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Product listing: Histone H3 (K36M Mutant Specific) Antibody, UniProt ID P84243 #26218 to FastScan™ Total TREM2 ELISA Kit, UniProt ID Q9NZC2 #23831

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Chondroblastoma is a rare type of benign tumor that is found at the rounded ends of the long bones in the arms and legs. More than 90% of chondroblastomas have been found to contain a heterozygous mutation in the H3F3A gene encoding the histone variant H3.3 (1). This mutation, a lysine to methionine amino acid substitution in codon 36 (K36M), inhibits at least two histone H3 lysine 36 methyltransferases, WHSC1 (MMSET) and SETD2, resulting in the reduction of global levels of histone H3 lysine 36 methylation (1). Chondrocytes containing the histone H3 K36M mutation exhibit several hallmarks of cancer cells, including increased ability to form colonies, resistance to apoptosis, and defects in differentiation. Reduction of global methylation levels in chondrocytes, resulting from the K36M mutation, contributes to tumorigenesis by altering the expression of cancer-associated genes. The histone H3 K36M mutation is also found to promote sarcomagenesis by impairing the differentiation of mesenchymal progenitor cells, resulting in undifferentiated sarcomas (2). The K36M mutation alters the histone methylation landscape, resulting in a genome-wide gain in histone H3 lysine 27 methylation and redistribution of polycomb respressive complex 1 and derepression of its target genes known to block mesenchymal differentiation. Finally, the histone H3 K36M mutation is also found in 13% of HPV-negative head and neck squamous cell carinomas, again contributing to tumorigenesis by altering global methylation levels of histone H3 lysine 36 (3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Pacific Blue™ fluorescent dye and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: FMS-related tyrosine kinase 3 (FLT3, also called Flk2), is a member of the type III receptor tyrosine kinase family, which includes c-Kit, PDGFR and M-CSF receptors. FLT3 is expressed on early hematopoietic progenitor cells and supports growth and differentiation within the hematopoietic system (1,2). FLT3 is activated after binding with its ligand FL, which results in a cascade of tyrosine autophosphorylation and tyrosine phosphorylation of downstream targets (3). The p85 subunit of PI3 kinase, SHP2, GRB2 and Shc are associated with FLT3 after FL stimulation (4-6). Tyr589/591 is located in the juxtamembrane region of FLT3 and may play an important role in regulation of FLT3 tyrosine kinase activity. Somatic mutations of FLT3 consisting of internal tandem duplications (ITDs) occur in 20% of patients with acute myeloid leukemia (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Extracellular Matrix (ECM) is a complex network of macromolecules that provides structural tissue support to cells in the basement membrane and interstitial matrix. It is composed of many molecules including proteins, glycoproteins, proteoglycans, and polysaccharides (1,2). One of the major proteins that comprises the ECM, and the human body, is collagen. Collagens are a large family of proteins. They are trimeric molecules comprised of three alpha polypeptide chains that form a triple helix structure that is characteristic of all collagens (3). The large family of collagens is divided into three sub groups: the fibrillar collagens, the non-fibril forming collagens, and the fibril-associated collagens. These sub groups differ in their structure and supramolecular assembly (3).Collagen11A1 (COL11A1) is a minor fibrillar collagen that is not normally expressed at high levels in most normal tissues with the exception of cartilage where it is expressed in high levels, and some other tissues/ organs, where it is expressed at a lower level (4). However, it has been reported that the expression of this molecule is correlated with advanced tumorigenic disease through meta analysis of data from multiple cancers, including ovarian, colon, breast, and lung (5). Additionally, it has also been associated with epithelial-mesenchymal transition (EMT) and metastasis (6,7). Cancer associated fibroblasts (CAFs) are typically the most abundant cell type in the stroma of many solid tumors. They are thought to contribute to ECM stiffness, which is ultimately thought to contribute to tumor growth and resistance to chemotherapeutic intervention. COL11A1 has been found to be elevated in CAFs and may contribute to chemotherapy resistance (8).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated GATA-3 (D13C9) XP® Rabbit mAb #5852.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: GATA proteins comprise a group of transcription factors that are related by the presence of conserved zinc finger DNA binding domains, which bind directly to the nucleotide sequence core element GATA (1-3). There are six vertebrate GATA proteins, designated GATA-1 to GATA-6 (3).

