Microsize antibodies for $99 | Learn More >>

Product listing: USP13 (D4P3M) Rabbit mAb, UniProt ID Q92995 #12577 to CD14 (61D3) Mouse mAb (FITC Conjugate), UniProt ID P08571 #29943

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzyme (DUB) action (1,2). Five DUB subfamilies are recognized, including the USP, UCH, OTU, MJD, and JAMM enzymes. Ubiquitin carboxyl-terminal hydrolase 13 (USP13; isopeptidase T-3) contains four ubiquitin-associated/translation elongation factor EF1B, amino terminal (UBA) domains and one ubiquitin-specific processing protease (UBP) domain. The UBP domain of USP13 contains a catalytic site, a zinc finger domain, and two UBA domains. Similar to other USP family members, USP13 contains cysteines and histidines that are likely involved in its catalytic mechanism. Studies show that USP13 plays a critical role in autophagy through the deubiquitination of target proteins such as BECN1 and USP10 (3). Research also suggests that USP13 is implicated in the pathogenesis of melanoma through its ability to regulate the ubiquitination status of MITF (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: YY1 (Yin Yang1) is a ubiquitously expressed transcription factor with fundamental roles in embryogenesis, differentiation, replication and proliferation. YY1 contains four zinc finger motifs of the Cys-Cys-His-His type and can activate different eukaryotic genes (such as CREB, c-myc, Histone H4, p53 and PARP-1) or repress different eukaryotic genes (such as α-actin, IFN-β and IFN-γ) as well as regulate some viral promoters (1). YY1 deficient embryos die approximately at the time of implantation, suggesting that YY1 has an essential role in embryonic development (2). YY1 is overexpressed in cancer cells such as prostate cancer and therefore may be considered a prognostic marker (1).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The 20S proteasome is the major proteolytic enzyme complex involved in intracellular protein degradation. PA700, PA28, and PA200 are three major protein complexes that function as activators of the 20S proteasome. There are three evolutionarily conserved subunits of PA28: PA28α (PSME1), PA28β (PSME2), and PA28γ (PSME3) (1,2). PA28α and PA28β form a heteroheptameric complex and function by binding to the 20S complex at its opening site(s). The PA28α/β complex is present throughout the cell and participates in MHC class I antigen presentation by promoting the generation of antigenic peptides from foreign proteins (2). PA28γ exists in the form of a homoheptamer and is mainly located in the nucleus. The PA28γ complex exerts its function by binding and guiding specific nuclear target proteins to the 20S proteasome for further degradation (3,4).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Calumenin belongs to the CREC family of proteins that also contains reticulocalbin, ERC-55/TCBP-49/E6BP, Cab45, and crocalbin/CBP-50. These EF-hand proteins localize to the endoplasmic reticulum (ER) and are involved in the secretory pathway in mammalian cells (1). Calumenin exists as two isoforms corresponding to alternativly spliced variants of the CALU gene (2). Calumenin has been shown to localize to the ER via a carboxy terminal HDEF ER retention signal (3), and undergoes secretion after trafficking through the secretory pathway (4). Secreted calumenin plays a role in amyloidosis by interacting with serum amyloid P component (5). Calumenin is also a chaperone for mutants of the cystic fibrosis transmembrane conductance regulator (CFTR) (6). Researchers performing a proteomics analysis of endometrial cancer identified calumenin as a potential target for endometrial carcinoma (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: GFAT1, glutamine:fructose-6-phosphate aminotransferase 1, is the rate-limiting enzyme of the hexosamine biosynthesis pathway (1). This enzyme catalyzes the conversion of fructose-6-phosphate and glutamine to glucosamine-6-phosphate and glutamate (2). The hexosamine biosynthesis pathway generates the building blocks for protein and lipid glycosylation (2). Furthermore, studies suggest that increased activity of this pathway is a contributing factor to hyperglycemia-induced insulin resistance (1,2). GFAT1 is more active in non-insulin-dependent diabetes mellitus (NIDDM) patients (3). Transgenice mice overexpressing this enzyme in skeletal muscle and adipose tissue show an insulin resistance phenotype (4,5). GFAT2, an isoenzyme of GFAT1, was later identified (6, 7). Studies show that the regulation