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Product listing: RUNX2 (D1L7F) Rabbit mAb (PE Conjugate), UniProt ID Q13950 #98059 to Snail (SN9H2) Rat mAb, UniProt ID O95863 #4719

$305
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 RUNX2 (D1L7F) Rabbit mAb #12556.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Runt-related transcription factor 2 (RUNX2) is a member of the RUNX family of transcription factors. It is involved in osteoblast differentiation and skeletal morphogenesis. RUNX2 regulates the transcription of various genes, including osteopontin, bone sialoprotein, and osteocalcin, via binding to the core site of the enhancers or promoters (1-3). RUNX2 is crucial for the maturation of osteoblasts and both intramembranous and endochondral ossification. Mutations in the corresponding RUNX2 gene have been associated with the bone development disorder cleidocranial dysplasia (CCD) (4-6). RUNX2 is also abnormally expressed in various human cancers including prostate cancer and breast cancer. It plays an important role in migration, invasion, and bone metastasis of prostate and breast cancer cells (7-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Runt-related transcription factor 2 (RUNX2) is a member of the RUNX family of transcription factors. It is involved in osteoblast differentiation and skeletal morphogenesis. RUNX2 regulates the transcription of various genes, including osteopontin, bone sialoprotein, and osteocalcin, via binding to the core site of the enhancers or promoters (1-3). RUNX2 is crucial for the maturation of osteoblasts and both intramembranous and endochondral ossification. Mutations in the corresponding RUNX2 gene have been associated with the bone development disorder cleidocranial dysplasia (CCD) (4-6). RUNX2 is also abnormally expressed in various human cancers including prostate cancer and breast cancer. It plays an important role in migration, invasion, and bone metastasis of prostate and breast cancer cells (7-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Runt-related transcription factor 3 (RUNX3, AML2), a member of the Runt family of transcription factors, plays an important role in the suppression of gastric epithelium cell proliferation (1), dorsal root ganglia neurogenesis (2), and T cell differentiation (3,4). RUNX3 is also involved in caspase-3-dependent apoptosis (5). Protein complexes containing RUNX3 and various transcription factors, such as Smads or β-catenin/TCF4, have tumor suppressor activity and regulate downstream target gene transcription (6,7). While typically localized to the nucleus, RUNX3 can be tyrosine phosphorylated and located in the cytoplasm of many cancer cells. This mislocalization of RUNX3 abolishes its tumor suppressor function and contributes to tumorigenesis (8). Research studies indicate that gene silencing or protein mislocalization inactivates RUNX3 in more than 80% of gastric cancers and other cancer types (1,9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Runt-related transcription factor 3 (RUNX3, AML2), a member of the Runt family of transcription factors, plays an important role in the suppression of gastric epithelium cell proliferation (1), dorsal root ganglia neurogenesis (2), and T cell differentiation (3,4). RUNX3 is also involved in caspase-3-dependent apoptosis (5). Protein complexes containing RUNX3 and various transcription factors, such as Smads or β-catenin/TCF4, have tumor suppressor activity and regulate downstream target gene transcription (6,7). While typically localized to the nucleus, RUNX3 can be tyrosine phosphorylated and located in the cytoplasm of many cancer cells. This mislocalization of RUNX3 abolishes its tumor suppressor function and contributes to tumorigenesis (8). Research studies indicate that gene silencing or protein mislocalization inactivates RUNX3 in more than 80% of gastric cancers and other cancer types (1,9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Members of the SALL gene family encode putative zinc finger transcription factors highly expressed during development (1). Sall4 is expressed very early in development with other pluripotency regulators, such as Oct-4 and Nanog (2). Recent studies suggest Sall4 works as a master regulator that controls its own expression and the expression of Oct-4 in a transcriptional regulation feedback loop governing stem cell pluripotency and stem cell fate (2,3). Immunohistochemical studies indicate that Sall4 is a sensitive and specific diagnostic marker for primary germ cell tumors and yolk sac tumors (4,5). Research studies have shown that Sall4 is constitutively expressed in acute myeloid leukemia (AML) and is a probable effector of the Wnt/β-catenin signaling pathway in this disease (6). In addition, mutations in Sall4 have been implicated in human malformation syndromes including Duane-radial ray syndrome (Okihiro syndrome) and Acro-renal-ocular syndrome (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Smad anchor for receptor activation (SARA, ZFYVE9) protein is an FYVE domain-containing protein originally identified as a regulator of TGF-β signaling (1). FYVE domains are zinc finger-like domains that bind to phosphatidylinositol 3-phosphate and are responsible for endosomal trafficking (2). While the role of Sara in TGF-β signaling has been questioned (3,4), early research studies demonstrate that Sara enhances TGF-β signaling by binding and recruiting non-activated Smad2 and Smad3 to the TGF-β receptor complex (1). Upon Smad2 activation, Sara dissociates from the complex while phosphorylated Smad2/3 translocates to the nucleus to bind to the common Smad, Smad4. Sara can also function as an anchor for the protein phosphatase 1 (PP1c) catalytic subunit, which is involved in the Smad7-mediated dephosphorylation of TGF-β type I receptor (5,6). Additional research studies show that expression of Sara plays a critical role in maintenance of the epithelial cell phenotype and that expression is regulated during the epithelial-to-mesenchymal transition (EMT) and fibrosis (7,8).

