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to violetFluor™ 450 and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The protein phosphatase (PTP) receptor CD45 is a type I transmembrane protein comprised of a pair of intracellular tyrosine phosphatase domains and a variable extracellular domain generated by alternative splicing (1). The catalytic activity of CD45 is a function of the first phosphatase domain (D1) while the second phosphatase domain (D2) may interact with and stabilize the first domain, or recruit/bind substrates (2,3). CD45 interacts directly with antigen receptor complex proteins or activates Src family kinases involved in the regulation of T- and B-cell antigen receptor signaling (1). Specifically, CD45 dephosphorylates Src-family kinases Lck and Fyn at their conserved negative regulatory carboxy-terminal tyrosine residues and upregulates kinase activity. Conversely, studies indicate that CD45 can also inhibit Lck and Fyn by dephosphorylating their positive regulatory autophosphorylation site. CD45 appears to be both a positive and a negative regulator that conducts signals depending on specific stimuli and cell type (1). Human leukocytes including lymphocytes, eosinophils, monocytes, basophils, and neutrophils express CD45, while erythrocytes and platelets are negative for CD45 expression (4).

$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 Estrogen Receptor α (D6R2W) Rabbit mAb #13258.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Estrogen receptor α (ERα), a member of the steroid receptor superfamily, contains highly conserved DNA binding and ligand binding domains (1). Through its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively), ERα regulates transcription by recruiting coactivator proteins and interacting with general transcriptional machinery (2). Phosphorylation at multiple sites provides an important mechanism to regulate ERα activity (3-5). Ser104, 106, 118, and 167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serine residues plays an important role in regulating ERα activity. Ser118 may be the substrate of the transcription regulatory kinase CDK7 (5). Ser167 may be phosphorylated by p90RSK and Akt (4,6). According to the research literature, phosphorylation at Ser167 may confer tamoxifen resistance in breast cancer patients (4).

The Exosomal Marker Antibody Sampler Kit provides an economical means to evaluate the presence of exosomal markers. The kit includes enough primary antibody to perform two western blot experiments for each target.
$115
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: DNA Dot Blot, Immunofluorescence (Immunocytochemistry)

Background: Methylation of DNA at cytosine residues is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting, and mammalian development (1,2). 5-methylcytosine is a repressive epigenetic mark established de novo by two enzymes, DNMT3a and DNMT3b, and is maintained by DNMT1 (3, 4). 5-methylcytosine was originally thought to be passively depleted during DNA replication. However, subsequent studies have shown that Ten-Eleven Translocation (TET) proteins TET1, TET2, and TET3 can catalyze the oxidation of methylated cytosine to 5-hydroxymethylcytosine (5-hmC) (5). Additionally, TET proteins can further oxidize 5-hmC to form 5-formylcytosine (5-fC) and 5-carboxylcytosine (5-caC), both of which are excised by thymine-DNA glycosylase (TDG), effectively linking cytosine oxidation to the base excision repair pathway and supporting active cytosine demethylation (6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Members of the Janus family of tyrosine kinases (Jak1, Jak2, Jak3, and Tyk2) are activated by ligands binding to a number of associated cytokine receptors (1). Upon cytokine receptor activation, Jak proteins become autophosphorylated and phosphorylate their associated receptors to provide multiple binding sites for signaling proteins. These associated signaling proteins, such as Stats (2), Shc (3), insulin receptor substrates (4), and focal adhesion kinase (FAK) (5), typically contain SH2 or other phospho-tyrosine-binding domains.

The Matrix Remodeling Antibody Sampler Kit provides an economical means of detecting different MMPs and TIMPs using the specific corresponding antibodies. The kit contains enough antibody to perform at least two western blot experiments with each primary antibody.

Background: Matrix remodeling is mainly controlled by MMPs and TIMPs. The matrix metalloproteinase (MMP) family of proteases are a group of zinc-dependent enzymes that target extracellular proteins, including growth factors, cell surface receptors, adhesion molecules, matrix structural proteins, and other proteases (1, 2). Among the family members, MMP-2, MMP-3, MMP-7, MMP-9, and MMP14 (MT1-MMP) have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (3). MMP activity is regulated by mechanisms of both transcriptional control and post translational protein processing. Once synthesized, MMPs exist as latent proenzymes. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full-length protein (4). MMP activity can be inhibited through its binding to endogenously expressed TIMPs. TIMPs are members of the family of tissue inhibitors of matrix metalloproteinases that include TIMP1, TIMP2, TIMP3, and TIMP4. The main function of TIMPs is their inhibitory effect on MMPs. TIMPs irreversibly inactivate MMPs by direct binding MMPs and chelating their zinc cofactor at the catalytic site to inhibit the proteinase function (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Stomatin-like protein 2 (SLP-2 and also known as STOML2) is a lipid-anchored mitochondrial protein that is part of a large protein complex that regulates mitochondrial biogenesis and function. Proteomic studies identified SLP-2 as a widely expressed mitochondria-enriched protein (1). As a member of both the stomatin family and stomatin-prohibitin-flotillin-HfLC/K (SPFH) superfamily of proteins, SLP-2 forms large hetero-oligomeric complexes with other mitochondrial proteins, including prohibtin, mitofusin 2, and cardiolipin (2, 3). SLP-2 contains a highly conserved SPFH domain that mediates its ability to associate with the mitochondrial inner membrane and form specialized membrane microdomains. As an inner membrane organizer of other mitochondrial proteins, SLP-2 performs multiple mitochondrial functions, including regulation of mitochondrial biogenesis, energy/calcium homeostasis, translation, and mitochondrial-mediated cellular stress responses (3, 4, 5, 6, 7, 8). Enhanced SLP-2 expression is also associated with several human cancers, including gallbladder, rectal, and gastric cancer (9, 10, 11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytochrome P450 2D6 (CYP2D6) is a member of the cytochrome P450 superfamily of enzymes. CYP2D6 is located in the endoplasmic reticulum where it oxidizes substrates such as drugs and environmental chemicals (1,2). CYP2D6 metabolizes more than 25% of current commonly used drugs including antidepressants, antipsychotics, analgesics, beta-adrenergic blocking agents, antiarrythmics, and antiemetics. The CYP2D6 gene is highly polymorphic in humans, resulting in phenotypes that vary from poor metabolizer to super metabolizer. A patient's CYP2D6 genotype was shown to be a good predictor of drug response and side effects and is thus used to guide treatments (3-5). Although abundantly expressed in liver, CYP2D6 is also expressed in other organs including brain. In brain, CYP2D6 and other CYP family members are expressed in a cell-specific, region-specific manner (6-8). CYP2D6 functions as a neuroprotective enzyme that increases with age and is induced by nicotine and alcohol (9,10).

