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Product listing: CD133 (D2V8Q) XP® Rabbit mAb, UniProt ID O43490 #64326 to GATA-1 (D52H6) XP® Rabbit mAb (PE Conjugate), UniProt ID P15976 #13353

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CD133, also known as Prominin, was first described as a cell surface marker recognized by monoclonal antibody AC133 on putative hematopoietic stem cells (1). Subsequent cDNA cloning indicated that CD133 is a five-transmembrane protein with a predicated molecular weight of 97 kDa. Due to heavy glycosylation, its apparent molecular weight is 130 kDa as determined by SDS-PAGE analysis (2). Besides blood stem cells, CD133 is expressed on and used to isolate other stem cells, including cancer stem cells (3-7). A deletion mutation in CD133 produces aberrant protein localization and may result in retinal degeneration in humans (8).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CD133, also known as Prominin, was first described as a cell surface marker recognized by monoclonal antibody AC133 on putative hematopoietic stem cells (1). Subsequent cDNA cloning indicated that CD133 is a five-transmembrane protein with a predicated molecular weight of 97 kDa. Due to heavy glycosylation, its apparent molecular weight is 130 kDa as determined by SDS-PAGE analysis (2). Besides blood stem cells, CD133 is expressed on and used to isolate other stem cells, including cancer stem cells (3-7). A deletion mutation in CD133 produces aberrant protein localization and may result in retinal degeneration in humans (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: SSEA-1 antibody detects a lactoseries oligosaccharide antigen that is expressed on the surface of mouse embryonal carcinoma and embryonic stem cells (1). This antigen is also found on early mouse embryos and both mouse and human germ cells, but is absent on human embryonic stem cells and human embryonic carcinoma cells. Expression of SSEA1 in these human cell types increases upon differentiation, while on the mouse cell types differentiation leads to decreased expression (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CDX2, a homeobox domain-containing transcription factor, is a master regulator of the trophoectoderm, the layer that gives rise to extra-embryonic tissues in mammalian development (1). CDX2 is also involved in intestinal development (2), and gain of expression or loss of expression has been associated with various human malignancies such as Barret Esophagus (3) and colorectal cancer (4,5). Mouse embryonic stem cells deficient in CDX2 display limited hematopoietic progenitor development and altered Hox gene expression (6), pointing to a role for CDX2 in Hox gene regulation. CDX2 is also implicated in the aberrant expression of Hox genes in human AML cell lines (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: CELSR2 (cadherin EGF LAG seven-pass G-type receptor, also known as flamingo homolog 3 or epidermal growth factor-like protein 2) is a member of the flamingo subfamily of non-classical cadherins, part of the cadherin superfamily. CELSR2 is a 7-transmembrane helix receptor that contains nine cadherin-like domains, seven EGF-like repeats, and 2 laminin A G-type repeats (1). It shares structural characteristics of both an adhesion molecule and a G protein-coupled receptor, suggesting putatives roles in both cell-cell adhesion and juxtacrine signaling. It's function has been associated with dendrite morphogenesis (2), neural plate anterior-posterior pattern formation (3), and regulation of transcription via the Wnt signaling pathway (4). In a loss-of-function mouse model, Celsr2 deletion resulted in defects in the planar organization of ependymal cilia, leading to defective cerebrospinal fluid dynamics and hydrocephalus (5). In humans, SNPs in the CELSR2 gene cluster on chromosome 1 have been associated with enhanced risk of coronary artery disease (6).