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Product listing: CrkII Antibody, UniProt ID P46108 #3492 to DAZL Antibody, UniProt ID Q92904 #8042

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: CrkII, a cellular homologue of v-Crk, belongs to a family of adaptor proteins with an SH2-SH3-SH3 domain structure that transmits signals from tyrosine kinases (1). The primary function of Crk is to recruit cytoplasmic proteins in the vicinity of tyrosine kinases through SH2-phospho-tyrosine interaction. Thus, the output from Crk depends on the SH3-binding proteins, which include the C3G and Sos guanine nucleotide exchange proteins, Abl tyrosine kinase, DOCK180 and some STE20-related kinases. The variety of Crk-binding proteins indicates the pleiotropic function of Crk (2). The two CrkII SH3 domains are separated by a 54 amino acid linker region, which is highly conserved in Xenopus, chicken and mammalian CrkII proteins (3). Tyrosine 221 in this region is phosphorylated by the Abl tyrosine kinase (4), IGF-I receptor (5) and EGF receptor (6). Once Tyr221 is phosphorylated, CrkII undergoes a change in intramolecular folding and SH2-pTyr interaction, which causes rapid dissociation of CrkII from the tyrosine kinase complex (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Collapsin Response Mediator Protein-2 (CRMP-2) is expressed at high levels in the developing nervous system and plays a critical role in axonal outgrowth by specifying axon/dendrite fate and establishing neuronal polarity (1,2). CRMP-2 enhances axon elongation and branching by binding to tubulin heterodimers to promote microtubule assembly (3). GSK-3β inactivates CRMP-2 by phosphorylating it at Thr514. CRMP-2 is primed following phosphorylation at Ser522 by CDK5 and at Thr518 by GSK-3β (2). Phosphorylation of CRMP-2, which decreases tubulin binding ability, can be inhibited by NT-3 and BDNF through the PI3 kinase/Akt pathway (2). CRMP-2 also mediates semaphorin-induced growth cone collapse (4). Hyperphosphorylation of CRMP-2 is found in Alzheimer disease plaques with concurrent elevated GSK-3β activity in these patients (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: CtBP2 (carboxy-terminal binding protein-2) and its homolog CtBP1 are transcriptional co-repressors originally identified as proteins that bind the carboxy-terminus of the human adenovirus E1A protein (1-3). CtBP proteins are thought to play important roles in regulating various developmental pathways because deletion of CtBP2 leads to embryonic lethality at E10.5 and is correlated with axial patterning defects (4). CtBP proteins regulate various oncogenic signaling pathways as promoters of epithelial-mesenchymal transition, apoptosis antagonists, and tumor suppressor genes repressors (1,5). The CtBP protein transcription co-repression activity results from interactions with numerous transcription factors and chromatin modulators, including the polycomb group proteins (1,6,7). Depending on the context, CtBP proteins interact with a short amino acid sequence motif (PXDLS) to mediate repression of target genes through both histone deacetylase-dependent and independent mechanisms (6,8,9). CtBP proteins display a high sequence homology to the bacterial D-isomer-specific 2-hydroxyacid dehydrogenase enzymes. Research studies indicate that nuclear NADH levels regulate CtBP transcription repression activities, as NADH binding is required for CtBP2 homodimerization and transcription co-repressor activity (6,9-11).