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

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

Background: Salvador homolog (SAV1), originally named WW45, was first identified as a 45 kDa protein containing a pair of WW domains and a coiled-coil region (1). SAV1 was subsequently shown to function as a scaffold protein, in a protein complex that includes the kinases MST2 and LATS1, and the transcriptional co-activator YAP (2). This protein complex comprises the core components of the Hippo signaling pathway, which regulates important cellular functions, including contact inhibition and apoptosis, that function to regulate tissue growth and organ size (3,4). A genetic screen in Drosophila identified a role for SAV1 in cell cycle regulation and apoptosis (5), while embryonic mice lacking Sav1 displayed hyperplastic growth and epithelial differentiation effects (6). These findings, together with the observation that SAV1 is mutated a number of human cancer cell lines, suggest that SAV1 functions as a tumor suppressor in the Hippo signaling pathway (5, 7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Stem cell factor (SCF) is a growth factor that is essential for hematopoiesis, melanogenesis and fertility. SCF is also known as mast cell growth factor (MCGF), steel factor (SLF), or kit ligand (KL) (1-3). SCF mediates its biological effects by binding to and activating c-Kit (4). SCF induces dimerization of c-Kit followed by trans-autophosphorylation of the cytoplasmic protein tyrosine kinase domain, leading to subsequent recruitment of signaling proteins, tyrosine phosphorylation of substrates and activation of multiple signaling pathways (5,6). SCF/c-Kit may take part in the growth control of human malignancies (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Secreted Frizzled-related proteins (SFRPs) display homology and structural similarity to the extracellular cysteine-rich Wnt-binding domain of the G protein-coupled receptor Frizzled (1,2). To date, five distinct SFRPs (SFRP1 to 5) have been found in mammalian cells. These secreted proteins typically act as antagonists to Wnt signaling by directly binding and inhibiting Wnt proteins, or by binding Frizzled to block Wnt protein interaction with the receptor (3). The various SFRPs bind and regulate Wnt proteins differentially; these proteins also display distinct expression patterns as they play important roles in regulating development (4-7). SFRP proteins appear to act as tumor suppressors, with loss of expression or function correlating with many invasive forms of cancer. Deletion of the corresponding SFRP1 gene and promoter hypermethylation leading to gene silencing has been reported in a number of cancers. Abnormal expression of SRFP1 and other Wnt signaling proteins is associated with some cases of retinitis pigmentosa (reviewed in 8).

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

Application Methods: Western Blotting

Background: Hedgehog proteins (Hh) are secreted signaling proteins that play many roles during animal development. Aberrant Hh signaling activity can be associated with numerous birth defects and uncontrolled Hh pathway activation is linked to the development of several types of cancers (1-2). The three identified vertebrate Hh genes are Sonic (Shh), Indian (Ihh) and Desert (Dhh), all of which have distinct as well as overlapping roles (3-5). Hh proteins are synthesized as 45 kDa precursors that undergo auto-cleavage to generate a 19 kDa amino-terminal peptide (Hh-N) and a carboxy-terminal peptide (Hh-C). The amino-terminal peptide becomes covalently attached to a cholesterol molecule at its carboxy terminus and acetylated at its amino terminus. This doubly modified Hh-N peptide is released from cells and responsible for all known Hedgehog signaling activity (6).

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

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

Background: Sine oculis homeobox (SIX) proteins belong to a family of evolutionarily conserved transcription factors discovered in Drosophila mutant screens for embryonic eye development genes (1-3). The prototypical family member (sine oculis, so) was named for eyeless embryos carrying mutations in a gene highly conserved among vertebrates, including humans (SIX1) (4). A total of six family members (SIX1-6) have been identified in vertebrates. Each SIX protein contains a homeobox nucleic acid recognition domain (HD) with a DNA-binding helix-turn-helix motif and an adjacent SIX domain, which may be involved in regulating protein-protein interactions (5). In addition to their critical functions during embryonic organogenesis, research studies suggest that SIX proteins play additional roles in postnatal cell cycle regulation, with potentially important implications in tumorigenesis (6,7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Sine oculis homeobox (SIX) proteins belong to a family of evolutionarily conserved transcription factors discovered in Drosophila mutant screens for embryonic eye development genes (1-3). The prototypical family member (sine oculis, so) was named for eyeless embryos carrying mutations in a gene highly conserved among vertebrates, including humans (SIX1) (4). A total of six family members (SIX1-6) have been identified in vertebrates. Each SIX protein contains a homeobox nucleic acid recognition domain (HD) with a DNA-binding helix-turn-helix motif and an adjacent SIX domain, which may be involved in regulating protein-protein interactions (5). In addition to their critical functions during embryonic organogenesis, research studies suggest that SIX proteins play additional roles in postnatal cell cycle regulation, with potentially important implications in tumorigenesis (6,7).