of GFAT2 is different from that of GFAT1, suggesting differential regulation of the hexosamine pathway in different tissues (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Fetuin A is produced by liver and secreted to plasma, and selectively concentrated in bone matrix. It is synthesized as a precursor and processed to generate 2 chains that are held together by a disulfide bond. It is a systemically acting calcification inhibitor (1). Reduced level of fetuin A in serum is associated with increased cardiovascular mortality in dialysis patients (2,3). Fetuin A can inhibit insulin-induced tyrosine phosphorylation of the insulin receptor tyrosine kinase and insulin receptor substrate-1 (4). Fetuin A deficient mice show high insulin sensitivity and high levels of serum fetuin A are associated with insulin resistance in humans (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Glucose homeostasis is regulated by hormones and cellular energy status. Elevations of blood glucose during feeding stimulate insulin release from pancreatic β-cells through a glucose sensing pathway. Feeding also stimulates release of gut hormones such as glucagon-like peptide-1 (GLP-1), which further induces insulin release, inhibits glucagon release and promotes β-cell viability. CREB-dependent transcription likely plays a role in both glucose sensing and GLP-1 signaling (1). The protein CRTC2 (CREB-regulated transcription coactivator 2)/TORC2 (transducer of regulated CREB activity 2) functions as a CREB co-activator (2,3) and is implicated in mediating the effects of these two pathways (4). In quiescent cells, CRTC2/TORC2 is phosphorylated at Ser171 and becomes sequestered in the cytoplasm via an interaction with 14-3-3 proteins. Glucose and gut hormones lead to the dephosphorylation of CRTC2/TORC2 and its dissociation from 14-3-3 proteins. Dephosphorylated CRTC2/TORC2 enters the nucleus to promote CREB-dependent transcription. CRTC2/TORC2 plays a key role in the regulation of hepatic gluconeogenic gene transcription in response to hormonal and energy signals during fasting (5).CRTC2/TORC2-related proteins CRTC1/TORC1 and CRTC3/TORC3 also act as CREB co-activators (2,3). CRTC1/TORC1, CRTC2/TORC2 and CRTC3/TORC3 associate with the HTLV Tax protein to promote Tax-dependent transcription of HTLV-1 long terminal repeats (6,7). CRTC1/TORC1 is highly phosphorylated at Ser151 in mouse hypothalamic cells under basal conditions (8). When these cells are exposed to cAMP or a calcium activator, CRTC1/TORC1 is dephosphorylated and translocates into the nucleus (8). CRTC1/TORC1 is essential for energy balance and fertility (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Anion exchange protein 1 (AE1), also named solute carrier family 4 member 1 (SLC4A1), is an anion transporter that mediates chloride-bicarbonate exchange in the kidney and regulates normal acidification of the urine (1,2). A different isoform of AE1 is a major integral membrane structure protein of erythrocytes, where it plays a critical role in the removal of carbon dioxide from tissues (3). In addition, AE1 is required for normal flexibility and stability of the erythrocyte membrane. Mutations in SLC4A1 can lead to hereditary spherocytosis, ovalocytosis, and distal renal tubular-acidosis (4-7). Other mutations that do not cause disease became novel blood group antigens, which are part of the Diego blood group system (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Tuberous sclerosis complex (TSC) is an autosomal dominant disorder that causes symptoms including hamartomas in brain, kidney, heart, lung and skin (1). The tumor suppressor genes TSC1 and TSC2 encode hamartin and tuberin, respectively (2,3). Hamartin and tuberin form a functional complex and are involved in numerous cellular activities such as vesicular trafficking, regulation of the G1 phase of the cell cycle, steroid hormone regulation, Rho activation and anchoring neuronal intermediate filaments to the actin cytoskeleton (4-9). The combination of genetic, biochemical and cell-biological studies demonstrate that the tuberin/hamartin complex functions as a GTPase-activating protein for the Ras-related small G protein Rheb and thus inhibits targets of rapamycin including mTOR. Cells lacking hamartin or tuberin fail to inhibit phosphorylation of S6 kinase resulting in the activation of S6 ribosomal protein's translation of 5'TOP mRNA transcripts (10). Hamartin is phosphorylated by CDK1 (cdc2) at Thr417, Ser584 and Thr1047 in cells in G2/M phase