$169
100 µg
This Cell Signaling Technology antibody is conjugated to APC-Cy7® and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: Cluster of Differentiation 4 (CD4) is a glycoprotein composed of an amino-terminal extracellular domain (four domains: D1-D4 with Ig-like structures), a transmembrane part and a short cytoplasmic tail. CD4 is expressed on the surface of T helper cells, regulatory T cells, monocytes, macrophages and dendritic cells, and plays an important role in the development and activation of T cells. On T cells, CD4 is the co-receptor for the T cell receptor (TCR), and these two distinct structures recognize the Antigen–Major Histocompatibility Complex (MHC). Specifically, the D1 domain of CD4 interacts with the β2-domain of the MHC class II molecule. CD4 ensures specificity of the TCR–antigen interaction, prolongs the contact between the T cell and the antigen presenting cell and recruits the tyrosine kinase Lck, which is essential for T cell activation (1).

$249
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to redFluor™ 710 and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The human leukocyte antigen (HLA) system is a gene complex encoding the major histocompatibility complex (MHC) proteins in humans. These cell surface proteins are responsible for the regulation of antigen-specific immunity in humans. HLA genes are highly polymorphic, allowing them to fine-tune the adaptive immune response. HLAs corresponding to MHC class I (HLA-A, B, and C) present small peptide antigens from inside the cell, approximately 8 to 10 amino acids in length, to CD8+ T lymphocytes in order to activate a cytotoxic T cell response. HLAs corresponding to MHC class II (HLA-DP, DM, DO, DQ, and DR) present antigens from outside of the cell, approximately 15 to 24 residues in length, to CD4+ T-helper cells, which in turn secrete cytokines and stimulate B cells to produce antibodies to that specific antigen. HLAs corresponding to MHC class III encode components of the complement system (1,2).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: B cell linker protein (BLNK), also known as SLP-65 or BASH, is an adaptor molecule that plays key roles in B cell activation and B cell antigen receptor (BCR) engagement. BLNK acts at the interface between BCR-associated Syk and downstream signaling cascades (1,2). BLNK has multiple SH2 binding motifs (YXXP) at its amino terminus and an SH2 domain at its carboxy terminus. After BCR ligation, BLNK is phosphorylated by Syk at multiple YXXP motifs including Tyr72, Tyr84, Tyr96, and Tyr178 (1). These phosphorylated motifs provide docking sites for signaling molecules, such as BTK, PLCγ, and Vav. These signaling molecules bind to BLNK through their SH2 domains and together activate downstream signaling pathways (3,4). Through its SH2 domain, BLNK can also interact with tyrosine-phosphorylated targets, such as HPK1, thereby recruiting them to the BCR complex for signaling (5).

$139
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to FITC and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The human leukocyte antigen (HLA) system is a gene complex encoding the major histocompatibility complex (MHC) proteins in humans. These cell surface proteins are responsible for the regulation of antigen-specific immunity in humans. HLA genes are highly polymorphic, allowing them to fine-tune the adaptive immune response. HLAs corresponding to MHC class I (HLA-A, B, and C) present small peptide antigens from inside the cell, approximately 8 to 10 amino acids in length, to CD8+ T lymphocytes in order to activate a cytotoxic T cell response. HLAs corresponding to MHC class II (HLA-DP, DM, DO, DQ, and DR) present antigens from outside of the cell, approximately 15 to 24 residues in length, to CD4+ T-helper cells, which in turn secrete cytokines and stimulate B cells to produce antibodies to that specific antigen. HLAs corresponding to MHC class III encode components of the complement system (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Chromatin IP-seq, Immunoprecipitation, Western Blotting