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

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

Background: CCCTC-binding factor (CTCF) and its paralog, the Brother of the Regulator of Imprinted Sites (BORIS), are highly conserved transcription factors that regulate transcriptional activation and repression, insulator function, and imprinting control regions (ICRs) (1-4). Although they have divergent amino and carboxy termini, both proteins contain 11 conserved zinc finger domains that work in combination to bind the same DNA elements (1). CTCF is ubiquitously expressed and contributes to transcriptional regulation of cell-growth regulated genes, including c-myc, p19/ARF, p16/INK4A, BRCA1, p53, p27, E2F1, and TERT (1). CTCF also binds to and is required for the enhancer-blocking activity of all known insulator elements and ICRs, including the H19/IgF2, Prader-Willi/Angelman syndrome, and Inactive X-Specific Transcript (XIST) anti-sense loci (5-7). CTCF DNA-binding is sensitive to DNA methylation, a mark that determines selection of the imprinted allele (maternal vs. paternal) (1). The various functions of CTCF are regulated by at least two different post-translational modifications. Poly(ADP-ribosyl)ation of CTCF is required for insulator function (8). Phosphorylation of Ser612 by protein kinase CK2 facilitates a switch of CTCF from a transcriptional repressor to an activator at the c-myc promoter (9). CTCF mutations or deletions have been found in many breast, prostate, and Wilms tumors (10,11). Expression of BORIS is restricted to spermatocytes and is mutually exclusive of CTCF (3). In cells expressing BORIS, promoters of X-linked cancer-testis antigens like MAGE-1A are demethylated and activated, but methylated and inactive in CTCF-expressing somatic cells (12). Like other testis specific proteins, BORIS is abnormally expressed in different cancers, such as breast cancer, and has a greater affinity than CTCF for DNA binding sites, detracting from CTCF’s potential tumor suppressing activity (1,3,13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Carboxyl-terminal modulator protein (CTMP) is a negative regulator of Akt and was identified as an Akt binding protein. Akt, also referred to as PKB or Rac, plays a critical role in controlling the balance between survival and apoptosis (1-3). This protein kinase, activated by insulin and various growth and survival factors, functions in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4), and by phosphorylation within the carboxy-terminus at Ser473. CTMP binds to the regulatory domain of Akt at the carboxy terminus of the protein and inhibits phosphorylation on Thr308 and Ser473 (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The high affinity copper uptake protein 1 (CTR1, SLC31A1) helps maintain copper homeostasis by mediating dietary copper intake chiefly in the small intestine (1). A series of methionine-rich repeats and other residues are conserved among CTR1 genes across taxa, and are thought to be important for copper transport (2,3). In mammalian cells, CTR1 is localized to the plasma membrane and intracellular vesicles (3). Upon copper uptake via plasma membrane into cells, CTR1 is down regulated by clathrin-dependent endocytosis and degradation of CTR1 protein (4). Research studies suggest that the CTR1 copper transporter also mediates uptake of the anticancer drug cisplatin in yeast and mammals and that decreased CTR1 can result in the development of cisplatin resistance (5,6). Treatment of cancer cells with cisplatin can result in reduced CTR1 expression, which reduces cisplatin accumulation within cells and leads to cisplatin resistance in some human cancer cells (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: CUE domain-containing 2 (CUEDC2) protein is involved in regulating many cellular events including cell cycle regulation (1) and inflammation (2). Research studies have shown that CUEDC2 is highly expressed in many types of tumors, suggesting this protein may play a role in tumorigenesis (1,3). CUEDC2 is activated in early mitosis when it is phosphorylated by Cdk1 at Ser110. Phosphorylated CUEDC2 binds to Cdc20, which leads to the release of the anaphase-promoting complex/cyclosome (APC/C) from checkpoint inhibition, initiating anaphase. CUEDC2 is then dephosphorylated when cells exit mitosis (1). CUEDC2 is also an inhibitor of IKKα and IKKβ activation (2) as well as Jak1/Stat3 signaling (4). Research indicates that inappropriate regulation of CUEDC2 may contribute to tumor development by causing chromosome instability (1). Multiple studies have reported that CUEDC2 plays a role in the downregulation of progesterone receptor and estrogen receptor α, impairing the effects of progesterone on breast cancer cell growth. Conversely, research studies have shown that CUEDC2 and HER2 expression have a significant positive correlation in breast cancers, leading investigators to suggest that CUEDC2 could be an important target for breast cancer therapy (3,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Three components are involved in the target protein-ubiquitin conjugation process. Ubiquitin is first activated by forming a thiolester complex with the activation component E1; the activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2, then from E2 to ubiquitin ligase E3 for final delivery to the epsilon-NH2 of the target protein lysine residue (1-3). Combinatorial interactions of different E2 and E3 proteins result in substrate specificity (4). Recent data suggest that activated E2 associates transiently with E3, and that the dissociation is a critical step for ubiqitination (5). Cullin homolog 1 (CUL1), the mammalian homolog of Cdc53 from yeast, is a molecular scaffold of the SCF (Skp1/CUL1/F-box) E3 ubiquitin ligase protein complex. Thus, CUL1 and its family members function in ubiquitin dependent proteolysis (6). In particular, CUL1 has been shown to mediate ubiquitin dependent degradation of p21 Waf1/Cip1, cyclin D and IkappaB-alpha (7,8).