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Notch proteins (Notch1-4) are a family of transmembrane receptors that play important roles in development and the determination of cell fate (1). Mature Notch receptors are processed and assembled as heterodimeric proteins, with each dimer comprised of a large extracellular ligand-binding domain, a single-pass transmembrane domain, and a smaller cytoplasmic subunit (Notch intracellular domain, NICD) (2). Binding of Notch receptors to ligands of the Delta-Serrate-Lag2 (DSL) family triggers heterodimer dissociation, exposing the receptors to proteolytic cleavages; these result in release of the NICD, which translocates to the nucleus and activates transcription of downstream target genes (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cripto, also known as teratocarcinoma derived growth factor 1 (TDGF-1), belongs to the EGF-CFC family of proteins. Members of this family are characterized by an N-terminal signal peptide, a conserved cysteine rich domain (CFC motif), and a short hydrophobic carboxy-terminal tail that contains GPI cleavage and attachment sites. The GPI moiety anchors Cripto and family members to the extracellular plasma membrane (1). An O-linked fucosylation site within the EGF-like motif is required for Cripto and related family members to perform their function as co-receptors for TGF-β-related ligands such as Nodal and Vg1/GDF1 (2,3). Soluble forms of Cripto can be produced - these contain intact EGF and CFC domains, and are thought to have paracrine activities, as opposed to the autocrine activity of Cripto functioning as a coreceptor (4). Understanding of this paracrine activity is not complete, but it is proposed that Cripto may act as co-ligand for Nodal (3).Cripto is an important modulator of embryogenesis and oncogenesis (4). It is highly expressed in early embryos, and in embryonic stem (ES) cells where it is involved in cardiomyocytic differentiation and acts as a negative regulator of neurogenesis (5-7). Transient activation of Cripto is essential for the capacity of stem cell self-renewal and pluripotency in ES cells, and in some adult derived stem cells (8). Signaling through Cripto can also stimulate other activities that promote tumorigenesis such as stimulation of proliferation, cell motility, invasion, angiogenesis and epithelial-mesenchymal transition (EMT) (9-11). Cripto is highly expressed in a broad range of tumors, where it acts as a potent oncogene.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: CtBP1 (C-terminal binding protein 1) was first recognized as a cellular factor that interacts with the C-terminal portion of adenovirus E1A, a protein involved in the transcriptional regulation of key cellular genes (1). CtBP1 is able to regulate gene activity through its intrinsic dehydrogenase activity (2,3) and by interacting with Polycomb Group (PcG) proteins during development (4). Along with its homologue, CtBP2, it acts as a transcriptional corepressor of zinc-finger homeodomain factor deltaEF1 to regulate a wide range of cellular processes through transrepression mechanisms (5). Through its direct interaction with PRDM16, CtBP1 has been shown to be involved in brown adipose tissue differentiation by mediating the repression of white fat genes and directing differentiation toward the brown fat gene program (6). CtBP1 also plays a role in lipid metabolic pathways and membrane fission by regulating the fission machinery operating Golgi tubular networks (7). CtBP1 has recently been shown to repress transcription of BRCA1 via a redox regulated mechanism (8). Furthermore, it is thought that downregulation of BRCA1 and E-cadherin in invasive ductal breast carcinoma correlates directly with activation of CtBP1 (9).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin)

