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Product listing: Cyclin F (D9K2U) Rabbit mAb, UniProt ID P41002 #81045 to DAX1 (D2F1) Rabbit mAb, UniProt ID P51843 #13538

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Cyclin F is the founding member of the F-box protein family, present in all eukaryotic cells. F-box proteins are components of the Skp1-Cullin-F-box (SCF) ubiquitin ligase complex. The substrate specificity of the SCF complex is determined by the interchangeable F-box proteins, which act as adaptors by associating with phosphorylated substrate proteins and recruiting them to the SCF core (1).Cyclin F contains a cyclin box domain in addition to an F-box domain, but does not regulate the activity of cyclin dependent kinases. Cyclin F expression does oscillate during the cell cycle, however, peaking in G2 phase (2).Cyclin F interacts with the centrosomal protein CP110, which plays critical roles centriole duplication and spindle formation. Cyclin F-mediated degradation of CP110 in G2 phase is required for normal progression into mitosis (3). In response to ionizing radiation, which causes DNA double strand breaks, Cyclin F interacts with B-Myb, preventing cyclin A-dependent phosphorylation of B-Myb, and delaying progression into mitosis. This G2 phase arrest allows the cell to respond to the DNA damage-induced G2/M phase checkpoint (4). Cyclin F also controls the stability of the ribonucleotide reductase M2 subunit, RRM2, which functions in maintaining the levels of dNTPs available in the cell for DNA synthesis and repair, in response to genotoxic stress (5). Researchers have implicated cyclin F as a prognostic marker in hepatocellular carcinoma (HCC) (6).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Positive transcription elongation factor (P-TEFb) is a heterodimer composed of cyclin T proteins and CDK9. P-TEFb plays a critical role in the transition of the RNA polymerase II (RNAPII) machinery from transcription initiation to elongation (1). At some genes during transcription initiation, RNAPII moves approximately 50 nucleotides away from the transcription start site into the gene where it then pauses and awaits signaling for the formation of a productive transcription elongation complex (1,2). The release of this promoter proximal pausing of RNAPII is signaled by phosphorylation of the C-terminal domain (CTD) within the largest subunit of RNAPII at Ser2 of the heptapeptide repeat sequence by P-TEFb (3). This phosphorylation event is important for the recruitment of mRNA processing factors and chromatin modifiers that are necessary for proper gene expression (4,5). P-TEFb also promotes transcription elongation by phosphorylating DSIF (DRB-induced stimulating factor) and NELF (negative elongation factor), two negative elongation factors that retain RNAPII at the promoter proximal region of genes to initiate transcription elongation (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Cyclophilins are a highly conserved family of peptidylprolyl cis-trans-isomerases (PPIA) that are targets of the immunosuppressant drug cyclosporin A (CsA) (1,2). The complex of cyclophilin and CsA can bind to and inhibit calcineurin which leads to inhibition of the transcription factor NFAT and decreased production of cytokines (3,4). As isomerases, cyclophilins have been proposed to aid in protein folding. Cyclophilin A can bind to the p55 Gag protein of HIV and appears necessary for HIV infection (5,6). There is also some evidence that cyclophilins have nuclease activity and play a role in apoptosis (7).

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

Application Methods: Western Blotting

Background: Cyclophilin B (CyPB) is an ER-localized chaperone protein belonging to the family of peptidyl-prolyl cis-trans isomerases (PPIases) (1,2). Research studies have demonstrated that CyPB associates with type I procollagen and is involved in its sorting and transport through the secretory compartment (3). Mutations in the gene encoding CyPB, PPIB, lead to aberrant biosynthesis of type I procollagen, which underlies the pathogenesis of osteogenesis imperfecta (OI), a disorder characterized by bone fragility (4-7). In additional to its role in OI, research studies demonstrate that CyPB overexpression supports the expression of multiple oncogenic drivers of glioblastoma multiforme (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: CYLD is a cytoplasmic deubiquitinating enzyme encoded by a tumor suppressor gene altered in individuals diagnosed with cylindromatosis, a genetic condition characterized by benign tumors of skin appendages (1,2). Functional CYLD deubiquitinase regulates inflammation and cell proliferation by down regulating NF-κB signaling through removal of ubiquitin chains from several NF-κB pathway proteins (3,4). CYLD is a negative regulator of proximal events in Wnt/β-catenin signaling and is a critical regulator of natural killer T cell development (5,6). The transcription factor Snail can inhibit CYLD expression, resulting in melanoma cell proliferation (7).