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

Application Methods: Western Blotting

Background: CUL3 (Cullin-3) is a member of the cullin-based ubiquitin ligase family. By interacting with Hrt1 and BTB domain containing proteins, the complex functions as a CUL3-based E3 ligase to bring specific substrates to ubiquitinylation and degradation (1). The CUL3 complex has been shown to target many substrates involved in cell cycle progression (2), transcription (3), development and differentiation (4,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Cullin-4 (CUL4) is a member of the cullin family of related ubiquitin ligases (1). A pair of mammalian CUL4 proteins - CUL4A and CUL4B - has been identified. The carboxy-terminal domain of CUL4 interacts with Rbx1 and E2 enzyme while the amino-terminal CUL4 domain interacts with BPB domain of UV-damaged DNA binding protein DDB1 to form a CUL4-DDB1 ubiquitin ligase complex (2). This CUL4-DDB1 complex binds a variety of WD40-containing proteins that help to enhance additional substrate recruitment (2,3). The CUL4 complex has been shown to target substrates involved in DNA repair, cell cycle progression (2), transcription (3), and development (2-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: CUTL1 (Cut-like 1), also known as CUX1 (Cut homeobox 1) (CUX1), is a transcription factor that has been implicated in many cellular processes in different tissues, such as cell migration, neuronal differentiation, and DNA repair (1-5). CUTL1 expression and activities are altered in cancer. Research studies have shown the CUTL1 gene to be a frequent target of loss-of-heterozygocity in various cancers (6,7). On the other hand, CUTL1 expression is elevated in many cancers and is associated with shorter disease-free survival (8). These accumulating evidence suggest that decreased CUTL1 expression promote tumor initiation and increased CUTL1 expression facilitates tumor progression (9). While full-length CUTL1 is about 200 kDa (p200), short forms p110 and p75 can also be generated by proteolytic processing and alternative transcription initiation site, respectively (10, 11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: The CXXC finger protein 1 (CXXC1, CGBP, CFP1) is a key subunit of the human SET1 histone methyltransferase complex (1,2) that methylates histone H3 at Lys4 to create a mark of transcriptionally active promoters (3,4). CXXC1 is enriched at CpG islands where it selectively binds non-methylated CpG motifs to provide a link between global H3K4 methylation and CpG islands (5). Research studies have revealed a role for CXXC1 in the maintenance of cytosine methylation through direct interaction with DNMT1 (6-9). The epigenetic functions of CXXC1 are critical for normal embryonic development. Targeted deletion of the murine Cxxc1 gene results in early embryonic lethality while Cxxc1-null embryonic stem (ES) cells exhibit increased apoptosis and fail to undergo differentiation in vitro following withdrawal of leukemia inhibitory factor LIF (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Cyclins are a family of proteins that activate specific cyclin-dependent kinases required for progression through the cell cycle. The entry of all eukaryotic cells into mitosis is regulated by activation of cdc2/cdk1 at the G2/M transition. This activation is a multi-step process that begins with the binding of the regulatory subunit, cyclin B1, to cdc2/cdk1 to form the mitosis-promoting factor (MPF). MPF remains in the inactive state until phosphorylation of cdc2/cdk1 at Thr161 by cdk activating kinase (CAK) (1,2) and dephosphorylation of cdc2/cdk1 at Thr14/Tyr15 by cdc25C (3-5). Five cyclin B1 