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Dickkopf (DKK) family proteins consist of four members DKK1, DKK2, DKK3 and DKK4 that function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5 and LRP6 (1,2). DKKs contain two cysteine-rich domains in which the positions of 10 cysteine residues are well conserved (3). Their expression is both temporally and spatially regulated during animal development (4). DKKs also bind with high affinity to transmembrane proteins Kremen1 and 2, which themselves also modulate Wnt signaling (5,6).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Notch signaling is activated upon engagement of the Notch receptor with its ligands, the DSL (Delta, Serrate, Lag2) proteins of single-pass type I membrane proteins. The DSL proteins contain multiple EGF-like repeats and a DSL domain that is required for binding to Notch (1,2). Five DSL proteins have been identified in mammals: Jagged1, Jagged2, Delta-like (DLL) 1, 3 and 4 (3). Ligand binding to the Notch receptor results in two sequential proteolytic cleavages of the receptor by the ADAM protease and the γ-secretase complex. The intracellular domain of Notch is released and then translocates to the nucleus where it activates transcription. Notch ligands may also be processed in a way similar to Notch, suggesting a bi-directional signaling through receptor-ligand interactions (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Notch signaling is activated upon engagement of the Notch receptor with its ligands, the DSL (Delta, Serrate, Lag2) proteins of single-pass type I membrane proteins. The DSL proteins contain multiple EGF-like repeats and a DSL domain that is required for binding to Notch (1,2). Five DSL proteins have been identified in mammals: Jagged1, Jagged2, Delta-like (DLL) 1, 3 and 4 (3). Ligand binding to the Notch receptor results in two sequential proteolytic cleavages of the receptor by the ADAM protease and the γ-secretase complex. The intracellular domain of Notch is released and then translocates to the nucleus where it activates transcription. Notch ligands may also be processed in a way similar to Notch, suggesting a bi-directional signaling through receptor-ligand interactions (4-6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Dishevelled (Dsh) proteins are important intermediates of Wnt signaling pathways. Dsh inhibits glycogen synthase kinase-3β promoting β-catenin stabilization. Dsh proteins also participate in the planar cell polarity pathway by acting through JNK (1,2). There are three Dsh homologs, Dvl1, Dvl2 and Dvl3 in mammals. Upon treatment with Wnt proteins, Dvls become hyperphosphorylated (3) and accumulate in the nucleus (4). Dvl proteins also associate with actin fibers and cytoplasmic vesicular membranes (5) and mediate endocytosis of the Fzd receptor after Wnt protein stimulation (6). Overexpression of Dvl has been reported in certain cancers (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: E-Ras (Embryonic Ras) is a member of the Ras family that includes K-Ras, N-Ras, and H-Ras. E-Ras is expressed in early mouse blastocysts and murine embryonic stem cells and is down-regulated upon differentiation (1). Amino acid substitutions as a result of mutation at three conserved positions in K-, H-, N-, and R-Ras proteins result in constitutive activation of these small GTPases, and oncogenic transformation. Intriguingly, the Eras gene encodes a protein where each of these amino acids are substituted, and so E-Ras is naturally constitutively active. E-Ras is thought to contribute to the tumorigenic potential of mouse ES cells to form teratomas in immunodeficient or isogenic mice (1). Despite the parallels between oncogenic mutated Ras, major differences in signaling exist between H-Ras G12V and E-Ras. While H-Ras G12V highly activates the MAPK pathway, E-Ras cannot bind to Raf1 to activate this pathway. Instead, E-Ras signals through PI3K to activate Akt (1). E-Ras is not expressed in human embryonic stem cells, nor is it is expressed in any adult tissues as found thus far (2). Reports have suggested it may be expressed in several tumor types, including gastric cancer (1,2,3). Researchers have speculated on the role of E-Ras in the early mouse blastocyst. Preimplantation embryos can survive in tissue culture in defined medium until the blastocyst stage without any requirement for serum or growth factors. Preimplantation embryos have a requirement for PI3K signaling, and in the absence of exogenous signals, E-Ras has been suggested to be the effector of this signal transduction (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: FAM3C, also known as ILEI (interleukin-like epithelial-to-mesenchymal transition [EMT] inducer), is a cytokine-like protein and member of the FAM3 family. FAM3C plays an important role in EMT and metastasis during cancer progression in human and mouse cells, and is highly expressed in human cancer (1,2). In colorectal cancer, researchers have indicated that FAM3C is a marker for EMT and tumor progression, and that high expression of FAM3C is predictive of poor prognosis (3). While EMT induction by FAM3C can be independent of TGF-beta, research studies have also shown TGF-beta-dependent regulation of FAM3C expression at the translational level in mouse and human cells (4,5).FAM3C has also been linked to regulation of osteoblast differentiation (6), and to accumulation of amyloid beta plaques in Alzheimer’s disease (7). FAM3C exists in monomeric and in homodimeric form, and research shows that FAM3C homodimers contain its EMT-inducing and tumor promoting activity (8).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: FGF19 is a member of the large and diverse Fibroblast Growth Factor (FGF) family of peptide growth factors. FGF19 functions as a high affinity ligand for the FGF4 receptor, to which it binds in a heparin-dependent manner (1). Under normal physiological conditions, FGF19 is produced in the ileum when absorbed bile acids bind to the farnesoid X receptor (FXR), activating transcription of the FGF19 gene. FGF19 in turn functions in a negative feedback fashion to regulate bile acid synthesis (2). Consequently, disruptions in FGF19 signaling have been linked with clinical defects in bile acid synthesis, which may manifest as primary bile acid diarrhea or cholestasis (3,4). Research studies in oncology have shown that FGF19 can function in an endocrine, paracrine or autocrine fashion to promote tumorigenesis. In human studies, this has been demonstrated for breast cancer (5), gastric cancer (6) prostate cancer (7, 8), and hepatocellular carcinoma (9). Similar tumorigenic effects have been described for the mouse ortholog (Fgf15), notably in genetic models of hepatocellular carcinoma (10, 11)