$180
1 ml
$676
5 x 1ml
5 ml
Protein A Magnetic Beads are an affinity matrix for the small-scale isolation of immunocomplexes from immunoprecipitations (IP assays). Protein A is covalently coupled to a magnetic particle.Protein A 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

Application Methods: Immunoprecipitation

$489
96 assays
1 Kit
The PathScan® Total CD31 (PECAM-1) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of CD31 (PECAM-1) protein. A CD31 (PECAM-1) mouse mAb has been coated onto the microwells. After incubation with cell lysates, the CD31 (PECAM-1) proteins are captured by the coated antibody. Following extensive washing, a CD31 (PECAM-1) biotinylated detection mAb is added to detect captured CD31 (PECAM-1) proteins. HRP-linked Streptavidin is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of absorbance for the developed color is proportional to the quantity of CD31 (PECAM-1) protein.Antibodies in the kit are custom formulations specific to the kit.
REACTIVITY
Human

Background: CD31 (Platelet Endothelial Cell Adhesion Molecule-1: PECAM-1), a member of the Ig superfamily of cell adhesion molecules, is expressed by circulating platelets, monocytes, neutrophils, some T cells, and endothelial cells and modulates cell adhesion, endothelial cell migration, and angiogenesis (1). CD31 is phosphorylated on Tyr686 at the cytoplasmic carboxy-terminal tail upon various stimuli (e.g. mechanical or oxidative stress), presumably by Src family members (2). The tyrosine phosphorylation mediates associations with a number of SH2 domain-containing binding partners such as PI3 kinase, SHIP, PLCγ, and SHP-2. Thus, CD31 serves as a scaffold for various signaling molecules (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The type I interferon (IFN) family includes IFN-β1 and IFN-α1 through IFN-α13 in humans and IFN-α1 through IFN-α14 in mice. Type I IFN is produced following detection of pathogen-associated molecular patterns (PAMPs) and is important for induction of antiviral genes, activation of dendritic cells, and initiation of adaptive immunity (1, 2). Type I IFNs signal through the IFN alpha receptor (IFNAR), which is a heterodimer composed of IFNAR1 and IFNAR2. Activation of IFNAR leads to formation of the nuclear complex IFN-stimulated gene factor 3 (ISGF3), which consists of STAT1, STAT2, and IRF-9 (3, 4). ISGF3 binds to IFN-stimulated response elements (ISREs) to initiate transcription of interferon-stimulated genes (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Integrins are transmembrane glycoproteins that form heterodimers consisting of one α and one β subunit. Integrin dimers act as receptors for extracellular matrix proteins and cell-surface ligands. Integrin signaling to (inside-out) and from (outside-in) extracellular molecules regulates multiple cellular processes, such as development, wound healing, immune response, invasion, metastasis, and angiogenesis (1,2). Integrin β2 (CD18) is the β subunit of the leukocyte-specific integrin family. Leukocyte integrins include Integrin β2 (CD18)/αL (CD11a) (LFA-1, lymphocyte function associated antigen 1), Integrin β2 (CD18)/αM (CD11b) (Mac-1), Integrin β2(CD18)/αX (CD11c), and Integrin β2 (CD18)/αD (CD11d). These integrins bind to immunoglobulin superfamily members, such as ICAM-1 and VCAM-1 on endothelial cells, to mediate firm adhesion and transendothelial migration of leukocytes (3). Integrin β2 (CD18) deficiency results in LAD (leukocyte adhesion deficiency), a disease characterized by impairment of leukocyte recruitment resulting in inability to fight infection (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Retromer is a heteropentameric protein complex that consists of two protein compounds, a sortin-nexin dimer and a trimeric VPS26-VPS29-VPS35 protein subcomplex. The retromer complex associates with endosomes at their cytosolic side to mediate retrograde transport of transmembrane proteins from endosomes to the trans-Golgi network (1-3). Vacuolar protein sorting-associated protein 29 (VPS29) is considered a cryptic metallophosphoesterase, as it contains a conserved metallophosphoesterase-fold that includes a phenylalanine in place of an essential histidine residue within the active site (4). While VPS29 is capable of binding metal ions, it does so with low affinity and exhibits no enzymatic activity. Instead, VPS29 serves as a scaffold protein that interacts with the carboxy-terminal region of VPS35 and is essential for association of the retromer with other endosomal transport proteins (5).