phosphorylation sites (Ser116, 126, 128, 133, and 147) are located in the cytoplasmic retention signal (CRS) domain and are thought to regulate the translocation of cyclin B1 to the nucleus at the G2/M checkpoint, promoting nuclear accumulation and initiation of mitosis (6-9). While MPF itself can phosphorylate Ser126 and Ser128, polo-like kinase 1 (PLK1) phosphorylates cyclin B1 preferentially at Ser133 and possibly at Ser147 (6,10). At the end of mitosis, cyclin B1 is targeted for degradation by the anaphase-promoting complex (APC), allowing for cell cycle progression (11). Research studies have shown that cyclin B1 is overexpressed in breast, prostate, and non-small cell lung cancers (12-14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Activity of the cyclin-dependent kinases CDK4 and CDK6 is regulated by T-loop phosphorylation, by the abundance of their cyclin partners (the D-type cyclins), and by association with CDK inhibitors of the Cip/Kip or INK family of proteins (1). The inactive ternary complex of cyclin D/CDK4 and p27 Kip1 requires extracellular mitogenic stimuli for the release and degradation of p27 concomitant with a rise in cyclin D levels to affect progression through the restriction point and Rb-dependent entry into S-phase (2). The active complex of cyclin D/CDK4 targets the retinoblastoma protein for phosphorylation, allowing the release of E2F transcription factors that activate G1/S-phase gene expression (3). Levels of cyclin D protein drop upon withdrawal of growth factors through downregulation of protein expression and phosphorylation-dependent degradation (4).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Cyclin E1 and cyclin E2 can associate with and activate CDK2 (1). Upon DNA damage, upregulation/activation of the CDK inhibitors p21 Waf1/Cip1 and p27 Kip1 prevent cyclin E/CDK2 activation, resulting in G1/S arrest. When conditions are favorable for cell cycle progression, cyclin D/CDK4/6 phosphorylates Rb and is thought to reduce the activity of p21 Waf1/Cip1 and p27 Kip1, allowing subsequent activation of cyclin E/CDK2 (1,2). Cyclin E/CDK2 further phosphorylates Rb to allow progression into S-phase, where cyclin E/CDK2 is thought to phosphorylate and activate multiple proteins involved in DNA synthesis (2,3). Turnover of cyclin E is largely controlled by phosphorylation that results in SCFFbw7-mediated ubiquitination and proteasome-dependent degradation (4,5). Cyclin E1 is phosphorylated at multiple sites in vivo including Thr62, Ser88, Ser72, Thr380 and Ser384, and is controlled by at least two kinases, CDK2 and GSK-3 (6,7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Cyclin H belongs to a conserved cyclin family that plays a critical role in the regulation of cell cycle dependent kinases (CDKs) necessary for cell cycle progression (1,2). In general, the activity of CDKs requires the binding of appropriate cyclins as well as phosphorylation driven by Cdk-activating kinase (CAK). Cyclin H is part of the CAK complex that includes the kinase CDK7, and an assembly factor p36/Mat1, which enhances binding between cyclin H and CDK7 and increases activity (3,4). CAK regulates progression through the cell cycle by activating cdc2, CDK2, and CDK4 kinases through phosphorylation of a critical threonine residue in the T-loop of the CDK-cyclin complexes (5,6). The CAK complex can exist either in its free form or in association with transcription factor IIH (TFIIH) which can affect its substrate specificity (7,8,9). When bound to TFIIH, CAK preferentially phosphorylates the carboxy-terminal domain of RNA polymerase II (9), providing a link between cell cycle control, transcriptional regulation, and DNA repair.