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

Application Methods: Western Blotting

Background: CYLD is a cytoplasmic deubiquitinating enzyme encoded by a tumor suppressor gene altered in individuals diagnosed with cylindromatosis, a genetic condition characterized by benign tumors of skin appendages (1,2). Functional CYLD deubiquitinase regulates inflammation and cell proliferation by down regulating NF-κB signaling through removal of ubiquitin chains from several NF-κB pathway proteins (3,4). CYLD is a negative regulator of proximal events in Wnt/β-catenin signaling and is a critical regulator of natural killer T cell development (5,6). The transcription factor Snail can inhibit CYLD expression, resulting in melanoma cell proliferation (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: In steroidogenic tissues, such as the adrenal cortex, testis, ovary, and placenta, all steroids are synthesized from the common precursor cholesterol. Two families of steroidogenic enzymes, cytochrome P450 hydroxylase enzymes (CYP) and hydroxysteroid dehydrogenases (HSD), catalyze the production of most steroids. There are six distinct steroid hydroxylases, which are cytochrome P450 enzymes encoded by the steroidogenic CYP gene family (1). The cytochrome P450scc (cholesterol side-chain cleavage enzyme) encoded by CYP11A1 catalyzes the first and rate-limiting step in steroidogenesis, conversion of cholesterol into pregnenolone (2).CYP11A1, located in the inner membrane of mitochondria, cooperates with two coenzymes, ferredoxin and ferredoxin reductase, to carry out three successive oxidation-reduction reactions of cholesterol (3-5). In the adrenal cortex, testis, and ovary, CYP11A1 expression is regulated by the cAMP-PKA pathway (6), and the transcription factor SF1/NR5A1 has been shown to play a central role in mediating the cAMP signal on the CYP11A1 promoter within steroidogeneic cells of the adrenal cortex and gonads (7). Defects in CYP11A1 are the cause of adrenal insufficiency congenital with 46, XY sex reversal (AICSR), which is a rare disorder that can present as acute adrenal insufficiency in infancy or childhood (8,9).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: CYP17A1, also known as cytochrome P450C17, is a steroidogenic enzyme belonging to the P450 cytochrome superfamily of monooxygenases (1, 2). In humans, CYP17A1 expression is abundantly expressed in the adrenal cortex, where it plays a central role in the androgen synthesis pathway (2). CYP17A1 is the primary target of abiraterone, a synthetic steroid used in the treatment of castration-resistant prostate cancer (CRPC) (3, 4). Abiraterone is converted to the more active form D4A, which antagonizes androgen receptor signaling by inhibiting CYP17A1 and other steroidogenic enzymes (3, 4). This suppresses the synthesis of 5α-dihydrotestosterone (DHT), which is a driver of castration-resistant prostate cancer cell growth (3, 4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CYP17A1, also known as cytochrome P450C17, is a steroidogenic enzyme belonging to the P450 cytochrome superfamily of monooxygenases (1, 2). In humans, CYP17A1 expression is abundantly expressed in the adrenal cortex, where it plays a central role in the androgen synthesis pathway (2). CYP17A1 is the primary target of abiraterone, a synthetic steroid used in the treatment of castration-resistant prostate cancer (CRPC) (3, 4). Abiraterone is converted to the more active form D4A, which antagonizes androgen receptor signaling by inhibiting CYP17A1 and other steroidogenic enzymes (3, 4). This suppresses the synthesis of 5α-dihydrotestosterone (DHT), which is a driver of castration-resistant prostate cancer cell growth (3, 4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Cytochrome P450 (CYP) is a family of enzymes that contain a heme group (1). These enzymes, when reduced and bound by carbon monoxide, maximally absorb light of 450 nm (1). Type I cytochrome P450s are found in mitochondria and function in the biosynthesis of essential molecules (1). Type II cytochrome P450s are found in endoplasmic reticulum (1). Some type II cytochrome P450s play a role in the biosynthesis of essential molecules whereas others metabolize xenobiotics (1). Research studies show that cytochrome P450s form various heteromeric complexes with other members of the P450 family influencing their catalytic activities (2-4). CYP1A2 is in the endoplasmic reticulum of hepatocytes and responsible for the breakdown of a variety of xenobiotic substances and bioactivation of carcinogens (2, 5). CYP1 enzymes, including CYP1A2, have been implicated in smoking-related osteoporosis (6). A meta-analysis shows that a particular polymorphism in CYP1A2 is potentially linked to increased cancer risk (5).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Cytochrome P450, subfamily 3A, polypeptide 4 (CYP3A4) is a mono-oxygenase enzyme (1) found in the endoplasmic reticulum membrane of liver and prostate microsomes. It is an important enzyme in drug metabolism; it catalyzes phase I oxidation reactions in approximately 50% of drugs in the modern market, as well as steroids, fatty acids, and some carcinogens (2). It is also involved in steroid and cholesterol synthesis (3,4). Expression of CYP3A4 can be induced by glucocorticoids, carcinogens, pesticides, and drugs, which can lead to drug interactions and toxicity (5).