Background: PR domain zinc finger protein 14 (PRDM14) is a likely protein lysine methyltransferase that is primarily expressed in primordial germ cells and pluripotent embryonic stem cells. It is essential for the establishment and maintenance of primordial germ cells and critical for the maintenance of pluripotency in embryonic stem cells (1-3). PRDM14 represses genes involved in the differentiation of stem cells into various cell lineages, likely via a combination of interactions with TET proteins, the polycomb repressive complex 2 (PRC2), and CBFA2T2 (3-8). In addition, overexpression of PRDM14 in combination with Jarid2 promotes induced pluripotent stem cell (iPSC) formation (9). PRDM14 protein levels are overexpressed in certain cancers, including breast, leukemia (T-ALL), and non-small cell lung cancer (NSCLC) (10-13), and PRDM14 overexpression may serve as a novel prognostic marker in NSCLC (14). Targeting PRDM14 overexpression with a siRNA-based therapy was shown to decrease liver metastasis in a murine pancreatic cancer model, suggesting potential as a therapeutic option for cancers where this protein is abnormally expressed (15).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: DNA-dependent protein kinase (DNA-PK) is an important factor in the repair of double-stranded breaks in DNA. Cells lacking DNA-PK or in which DNA-PK is inhibited fail to show proper nonhomologous end-joining (NHEJ) (1-7). DNA-PK is composed of two DNA-binding subunits (Ku70 and Ku86) and one 450 kDa catalytic subunit (DNA-PKcs) (8). It is thought that a heterodimer of Ku70 and Ku86 binds to double-stranded DNA broken ends before DNA-PKcs binds and is activated (1,9). Activated DNA-PKcs is a serine/threonine kinase that has been shown to phosphorylate a number of proteins in vitro, including p53, transcription factors, RNA polymerase, and Ku70/Ku86 (10,11). DNA-PKcs autophosphorylation at multiple sites, including Thr2609 and Ser2056, results in an inactivation of DNA-PK kinase activity and NHEJ ability (12,13). It has been demonstrated, however, that DNA-PK preferentially phosphorylates substrates before it autophosphorylates, suggesting that DNA-PK autophosphorylation may play a role in disassembly of the DNA repair machinery (14,15). Autophosphorylation at Thr2609 has also been shown to be required for DNA-PK-mediated double strand break repair, and phosphorylated DNA-PK co-localizes with H2A.X and 53BP1 at sites of DNA damage (16). Phosphorylation at Ser2056 occurs in response to double-stranded DNA breaks and ATM activation (17).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated α-Synuclein (D37A6) XP® Rabbit mAb #4179.
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: α-Synuclein is a protein of 140-amino acids expressed abundantly in the brain. α-Synuclein is also the main component of pathogenic Lewy bodies and Lewy neurites. Research studies have shown that mutations of the α-synuclein gene are linked to Parkinson's disease (1).

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

Application Methods: Western Blotting

Background: Vacuolar protein sorting-associated protein 26A (VPS26A), together with VPS29 and VPS35, is part of a trimeric protein complex known as the cargo-selective complex (CSC) (1). The CSC is regarded as the core functional component of the retromer, a multimeric protein complex involved in selective transport of cargo proteins from endosomes to the trans-Golgi network or plasma membrane (2). As part of the CSC, VPS26A does not have intrinsic membrane-binding activity but relies on association with RAB7A for recruitment to the cytosolic face of the endosomal membrane (3,4). Retromer defects are associated with neurological disease, and VPS26A mutations have been linked to perturbed endosomal cargo sorting in atypical parkinsonism (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Multiple exome sequencing analyses have uncovered a high frequency of histone H3 driver mutations in a number of different cancers, including diffuse intrinsic pontine glioma (DIPG), chondroblastoma, sarcomas, and HPV-negative head and neck squamous cell carcinoma. Previous studies have shown that lysine to methionine histone mutations in these cancers act as potent inhibitors of their respective lysine methyltransferases, resulting in gross alterations to the histone methylation landscape and deregulation of gene expression. In DIPG for example, the histone H3 K27M mutation is accompanied by a dramatic reduction in the levels of polycomb repressive complex 2 (PRC2)-mediated trimethylation of histone H3 lysine 27, changes in the distribution of PRC2 on the genome, and altered expression of genes associated with various cancer pathways (1-3). In chondrocytomas, the histone H3 K36M mutation functions to inhibit the WHSC1 (MMSET) and SETD2 histone methyltransferases, resulting in a reduction in the levels of histone H3 lysine 36 tri-methylation and deregulation of a number of cancer-associated genes (4). Similar to the H3K27M and H3K26M mutations, the histone H3 K9M mutation has been shown to inhibit the H3K9-directed histone methyltransferase G9a, resulting in reduced levels of histone H3 lysine 9 trimethylation. Given the widespread role of G9a in the regulation of gene expression, it is likely that this K9M mutation also plays a role in cancer.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Chromatin IP, Western Blotting