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

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, Mouse

Application Methods: Western Blotting

Background: Cytoplasmic FMR1-interacting protein 1 (CYFIP1) is a component of the CYFIP1/EIF4E/FMR1 complex which mediates translational repression by binding to the mRNA cap (1). CYFIP1 also plays a role in neuronal axonal growth dynamics by binging to the WAVE complex to regulate remodeling of actin filaments (2). Mutations in the gene encoding CYFIP1 has been linked to multiple neural development and psychiatric disorders, including autism spectrum disorder and schizophrenia (3-6). The specific mechanism by which CYFIP1, which is enriched in synapses, contributes to these neurological diseases is unknown, but may involve regulating the balance of synaptic excitation and inhibition to maintain neuronal circuit homeostasis during development and in mature brains (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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
Human

Application Methods: 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).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, 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, Mink, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The common beta-chain (beta-c) of the granulocyte macrophage colony-stimulating factor (GM-CSF), interleukin-3 (IL-3) and IL-5 receptors is the major signaling subunit of these receptors, coupling ligand binding to multiple biological activities (1-3). Tyrosine phosphorylation of cytokine receptor common beta-chain is one of the first events in GM-CSF, IL-3 and IL-5 receptor activation and in signaling initiation (4). Serine phosphorylation within the 14-3-3 binding sequence of the common beta-chain is also involved in GM-CSF, IL-3 and IL-5 receptor-specific functions (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Reelin signaling pathway plays a critical role in neuronal development. Reelin is a secreted glycoprotein that binds to the lipoprotein receptors VLDLR and ApoER2 or alpha3beta1 integrin on the surface of neurons (1,2). Activation of these receptors induces tyrosine phosphorylation of Disabled 1 (Dab1), an intracellular adaptor. It is generally believed that tyrosine phosphorylation of Dab1 by Src family tyrosine kinases is the most critical downstream event in Reelin signaling. The phosphotyrosine-binding (PTB) domain within its amino terminus enables Dab1 to recognize and bind to a conserved sequence motif within the cytoplasmic tail of the receptors. In addition, the PTB contains a Pleckstrin Homology-like subdomain that binds to phosphoinositides. The phosphoinositide-binding region within the Dab1 PTB domain is required for membrane localization and basal tyrosine phosphorylation of Dab1 independent of VLDLR and ApoER2 (3). It has been demonstrated that Src, CrkII, CrkL and Dock1 associate with tyrosine-phosphorylated Dab. The CrkII-Dab1 interaction requires tyrosine phosphorylation of Dab1 at residues 220 or 232 (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Death associated protein 1 (DAP1) is a 15 kDa protein that functions as a positive mediator of cell death initiated by interferon-gamma (1, 2). The DAP1 protein is proline rich and possesses one SH3 binding motif, as well as several consensus protein kinase phosphorylation sites (1). The protein is localized in the cytoplasm, but the detailed mechanism of its proapoptotic function is unclear. Death associated protein 3 (DAP3) is widely expressed, and the expression is upregulated during membrane receptor-mediated apoptosis. In interferon-gamma- and Fas-induced apoptosis, DAP3 acts as a positive mediator, functioning downstream of the receptor signaling complex and upstream of the effector caspases (3,4). Death associated protein 5 (DAP5) is a 97 kDa protein with a high degree of amino acid sequence homology to eukaryotic translation initiation factor 4G (Elf4G) (1,5). Compared with elF4G, DAP5 lacks the amino-terminal region necessary for cap-dependent translation, and has a unique carboxy-terminal region that functions as a regulator of interferon-gamma-induced cell death (5,6). During induction of apoptosis, DAP5 is cleaved at aspartic acid 790. The carboxy-terminal truncated form of DAP5 functions as a cap-independent translation initiation factor responsible for the mediation of its own translation during apoptosis (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Death-associated protein kinase (DAPK1) is a Ca2+/calmodulin-regulated serine/threonine kinase that participates in a wide range of apoptotic signals including interferon-γ, tumor necrosis factor α, Fas, activated c-Myc, and detachment from the extracellular matrix. In addition to the kinase domain and calmodulin regulatory segment, DAPK1 also has eight ankyrin repeats, a cytoskeleton binding region, and a conserved death domain (1-3). Deletion of the calmodulin-regulatory domain generates a constitutively active mutant kinase. Ectopic expression of wild-type DAPK1 induced cell death in HeLa cells. Conversely, expression of a catalytically inactive mutant protected cells from interferon-γ-induced cell death (4). The catalytic domain of DAPK1 has very high sequence similarity to vertebrate myosin light chain kinase (MLCK) and a RXX(S/T)X motif derived from myosin light chain protein was shown to be phosphorylated in vitro by DAPK1 (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Death-associated protein kinase (DAPK1) is a Ca2+/calmodulin-regulated serine/threonine kinase that participates in a wide range of apoptotic signals including interferon-γ, tumor necrosis factor α, Fas, activated c-Myc, and detachment from the extracellular matrix. In addition to the kinase domain and calmodulin regulatory segment, DAPK1 also has eight ankyrin repeats, a cytoskeleton binding region, and a conserved death domain (1-3). Deletion of the calmodulin-regulatory domain generates a constitutively active mutant kinase. Ectopic expression of wild-type DAPK1 induced cell death in HeLa cells. Conversely, expression of a catalytically inactive mutant protected cells from interferon-γ-induced cell death (4). The catalytic domain of DAPK1 has very high sequence similarity to vertebrate myosin light chain kinase (MLCK) and a RXX(S/T)X motif derived from myosin light chain protein was shown to be phosphorylated in vitro by DAPK1 (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: 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: Immunoprecipitation, Western Blotting

Background: The human Deleted in AZoospermia (DAZ) genes encode a family of RNA-binding proteins that are expressed exclusively in the germ cells and play a role in the regulation of mRNA translation (1). Members of the family include DAZ, DAZL, and BOULE. The essential role of DAZL and BOULE in spermatogenesis has been established (2-4), but the role of DAZ remains unclear. Men with deletions in the DAZ1 gene can produce sperm, although in lower numbers, and are capable of reproduction and transmission of the genetic lesions (5-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The human DAZ (Deleted in Azoospermia) gene family contains at least three members that encode RNA-binding proteins with a common RNA-recognition motif (1). An autosomal homolog of DAZ, DAZL (DAZ-like), is specifically expressed in germ cells and is essential for the specification of the germ cell lineage during embryogenesis and during gametogenesis in adults of both sexes (2,3). DAZL may function by directly recruiting poly(A)-binding proteins (PABPs) in order to activate silent mRNAs during germ cell development (2). Deletions encompassing the Y chromosomal DAZ genes are the most common molecularly defined cause of infertility in humans (4,5).