of the cell cycle (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Wiskott-Aldrich syndrome proteins (WASPs) mediate actin dynamics by activating the Arp2/3 actin nucleation complex in response to activated Rho family GTPases. In mammals, five WASP family members have been described. Hematopoietic WASP and ubiquitously expressed N-WASP are autoinhibited in unstimulated cells. Upon stimulation they are activated by cdc42, which relieves the autoinhibition in conjunction with phosphatidyl inositol 4,5-bisphosphate. Three WAVE (Wasf, SCAR) family proteins are similar in sequence to WASP and N-WASP but lack the WASP/N-WASP autoinhibition domains and are indirectly activated by Rac (reviewed in 1). Both WASP and WAVE functions appear to be essential, as knockout of either N-WASP or Scar-2 in mice results in cardiac and neuronal defects and embryonic lethality (2,3). Loss of WASP results in immune system defects and fewer immune cells (4). WAVE-2 (WASF2) is widely distributed, while WAVE-1 and WAVE-3 are strongly expressed in brain (5). WAVE-3 may act as a tumor suppressor in neuroblastoma, a childhood disease of the sympathetic nervous system (6). Increased expression of WAVE-3 is seen in breast cancer, and studies in breast adenocarcinoma cells indicate that WAVE-3 regulates breast cancer progression, invasion and metastasis through the p38 mitogen-activated protein kinase (MAPK) pathway (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Host cell factor C1 (HCFC1) was first identified as the host cell factor for human herpes simplex virus infection. HCFC1 and the viral protein VP16 belong to a multi-protein complex that promotes transcription of viral immediate early genes (1). The relatively large HCFC1 protein contains 6 centrally located 26 amino acid repeats that can be O-GlcNAcylated and subjected to O-linked beta-N-acetylglucosamine transferase (OGT) cleavage (2-4). The resulting amino-terminal (HCFC1-N) and carboxy-terminal (HCFC1-C) fragments are non-covalently associated and play important roles in cell cycle regulation. The HCFC1-N peptide facilitates progression through the G1 phase of the cell cycle while HCFC1-C enables proper mitosis and cytokinesis during the M phase (5-7). As HCFC1 plays an important role in neurodevelopment, mutations in the corresponding gene are associated with neurodevelopmental disorders (e.g., intellectual disability) in humans (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: DUSP3, also known as VHR (VH1 related) is a small dual-specific phosphatase with specificity for MAP kinase ERK1/2 and JNK, but not for p38 MAPK (1,2). Unlike most of the dual-specific phosphatases, which have inducible expression patterns, DUSP3 is constitutively expressed (2). In antigen stimulated T cells, DUSP3 is phosphorylated by ZAP-70 at Tyr138 (3). Tyr138 phosphorylation is required for DUSP3 to down-regulate the ERK and JNK pathways (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: PTP-PEST is a ubiquitously expressed cytosolic protein tyrosine phosphatase with multiple proline-rich regions that appear to be the docking sites for PTP-PEST binding partners or substrates (1). PTP-PEST regulates fibroblast adhesion, migration, and cytokinesis through its association with and dephosphorylation of p130 Cas, paxillin, PSTPIP1, WASP, and other adhesion molecules (1-5). By modulating phosphorylation states of Shc, Pyk2, Fak, and WASP, PTP-PEST negatively regulates lymphocyte activation (1,6). In mammary epithelial cells, EGF facilitates the dephosphorylation of Jak2 by PTP-PEST, thereby interfering with lactogenic hormone PRL signaling (7). PTP-PEST dephosphorylates c-Abl as well, which affects the phosphorylation states of PTP-PEST substrates such as paxillin, p130 Cas, Crk, and PSTPIP1 (8).PTP-PEST regulates adhesion and motility of cultured epithelial cells through modulation of Rho GTPase activity (9), and is required for integrin-mediated endothelial cell adhesion and migration (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Non-T cell activation linker (NTAL)/linker for activation of B cells (LAB) is a small transmembrane adaptor protein associated with glycolipid-enriched membrane fractions (1,2). NTAL/LAB is also known as LAT2 (linker for activation of T cells 2), WBSCR5, WBS15, and WBSCR15 (Williams-Beuren syndrome chromosome region 15 protein). It is expressed in B cells, monocytes, mast cells, and natural killer cells, but not in resting T cells (3). Upon activation of several receptors, NTAL/LAB becomes