Background: MYST3, also known as Monocytic leukemia zinc finger protein (MOZ) and lysine acetyltransferase 6A (KAT6), is a member of the MYST (MOZ, YBF2, SAS2, and TIP60) family of histone acetyltransferases (1,2). First discovered as a fusion partner of CREBBP in acute myeloid leukemia, MYST3 contributes to Hox gene expression and segment identity during development (3-6). MYST3 forms an evolutionarily conserved complex with ING5, EAF6, and BRD1 and has been shown to be a coactivator for many different transcription factors including PU.1, NRF2, and Runx family members (7-9). MYST3 is critical in hematopoietic stem cell maintenance, where it acts synergistically with polycomb member BMI1 (10). Inhibitors of MYST3 are being investigated for therapeutic value as they can induce senescence and decrease tumor growth (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Cancer/testis antigens (CTAs) are a family of more than 100 proteins whose normal expression is largely restricted to immune privileged germ cells of the testis, ovary, and trophoblast cells of the placenta. Although most normal somatic tissues are void of CTA expression, due to epigenetic silencing of gene expression, their expression is upregulated in a wide variety of human solid and liquid tumors (1,2). As such, CTAs have garnered much attention as attractive targets for a variety of immunotherapy-based approaches to selectively attack tumors (3).

$348
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 Arginase-1 (D4E3M™) XP® Rabbit mAb #93668.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4,6). The reduced availability of L-arginine suppresses T-cell proliferation and function and thus contributes to tumor progression (4,6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that Arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: BCAT1 and BCAT2 are cytosolic and mitochondrial branched chain aminotransferases, respectively (1,2). Research studies have implicated BCAT1 in distant metastasis in patients with advanced colorectal cancer (3). Disruption of BCAT2 in mice leads to higher levels of plasma branched-chain amino acids, reduced adiposity and body weight, and increased energy expenditure, suggesting its role in regulating insulin sensitivity (4).

$320
100 µg
This Cell Signaling Technology antibody is conjugated to PerCP-Cy5.5® and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: L-selectin (CD62L, MEL-14, LAM1, SELL) is a cell adhesion molecule, responsible for homing and mediating the binding of lymphocytes to high endothelial venules (HEV) in secondary lymphoid tissues (1-5). It is a commonly used marker for distinguishing naive and memory T cells from effector T cells (6).

$299
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to APC-Cy7® and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The human leukocyte antigen (HLA) system is a gene complex encoding the major histocompatibility complex (MHC) proteins in humans. These cell surface proteins are responsible for the regulation of antigen-specific immunity in humans. HLA genes are highly polymorphic, allowing them to fine-tune the adaptive immune response. HLAs corresponding to MHC class I (HLA-A, B, and C) present small peptide antigens from inside the cell, approximately 8 to 10 amino acids in length, to CD8+ T lymphocytes in order to activate a cytotoxic T cell response. HLAs corresponding to MHC class II (HLA-DP, DM, DO, DQ, and DR) present antigens from outside of the cell, approximately 15 to 24 residues in length, to CD4+ T-helper cells, which in turn secrete cytokines and stimulate B cells to produce antibodies to that specific antigen. HLAs corresponding to MHC class III encode components of the complement system (1,2).