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Cysteine-rich protein 61 (CYR61, CCN1) is a secreted, matrix-associated protein belonging to the CCN family, a protein group characterized primarily by its high cysteine content (1). CYR61 regulates diverse cellular events including cell proliferation, differentiation, angiogenesis, and extracellular matrix formation. Research studies have implicated CYR61 in the development or progression of various cancers, including breast, prostate, lung, and hepatocellular carcinoma (1-4). Notably, its role in promoting cancer progression appears to be context-dependent. For example, investigators have shown that overexpression of CYR61 was positively associated with invasiveness of breast cancer cell lines (2), whereas in primary prostate tumors, expression levels were inversely correlated with tumor aggressiveness (3). In additional research studies of hepatocellular carcinoma, where CYR61 expression was positively associated with cancer progression, CYR61 was shown to be transcriptionally regulated by the Wnt/β-catenin signaling pathway (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Cysteine-rich protein 61 (CYR61, CCN1) is a secreted, matrix-associated protein belonging to the CCN family, a protein group characterized primarily by its high cysteine content (1). CYR61 regulates diverse cellular events including cell proliferation, differentiation, angiogenesis, and extracellular matrix formation. Research studies have implicated CYR61 in the development or progression of various cancers, including breast, prostate, lung, and hepatocellular carcinoma (1-4). Notably, its role in promoting cancer progression appears to be context-dependent. For example, investigators have shown that overexpression of CYR61 was positively associated with invasiveness of breast cancer cell lines (2), whereas in primary prostate tumors, expression levels were inversely correlated with tumor aggressiveness (3). In additional research studies of hepatocellular carcinoma, where CYR61 expression was positively associated with cancer progression, CYR61 was shown to be transcriptionally regulated by the Wnt/β-catenin signaling pathway (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Cystathionine γ-lyase (CGL) is an enzyme in the transsulfuration pathway, a route in the metabolism of sulfur-containing amino acids (1). This enzyme regulates local vasodilation and blood pressure by generating hydrogen sulfide (H2S) as a physiological signaling molecule (2). A rodent model of sleep apnea showed that H2S production by cystathionine γ-lyase in the carotid body triggers hypertension in rodents during intermittent hypoxia, suggesting that inhibition of this enzyme may prevent the hypertension associated with sleep apnea (3). In addition, dietary restriction of sulfur-containing amino acids upregulates hepatic cystathionine γ-lyase expression in mice, leading to elevated production of H2S and protection from hepatic ischemia perfusion injury, indicating that this enzyme is critical for the benefits of dietary restriction (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Cystathionine γ-lyase (CGL) is an enzyme in the transsulfuration pathway, a route in the metabolism of sulfur-containing amino acids (1). This enzyme regulates local vasodilation and blood pressure by generating hydrogen sulfide (H2S) as a physiological signaling molecule (2). A rodent model of sleep apnea showed that H2S production by cystathionine γ-lyase in the carotid body triggers hypertension in rodents during intermittent hypoxia, suggesting that inhibition of this enzyme may prevent the hypertension associated with sleep apnea (3). In addition, dietary restriction of sulfur-containing amino acids upregulates hepatic cystathionine γ-lyase expression in mice, leading to elevated production of H2S and protection from hepatic ischemia perfusion injury, indicating that this enzyme is critical for the benefits of dietary restriction (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cystatin C (cystatin-3, CST3) belongs to the cystatin type 2 superfamily of cysteine peptidase inhibitors (1). The 146 amino acid cystatin C precursor protein contains a 26 residue, amino-terminal secretory signal sequence. The mature 120 amino acid cystatin C protein contains two disulfide bridges (2,3). Cystatin C is secreted in body fluids and is a marker of kidney (4) and cardiovascular (5) dysfunction. Research studies report of changes in cystatin C levels in the cerebral spinal fluid as well as in specific neuronal cell populations in a number of neurodegenerative diseases (6-8). Interestingly, experimental evidence suggests that cystatin C has protective effects against neurodegeneration, such as inhibition of amyloid-β oligomerization and fibril formation (9,10), induction of autophagy (11), induction of neurogenesis (12), and inhibition of cysteine proteases whose activity has been associated with several neurodegenerative diseases (13).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Cytochrome c is a well conserved electron-transport protein and is part of the respiratory chain localized to mitochondrial intermembrane space (1). Upon apoptotic stimulation, cytochrome c released from mitochondria associates with procaspase-9 (47 kDa)/Apaf 1. This complex processes caspase-9 from inactive proenzyme to its active form (2). This event further triggers caspase-3 activation and eventually leads to apoptosis (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation

Background: Cytochrome c is a well conserved electron-transport protein and is part of the respiratory chain localized to mitochondrial intermembrane space (1). Upon apoptotic stimulation, cytochrome c released from mitochondria associates with procaspase-9 (47 kDa)/Apaf 1. This complex processes caspase-9 from inactive proenzyme to its active form (2). This event further triggers caspase-3 activation and eventually leads to apoptosis (3).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cytochrome c (D18C7) Rabbit mAb #11940.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Cytochrome c is a well conserved electron-transport protein and is part of the respiratory chain localized to mitochondrial intermembrane space (1). Upon apoptotic stimulation, cytochrome c released from mitochondria associates with procaspase-9 (47 kDa)/Apaf 1. This complex processes caspase-9 from inactive proenzyme to its active form (2). This event further triggers caspase-3 activation and eventually leads to apoptosis (3).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Cytochrome c is a well conserved electron-transport protein and is part of the respiratory chain localized to mitochondrial intermembrane space (1). Upon apoptotic stimulation, cytochrome c released from mitochondria associates with procaspase-9 (47 kDa)/Apaf 1. This complex processes caspase-9 from inactive proenzyme to its active form (2). This event further triggers caspase-3 activation and eventually leads to apoptosis (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Disabled homologue 2 (Dab2) is a mitogen responsive phosphoprotein that exerts multiple functions through association with numerous proteins. Dab2 modulates signaling pathways through interactions with proteins such as Smads and TGF-β receptors (1,2), axin (3), GRB (4) and Src (5). Dab2 also serves as a cargo-specific adaptor of clathrin-mediated endocytosis via interaction with clathrin (6), AP2 (7), NPXY-containing cargo (8-10), and myosin VI (11,12). In addition, Dab2 regulates cell adhesion by directly binding integrins (13,14). The diverse functions of Dab2 enable it to coordinate cell adhesion, cell motility, membrane trafficking, and signaling. Research studies have shown Dab2 is down-regulated in a number of cancers, thereby suggesting a role as a tumor suppressor (15-17). Phosphorylation of Dab2 decreases its endocytotic function (18).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