tyrosine-phosphorylated and recruits signaling molecules such as GRB2 and c-Cbl into receptor signaling complexes (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Thioredoxin is a small redox protein found in many eukaryotes and prokaryotes. A pair of cysteines within a highly conserved, active site sequence can be oxidized to form a disulfide bond that is then reduced by thioredoxin reductase (1). Multiple forms of thioredoxin have been identified, including cytosolic thioredoxin 1 (TRX1) and mitochondrial thioredoxin 2 (TRX2). Thioredoxin participates in many cellular processes including redox signaling, response to oxidative stress, and protein reduction (1). A potential role of thioredoxin in human disorders such as cancer, aging, and heart disease is currently under investigation (2). Thioredoxin can play a key role in cancer progression, because it acts as a negative regulator of the proapoptotic kinase ASK1 (3). Changes in thioredoxin expression have been associated with meningococcal septic shock and acute lung injury (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. Control of autophagy was largely discovered in yeast and involves proteins encoded by a set of autophagy-related genes (Atg) (1). Formation of autophagic vesicles requires a pair of essential ubiquitin-like conjugation systems, Atg12-Atg5 and Atg8-phosphatidylethanolamine (Atg8-PE), which are widely conserved in eukaryotes (2). Numerous mammalian counterparts to yeast Atg proteins have been described, including three Atg8 proteins (GATE-16, GABARAP, and LC3) and four Atg4 homologs (Atg4A/autophagin-2, Atg4B/autophagin-1, Atg4C/autophagin-3, and Atg4D/autophagin-4) (3-5). The cysteine protease Atg4 is pivotal to autophagosome membrane generation and regulation. Atg4 primes the Atg8 homolog for lipidation by cleaving its carboxy terminus and exposing its glycine residue for E1-like enzyme Atg7. The Atg8 homolog is transferred to the E2-like enzyme Atg3 before forming the Atg8-PE conjugate. During later stages of autophagy, Atg4 can reverse this lipidation event by cleaving PE, thereby recycling the Atg8 homolog (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: ACE2 is a carboxypeptidase that catalyses the conversion of angiotensin I to angiotensin 1-9, or of angiotensin II to the vasodilator angiotensin 1-7 (1). ACE2 is a critical component in the renin-angiotensin system (RAS). ACE2 is predominantly expressed in vascular endothelial cells of the heart and kidney and Leydig and Sertoli cells of the testis (2,3). The unique expression pattern of ACE2 determines its essential role in the regulation of cardiovascular and kidney functions, as well as fertility. ACE2 protein is localized mainly in the extracellular space with its carboxy terminal end attached to the membrane via its transmembrane domain. Active ACE2 enzyme is secreted by cleavage at the amino terminus. Research studies have shown that ACE2 expression is elevated in human failing heart (4). ACE2 is also a functional receptor for SARS coronavirus (SARS-CoV) (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

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

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

Application Methods: Western Blotting

Background: The polycomb group (PcG) of proteins contributes to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). Bmi1 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7). Bmi1 plays an important role in the regulation of cell proliferation and senescence through repression of the p16 INK4A and p19 ARF genes and is required for maintenance of adult hematopoietic and neural stem cells (3,4,8-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The methylation state of lysine residues in histone proteins is a major determinant of the formation of active and inactive regions of the genome and is crucial for proper programming of the genome during development (1,2). Jumonji C (JmjC) domain-containing proteins represent the largest class of potential histone demethylase proteins (3). The JmjC domain can catalyze the demethylation of mono-, di-, and tri-methyl lysine residues via an oxidative reaction that requires iron and α-ketoglutarate (3). Based on homology, both humans and mice contain at least 30 such proteins, which can be divided into 7 separate families (3). The jumonji domain-containing protein 2 (JMJD2) family, also known as the JmjC domain-containing histone demethylation protein 3 (JHDM3) family, contains four members: JMJD2A/JHDM3A, JMJD2B/JHDM3B, JMJD2C/JHDM3C, and JMJD2D/JHDM3D. In addition to the JmjC domain, these proteins also contain JmjN, PHD, and tudor domains, the latter of which has been shown to bind to methylated histone H3 at Lys4 and Lys9, and methylated histone H4 at Lys20 (4,5). JMJD2 proteins have been shown to demethylate di- and tri-methyl histone H3 at Lys9 and Lys36 and function as both activators and repressors of transcription (6-11). JMJD2A, JMJD2C, and JMJD2D function as coactivators of the androgen receptor in prostate tumor cells (7). In contrast, JMJD2A also associates with Rb and NCoR corepressor complexes and is necessary for transcriptional repression of target genes (8,9). JMJD2B antagonizes histone H3 Lys9 tri-methylation at pericentric heterochromatin (10). JMJD2C, also known as GASC1, is amplified in squamous cell carcinomas and metastatic lung carcinoma and inhibition of JMJD2C expression decreases cell proliferation (11,12). JMJD2C has also been identified as a downstream target of Oct-4 and is critical for the regulation of self-renewal in embryonic stem cells (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The neurological condition Dystonia is associated with sustained muscle contractions and abnormal posturing (1). TorsinA, torsinB, torp2A and torp3A belong to the family of ATPases associated with cellular activites (AAA+) and mutations in torsinA cause early onset dystonia (2). TorsinA has been shown to suppress intracellular protein aggregation in C. elegans and possesses chaperon activity. Interestingly, torsinA is highly expressed in dopaminergic neurons and associates with alpha-synuclein in Lewy bodies, which pathologically characterize Parkinson's Disease (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Stable Tubule Only Polypeptide (STOP) is a microtubule-associated protein, and its microtubule-stabilizing activity is regulated by calmodulin (1-2). STOPs have several tissue- and developmental-specific isoforms that are encoded by a single gene. Neurons express N-STOP (exons 1-4) and E-STOP (exons 1-3), fibroblasts express F-STOP (exons 1-2), oligodendrocytes express O-STOP, and astrocytes A-STOP (3). STOPs are the major contributors stabilizing microtubules that resist depolymerization due to cold or depolymerizing drugs. STOP knock-out mice display impaired synaptic plasticity associated with severe behavioral disorders in contrast to the anticipated neuronal development and brain anatomy defects (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: SH2-containing inositol phosphatase 1 (SHIP1) is a hematopoietic phosphatase that hydrolyzes phosphatidylinositol-3,4,5-triphosphate to phosphatidylinositol-3,4-bisphosphate (1). SHIP1 is a cytosolic phosphatase with an SH2 domain in its amino terminus and two NPXY Shc binding motifs in its carboxy terminus (1,2). Upon receptor cross-linking, SHIP is first recruited to the membrane junction through binding of its SH2 domain to the phospho-tyrosine in the ITIM motif (2), followed by tyrosine phosphorylation on the NPXY motif (2). The membrane relocalization and phosphorylation on the NPXY motif is essential for the regulatory function of SHIP1 (3-5). Its effect on calcium flux, cell survival, growth, cell cycle arrest, and apoptosis is mediated through the PI3K and Akt pathways (3-5). Tyr1021 is located in one of the NPXY motifs in SHIP1, and its phosphorylation is important for SHIP1 function (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Lyric/AEG-1 (Astrocyte Elevated Gene 1)/MTDH (Metadherin) was identified as a tight junction (TJ) protein based on its localization to TJ proteins in polarized epithelium (1).Differential subcellular localization and overexpression of Lyric/AEG-1/MTDH has been seen in multiple human cancers. Lyric/AEG-1/MTDH is involved in signaling pathways related to various cellular functions including proliferation and apoptosis/survival, and its alteration in cancer is associated with poor prognosis (reviewed in 2). In breast cancer, increased Lyric/AEG-1/MTDH may confer increased chemoresistance as well as metastasis (3,4). Lyric/AEG-1/MTDH expression is important in signaling and disease progression of hepatocellular carcinoma (HCC) (5) and glioblastoma multiforme (GBM) (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: INCENP (inner centromere protein antigens 135 kDa, 155 kDa) is a chromosomal passenger protein crucial for multiple events that mediate chromosome separation during mitosis (1). At prophase INCENP is associated with chromatin whereas