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

Application Methods: Western Blotting

Background: FIH (Factor inhibiting HIF-1, HIF asparagine hydroxylase) is a dioxygen-dependent asparaginyl hydroxylase that modifies target protein function by hydroxylating target protein asparagine residues (1-3). Hypoxia-inducible factor (HIF), a transcriptional activator involved in control of cell cycle in response to hypoxic conditions, is an important target for FIH regulation. FIH functions as an oxygen sensor that regulates HIF function by hydroxylating at Asn803 in the carboxy-terminal transactivation domain (CAD) of HIF (4,5). During normoxia, FIH uses cellular oxygen to hydroxylate HIF-1 and prevent interaction of HIF-1 with transcriptional coactivators, including the CBP/p300-interacting transactivator. Under hypoxic conditions, FIH remains inactive and does not inhibit HIF, allowing the activator to regulate transcription of genes in response to low oxygen conditions (4-6). FIH activity is regulated in through interaction with proteins, including Siah-1, which targets FIH for proteasomal degradation (7). The Cut-like homeodomain protein CDP can bind the FIH promoter region to regulate FIH expression at the transcriptional level (8). Phosphorylation of HIF at Thr796 also can prevent FIH hydroxylation on Asn803 (9). Potential FIH substrates also include proteins with ankyrin repeat domains, such as Iκ-B, Notch, and ASB4 (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Friend leukemia integration 1 (FLI1) transcription factor is an ETS domain-containing transcription factor that plays an important and highly conserved role in vertebrate development, particularly hematopoiesis, where it functions to activate transcription of genes that promote erythroblast proliferation (1-4). In mice, the Fli1 locus is a common retroviral insertion site for the Friend murine leukemia virus (F-MuLV), such that a majority of F-MuLV-induced erythroleukemias are associated with aberrant Fli1 expression (5). Notably in humans, aberrant FLI1 expression has also been linked to poor prognosis in acute myeloid leukemia (6). Also in humans, a t(11;22)(q24;q12) chromosomal translocation has been described that generates a chimeric protein (EWS/FLI1) comprised of the amino-terminal transactivation domain of Ewing's sarcoma breakpoint region 1 (EWS) and the carboxy-terminal ETS domain of FLI1 (7). The EWS/FLI1 fusion protein functions as a transcriptional activator that is reportedly responsible for >85% of the known cases of pediatric Ewing’s sarcoma, an aggressive bone and soft tissue tumor (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors defined by the presence of a winged helix DNA binding domain called a Forkhead box (1). In humans, there are over 40 known Fox protein family members, divided into 19 subfamilies, which have evolved to regulate gene transcription in diverse and highly specialized biological contexts throughout development (2). Mutations that disrupt the expression of Fox gene family members have consequently been implicated in a broad array of human disorders, including immunological dysfunction, infertility, speech/language disorders, and cancer (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: FoxD3 is a member of the Forkhead Box family and is characterized by a winged-helix DNA-binding structure and the important role it plays in embryonic development (1). This transcriptional regulator is required for the maintenance of pluripotency in the pre-implantation and peri-implantation stages of mouse embryonic development (2) and is also required for trophoblast formation (3). FoxD3 is required for the maintenance of the mammalian neural crest; FoxD3(-/-) mouse embryos fail around the time of implantation with loss of neural crest-derived structures (4). FoxD3 also forms a regulatory network with Oct-4 and NANOG to maintain the pluripotency of ES cells (5,6).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated FoxP1 (D35D10) XP® Rabbit mAb #4402.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).