$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 4-1BB/CD137/TNFRSF9 (D2Z4Y) Rabbit mAb #34594.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: TNFRSF9 is a member of the tumor necrosis factor receptor superfamily (1, 2). It is also called 4-1BB or CD137 (1, 2). 4-1BB/CD137/TNFRSF9 is expressed in activated CD4+ and CD8+ T cells, natural killer cells and dendritic cells (2-5). The ligand 4-1BBL/CD137L/TNFSF9 on antigen presenting cells binds to 4-1BB/CD137/TNFRSF9 and costimulates the activation of T cells (5). The binding of agonistic antibodies to 4-1BB/CD137/TNFRSF9 also leads to costimulation for T cell activation (5). Studies have shown the effectiveness of targeting 4-1BB/CD137/TNFRSF9 by its agonistic antibodies in cancer immunotherapy (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytotoxic T-lymphocyte protein 4 (CTLA-4, CD152) is an Ig superfamily member that negatively regulates early T cell activation (1-4). The CTLA-4 protein is primarily expressed on T cells, including CD8+ cytotoxic T cells, CD4+ helper T cells, and CD4+/FoxP3+ regulatory T cells (1,2). CTLA-4 protein competes with CD28 for B7.1 (CD80) and B7.2 (CD86) binding at the cell surface, which results in the down regulation of T cell activity (5). The activation of SHP-2 and PP2A downstream of CTLA-4 attenuates TCR signaling (6). Research studies indicate that CTLA4 knockout mice display lymphoproliferative disorders leading to early death, confirming the role of CTLA-4 as a negative regulator of T cells (7). Mutations in the corresponding CTLA4 gene are associated with multiple disorders, including insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, and type V autoimmune lymphoproliferative syndrome (8,9). Additional studies demonstrate that CTLA-4 blockade is an effective strategy for tumor immunotherapy (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Complement receptor type 2 (CR2/CD21) is a type 1 transmembrane glycoprotein whose expression is largely restricted to B lymphocytes and follicular dendritic cells (1,2). Research studies have shown that CR2/CD21 functions to bind the complement fragments iC3b, C3dg, and C3d, which function to activate the alternative complement pathway and MAC formation (3,4). In addition to its function as a complement receptor, CR2/CD21 also functions as the B-lymphocyte receptor for Epstein-Barr virus (5) and interferon alpha (6). Research studies have also shown that CR2/CD21 participates in B-cell activation, proliferation, and protection from apoptosis through its association with components of the B-cell coreceptor signaling complex such as CD19 and CD21 (7-9).

$73
50 ml
This product is a concentrated fixation and permeabilization reagent designed for use with components of the FoxP3/Transcription Factor Fixation/Permeabilization Kit #43481. This reagent immobilizes cellular proteins and enables antibody binding of transcription factors localized within the nucleus, and is compatible with fluorescent detection by flow cytometry.Note: Precipitation may occur. The presence of precipitate does not affect the performance of the reagent.
APPLICATIONS

Application Methods: Flow Cytometry

$34
160 ml
This product is a diluent designed for use with components of the FoxP3/Transcription Factor Fixation/Permeabilization Kit #43481. Proper dilution of the FoxP3/Transcription Factor Fixation/Permeabilization Concentrate (4X) #44931 results in the reagent immobilizing cellular proteins and enabling antibody binding of transcription factors localized within the nucleus. This product is compatible with fluorescent detection by flow cytometry.Note: Precipitation may occur. The presence of precipitate does not affect the performance of the reagent.
APPLICATIONS

Application Methods: Flow Cytometry

$71
150 ml
This product is a concentrated buffer suitable for antibody incubation and wash steps, and is designed for use with components of the FoxP3/Transcription Factor Fixation/Permeabilization Kit #43481. This reagent enables antibody access to intracellular targets and is compatible with fluorescent detection by flow cytometry.Note: Precipitation may occur. The presence of precipitate does not affect the performance of the reagent.
APPLICATIONS