during prometaphase and metaphase it translocates to the inner centromere (1). Depletion of INCENP results in aberrant chromosome alignment at the metaphase plate, incomplete chromosome separation, and disruption of proper spindle formation and cytokinesis (2). INCENP is part of the chromosomal passenger complex that also contains Aurora B, borealin and survivin (2). Aurora B and INCENP are mutually dependent on each other for proper localization (3), and in Drosophila cells and C.elegans embryos that lack INCENP or survivin, Aurora B cannot organize the kinetochores and the midbody (4,5). Phosphorylation on INCENP by CDK1 on Thr59 and Thr388 leads to the association of INCENP with Plk1, another important regulator of mitotic entry and exit (6). Interaction of INCENP with Plk1 is necessary for recruitment of Plk1 to the kinetochores, and the metaphase to anaphase transition (6). Interactions have also been reported between INCENP and heterochromatin protein 1α (HP1) (7) and β-tubulin (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: SNIP (SNAP25-interacting protein)/p140Cap (p130Cas-associated protein) is a cytoskeleton-associated protein identified initially in rat as a protein interacting with the brain-specific synaptosome protein SNAP25 (1) and subsequently as interacting with the broadly expressed scaffold protein p130Cas (2). SNAP25, a presynaptic protein implicated in neurotransmitter secretion, membrane fusion and neurite outgrowth, is part of the SNARE complex that includes syntaxin and synaptobrevin/VAMP (3). SNIP-SNAP25 association is mediated by coiled-coil interactions (1). Overexpression of SNIP inhibits calcium-dependent exocytosis in PC12 cells (1). Human and mouse orthologs of SNIP, termed p140Cap, were subsequently identified through association with p130Cas, a substrate of v-Src and v-Crk that is tyrosine-phosphorylated in response to cell adhesion and mitogenic stimuli (2,4,5). Expression of p140Cap was observed in brain, testis and epithelial-rich tissues and may exist in various alternatively spliced, tissue-specific isoforms (2). p140Cap is also tyrosine-phosphoryalated in response to adhesion molecules and EGF treatment (2). Together these studies suggest a role for SNIP/p140Cap in controlling cell spreading, migration and neurosecretion.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: FYVE-CENT (ZFYVE26) contains an FYVE zinc finger domain characterized by conserved R(R/RK) and HHCRxCG motifs (1). Phosphatidylinositol 3 phosphate binds to FYVE-CENT via the FYVE domain and this binding is crucial in phosphoinositide (PtdIns3P)-regulated cytokinesis (1-3). Research evidence suggests that during cytokinesis, FYVE-CENT directly interacts with TTC19 and is recruited to the midbody by the kinesin protein KIF13A (4). FYVE-CENT may also be involved in the tumor suppressor function of Beclin-1 (5). Researchers have linked the defects in FYVE-CENT to hereditary spastic paraplegia, a condition characterized by deterioration of the corpus callosum of the brain (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TTK (Mps1, PYT) is a cell cycle regulated dual specificity kinase present in rapidly proliferating tissues and cell lines (1-3). TTK localizes to kinetochores and centromeres and is an essential component of the mitotic spindle checkpoint as well as centrosome duplication (4-6). The mitotic checkpoint inhibits entry into anaphase until all chromosomes are attached to the spindle; inhibition of this process leads to genomic instability and tumorigenesis. Phosphorylation of the BLM helicase at Ser144 by TTK maintains chromosome stability during mitosis (7). Small molecule inhibitors of TTK can block the spindle checkpoint response, thereby making TTK a potential therapeutic target (8,9).TTK also participates in the DNA damage response by directly phosphorylating and activating the cell cycle checkpoint kinase Chk2 at Thr68. Two targets phosphorylated by Chk2 are the cell cycle phosphatase cdc25 and the transcription factor p53. Inactivation of cdc25 phosphatase results in the accumulation of inactive cyclin B and cell cycle arrest following DNA damage. Phosphorylation of p53 by active Chk2 stabilizes the transcription factor and promotes cell cycle arrest and apoptosis in response to DNA damage (10).

$193
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to FITC and tested in-house for direct flow cytometry analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

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