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

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

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Frizzled (Fzd) belongs to the seven transmembrane-spanning G-protein-coupled receptor (GPCR) superfamily (1). Fzds have a large extracellular N-terminal region containing a cysteine-rich domain (CRD), which is involved in binding to Wnt proteins (1,2). The intracellular C-terminus binds to the PDZ domain of Dvl proteins, a major signaling component downstream of Fzd (3). Wnt proteins bind to Fzd and the co-receptors LRP5 or LPR6, and activate Wnt/β-catenin pathway through inhibiting phosphorylation of β-catenin by GSK3-β (4,5). In addition to this canonical Wnt/β-catenin pathway, some Wnt proteins can also activate the Fzd/Ca2+ pathway and Fzd/PCP (planar cell polarity) pathway (6,7). The mammalian Fzd subfamily has 10 members (Fzd1 to Fzd10) and they may mediate signaling through different pathways (8). Some Fzds can also bind to other secreted proteins, like Norrin and R-Spondin (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Frizzled (Fzd) belongs to the seven transmembrane-spanning G-protein-coupled receptor (GPCR) superfamily (1). Fzds have a large extracellular N-terminal region containing a cysteine-rich domain (CRD), which is involved in binding to Wnt proteins (1,2). The intracellular C-terminus binds to the PDZ domain of Dvl proteins, a major signaling component downstream of Fzd (3). Wnt proteins bind to Fzd and the co-receptors LRP5 or LPR6, and activate Wnt/β-catenin pathway through inhibiting phosphorylation of β-catenin by GSK3-β (4,5). In addition to this canonical Wnt/β-catenin pathway, some Wnt proteins can also activate the Fzd/Ca2+ pathway and Fzd/PCP (planar cell polarity) pathway (6,7). The mammalian Fzd subfamily has 10 members (Fzd1 to Fzd10) and they may mediate signaling through different pathways (8). Some Fzds can also bind to other secreted proteins, like Norrin and R-Spondin (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: FERM domain-containing protein 6 (FRMD6, Willin) belongs to the 4.1 superfamily, a group of proteins characterized by the presence of a Band 4.1, Ezrin, Radixin, Moesin (FERM) domain in the amino-terminal region (1). Members of this protein superfamily, which also includes Merlin, Ezrin, Radixin, Moesin and Talin, function primarily as adaptor proteins that link plasma membrane-associated proteins to the actin cytoskeleton (2). FRMD6 is considered orthologous to the Drosophila Expanded (Ex) protein, which is a 4.1 family protein that functions together with Merlin and Kibra to regulate Hippo signaling, upstream of the Salvador/Warts/Hippo core kinase cassette (3). Research studies suggest a similar role for FRMD6 in regulating the Hippo pathway in mammals. For example, ectopic expression of FRMD6 leads to increased phosphorylation of MST1/2, LATS1, and YAP, which is indicative of Hippo pathway activation. Loss of FRMD6 expression in MCF10A cells induces a phenotype change resembling epithelial-mesenchymal transition (4).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: GAS6 (Growth Arrest Specific gene 6) is a vitamin K-dependent ligand of the TAM (Tyro3, Axl and MerTK) RTK family. It has an N-terminal Gla domain containing multiple Asp gamma-carboxylation sites, followed by four EGF repeats and two C-terminal LG domains. Vitamin K mediates multiple gamma-carboxylations of glutamic acid residues in the GAS6 Gla domain. These modifications are required for GAS6 to to activate its receptor (1,2). The two C-terminal LG (SHBG) domains form a V-shaped structure and provide a direct binding site for receptor interaction. Among the TAM family members, GAS6 has high affinity for Axl and low affinity for Tyro3 and MerTK. Ligand/receptor interaction activates multiple downstream signaling pathways such as PI3K/AKT, STAT/SOCS, PLC/FAK, and Grb2/RAS, and promotes cell survival, proliferation, migration and differentiation (3,4). GAS6 has been implicated in cancer development and immune-related disorders (inflammation and multiple sclerosis), and as such has been identified as a potential therapeutic target (3-6).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

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

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated GATA-1 (D52H6) XP® Rabbit mAb #3535.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

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