Application Methods: Flow Cytometry

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Ape1 (Apurinic/Apyrimidic eEndonuclease 1), also known as Ref1 (Redox effector factor 1), is a multifunctional protein with several biological activities. These include roles in DNA repair and in the cellular response to oxidative stress. Ape1 initiates the repair of abasic sites and is essential for the base excision repair (BER) pathway (1). Repair activities of Ape1 are stimulated by interaction with XRCC1 (2), another essential protein in BER. Ape1 functions as a redox factor that maintains transcription factors in an active, reduced state but can also function in a redox-independent manner as a transcriptional cofactor to control different cellular fates such as apoptosis, proliferation and differentiation (3). Increased expression of Ape1 is associated with many types of cancers including cervical, ovarian, prostate, rhabdomyosarcomas and germ cell tumors (4). Ape1 has been shown to stimulate DNA binding of several transcription factors known to be involved in tumor progression such as Fos, Jun, NF-κB, PAX, HIF-1, HLF and p53 (4). Mutation of the Ape1 gene has also been associated with amyotrophic lateral sclerosis (ALS) (5,6).

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

Application Methods: Flow Cytometry, Western Blotting

Background: The transcription factor ATF-2 (also called CRE-BP1) binds to both AP-1 and CRE DNA response elements and is a member of the ATF/CREB family of leucine zipper proteins (1). ATF-2 interacts with a variety of viral oncoproteins and cellular tumor suppressors and is a target of the SAPK/JNK and p38 MAP kinase signaling pathways (2-4). Various forms of cellular stress, including genotoxic agents, inflammatory cytokines, and UV irradiation, stimulate the transcriptional activity of ATF-2. Cellular stress activates ATF-2 by phosphorylation of Thr69 and Thr71 (2-4). Both SAPK and p38 MAPK have been shown to phosphorylate ATF-2 at these sites in vitro and in cells transfected with ATF-2. Mutations of these sites result in the loss of stress-induced transcription by ATF-2 (2-4). In addition, mutations at these sites reduce the ability of E1A and Rb to stimulate gene expression via ATF-2 (2).

$499
96 assays
1 Kit
The FastScan™ Phospho-Stat3 (Ser727) ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Stat3 when phosphorylated at Ser727. 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-Stat3 (Ser727) 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-Stat3 (Ser727). Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse, Rat

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$499
96 assays
1 Kit
The FastScan™ Total TREM2 ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of TREM2. 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 TREM2 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 TREM2. Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The triggering receptor expressed on myeloid cells 2 (TREM2) protein is an innate immune receptor that is expressed on the cell surface of microglia, macrophages, osteoclasts, and immature dendritic cells (1). The TREM2 receptor is a single-pass type I membrane glycoprotein that consists of an extracellular immunoglobulin-like domain, a transmembrane domain, and a cytoplasmic tail. TREM2 interacts with the tyrosine kinase-binding protein DAP12 to form a receptor-signaling complex (2). The TREM2 protein plays a role in innate immunity and a rare functional variant (R47H) of TREM2 is associated with the late-onset risk of Alzheimer’s disease (1,3). Research studies using mouse models of Alzheimer’s disease indicate that deficiency and haploinsufficiency of TREM2 can lead to increased β-amyloid (Aβ) accumulation as a result of dysfunctional microglia response (4). These results agree with the distribution of TREM2 in human brain regions (e.g., white matter, the hippocampus, and neocortex) that are involved in Alzheimer's disease pathology (2). In addition, amyloid plaque formation induces expression of TREM2 and amyloid phagocytosis (5). Loss-of-function mutations in the corresponding TREM2 or DAP12 genes can result in Nasu-Hakola disease, a rare form of progressive presenile dementia that results from polycystic osseous lesions (6). TREM2 membrane shedding occurs by cleavage at the extracellular site between H157/S158 generating an N-terminal shedded fragment and a membrane bound C-terminal fragment (7, 8).