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

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Diacylglycerol (DAG) lipases comprise two enzymes called DAG lipase α and β, which are the products of two related genes (1). DAG lipases are transmembrane proteins composed of a short amino-terminal intracellular domain, four transmembrane domains, and a large carboxy-terminal cytoplasmic domain containing the active site. These enzymes are responsible for the biosynthesis of 2-acylglycerol from diacylglycerol in a calcium-dependent manner (1). One of the major endocannabinoid ligands that activate cannabinoid receptors, 2-arachidonyl glycerol (2-AG), is produced by DAG lipases (2). Research studies suggest that DAG lipase α is the isoform primarily responsible for the central production of 2-AG (3). DAG lipase β has been implicated in studies of 2-AG production at the periphery in specific cell types and pathophysiological contexts, such as in hepatic stellate cells during alcohol induced fatty liver (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Diacylglycerol (DAG) lipases comprise two enzymes called DAG lipase α and β, which are the products of two related genes (1). DAG lipases are transmembrane proteins composed of a short amino-terminal intracellular domain, four transmembrane domains, and a large carboxy-terminal cytoplasmic domain containing the active site. These enzymes are responsible for the biosynthesis of 2-acylglycerol from diacylglycerol in a calcium-dependent manner (1). One of the major endocannabinoid ligands that activate cannabinoid receptors, 2-arachidonyl glycerol (2-AG), is produced by DAG lipases (2). Research studies suggest that DAG lipase α is the isoform primarily responsible for the central production of 2-AG (3). DAG lipase β has been implicated in studies of 2-AG production at the periphery in specific cell types and pathophysiological contexts, such as in hepatic stellate cells during alcohol induced fatty liver (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: DNAX-activating protein 12 (DAP12, TYROBP) is a signaling adaptor for several pathogen receptors expressed by cells of the innate immune system (1). The DAP12 protein structure consists of a short extracellular domain, a transmembrane domain, and a cytoplasmic immunoreceptor tyrosine-based activation motif (ITAM) (2). DAP12 protein is expressed by hematopoietic cells, including NK cells, monocytes, macrophages, dendritic cells, mast cells, basophils, eosinophils, neutrophils, and some γδ T cells and NKT cells (1). DAP12 exists as a homodimer that associates with a variety of receptors involved in pathogen detection, including the KIR family of NK cell receptors (2,3). Ligand binding by DAP12-associated receptors results in phosphorylation of tyrosine residues within the DAP12 ITAM by Src family kinases and leads to activation of Syk or Zap-70 and downstream signaling responses (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The dual adaptor of phosphotyrosine and 3-phosphoinositides (DAPP1/BAM32) is a cytoplasmic adaptor protein that mediates the recruitment and interaction of molecules required for signal transduction downstream of the B cell receptor (BCR) (1). The DAPP1/BAM32 protein contains an amino-terminal SH2 domain and a carboxy-terminal pleckstrin homology (PH) domain that binds to PI3K-derived phosphoinositides (i.e., PIP3). Upon BCR activation, DAPP1/BAM32 is phosphorylated at specific tyrosine residues and translocated from the cytoplasm to the membrane. Research studies indicate that phosphorylation and translocation of DAPP1/BAM32 is strongly dependent upon PI3K signaling (2,3). The amino-terminal SH2 domain binds to PLCγ2 and other tyrosine-phosphorylated targets. As a result of these interactions, DAPP1/BAM32 can adjust the response to receptor activation by coordinating membrane-localized interactions among proteins of distinct signal transduction pathways (1,4). DAPP1/BAM32 is expressed most abundantly in B lymphocytes; high expression during dendritic cell (DC) maturation and localization to contact sites between DC and allogenic T cells suggest that the DAPP1/BAM32 adaptor may play a role in the activation of T cells through MHC class I-mediated signaling pathways (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

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

Background: DARPP-32 (dopamine and cyclic AMP-regulated phosphoprotein, relative molecular mass 32,000) is a cytosolic protein highly enriched in medium-sized spiny neurons of the neostriatum (1). It is a bifunctional signaling molecule that controls serine/threonine kinase and serine/threonine phosphatase activity (2). Dopamine stimulates phosphorylation of DARPP-32 through D1 receptors and activation of PKA. PKA phosphorylation of DARPP-32 at Thr34 converts it into an inhibitor of protein phosphatase 1 (1). DARPP-32 is converted into an inhibitor of PKA when phosphorylated at Thr75 by cyclin-dependent kinase 5 (CDK5) (2). Mice containing a targeted deletion of the DARPP-32 gene exhibit an altered biochemical, electrophysiological, and behavioral phenotype (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: DSS-AHC critical region on the X chromosome protein 1 (DAX1) is an orphan nuclear receptor encoded by the nuclear receptor subfamily 0 group B member 1 (NR0B1) gene. DAX1 possesses an atypical DNA binding domain that allows it to form heterodimeric complexes with DNA binding partners and repress transcriptional activity (1,2). During development, DAX1 is important for establishment of the hypothalamic-pituitary-adrenal gonadal axis. The receptor is essential for development of several important hormone-producing organs that determine this axis, including the adrenal glands, pituitary, hypothalamus, and the male and female reproductive organs (3,4). Research studies suggest that DAX1 plays a role in maintenance of pluripotency in embryonic stem cells (5,6). Loss of DAX1 function through deletion or mutation results in adrenal insufficiency and hypogonadotropic hypogonadism (7), while duplication of the NR0B1 gene on the X-chromosome causes dosage-sensitive sex reversal (8).