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

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

Background: Slug (SNAI2) is a widely expressed transcriptional repressor and member of the Snail family of zinc finger transcription factors (1). Similar to the related Snail protein, Slug binds to the E-cadherin promoter region to repress transcription during development (2). The binding of Slug to integrin promoter sequences represses integrin expression and results in reduced cell adhesion (3). Down regulation of E-cadherin expression occurs during the epithelial-mesenchymal transition during embryonic development, a process also exploited by invasive cancer cells (4,5). The tumor suppressor protein p53 induces Slug expression in γ-irradiated cells; Slug protects damaged cells from apoptosis by repressing p53-induced transcription of the proapoptotic Bcl-2 family protein Puma (6). Deletion mutations in the corresponding Slug gene are associated with the pigmentation disorders Waardenburg Syndrome and Piebaldism, while a genetic duplication resulting in Slug overexpression is associated with a collection of congenital heart defects termed tetralogy of Fallot (7).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Smad1 (D59D7) XP® Rabbit mAb #6944.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Bone morphogenetic proteins (BMPs) constitute a large family of signaling molecules that regulate a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation, and apoptosis (1,2). BMP receptors are members of the TGF-β family of Ser/Thr kinase receptors. Ligand binding induces multimerization, autophosphorylation, and activation of these receptors (3-5). They subsequently phosphorylate Smad1 at Ser463 and Ser465 in the carboxy-terminal motif SSXS, as well as Smad5 and Smad9 (Smad8) at their corresponding sites. These phosphorylated Smads dimerize with the coactivating Smad4 and translocate to the nucleus, where they stimulate transcription of target genes (5).MAP kinases and CDKs 8 and 9 phosphorylate residues in the linker region of Smad1, including Ser206. The phosphorylation of Ser206 recruits Smurf1 to the linker region and leads to the degradation of Smad1 (6). Phosphorylation of this site also promotes Smad1 transcriptional action by recruiting YAP to the linker region (7).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Bone morphogenetic proteins (BMPs) constitute a large family of signaling molecules that regulate a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation, and apoptosis (1,2). BMP receptors are members of the TGF-β family of Ser/Thr kinase receptors. Ligand binding induces multimerization, autophosphorylation, and activation of these receptors (3-5). They subsequently phosphorylate Smad1 at Ser463 and Ser465 in the carboxy-terminal motif SSXS, as well as Smad5 and Smad9 (Smad8) at their corresponding sites. These phosphorylated Smads dimerize with the coactivating Smad4 and translocate to the nucleus, where they stimulate transcription of target genes (5).MAP kinases and CDKs 8 and 9 phosphorylate residues in the linker region of Smad1, including Ser206. The phosphorylation of Ser206 recruits Smurf1 to the linker region and leads to the degradation of Smad1 (6). Phosphorylation of this site also promotes Smad1 transcriptional action by recruiting YAP to the linker region (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the receptor-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, and 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved carboxy terminal SSXS motif. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Smad2 (D43B4) XP® Rabbit mAb #5339.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the receptor-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, and 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved carboxy terminal SSXS motif. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

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

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

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the receptor-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, and 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved carboxy terminal SSXS motif. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

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

Application Methods: Western Blotting

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the receptor-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, and 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved carboxy terminal SSXS motif. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Smad2/3 (D7G7) XP® Rabbit mAb #8685.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the receptor-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, and 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved carboxy terminal SSXS motif. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

$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 Smad2/3 (D7G7) XP® Rabbit mAb #8685.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the receptor-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, and 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved carboxy terminal SSXS motif. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

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

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

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the receptor-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, and 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved carboxy terminal SSXS motif. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

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

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

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the receptor-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, and 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved carboxy terminal SSXS motif. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

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

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

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmits TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the recepter-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Briefly, activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved SSXS motif at the carboxy-terminus of the proteins. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad, Smad4, and together the complex moves to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmits TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the recepter-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Briefly, activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved SSXS motif at the carboxy-terminus of the proteins. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad, Smad4, and together the complex moves to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Bone morphogenetic proteins (BMPs) constitute a large family of signaling molecules that regulate a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation, and apoptosis (1,2). BMP receptors are members of the TGF-β family of Ser/Thr kinase receptors. Ligand binding induces multimerization, autophosphorylation, and activation of these receptors (3-5). They subsequently phosphorylate Smad1 at Ser463 and Ser465 in the carboxy-terminal motif SSXS, as well as Smad5 and Smad9 (Smad8) at their corresponding sites. These phosphorylated Smads dimerize with the coactivating Smad4 and translocate to the nucleus, where they stimulate transcription of target genes (5).MAP kinases and CDKs 8 and 9 phosphorylate residues in the linker region of Smad1, including Ser206. The phosphorylation of Ser206 recruits Smurf1 to the linker region and leads to the degradation of Smad1 (6). Phosphorylation of this site also promotes Smad1 transcriptional action by recruiting YAP to the linker region (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Smad ubiquitin regulatory factor 2 (Smurf2) is a HECT domain E3 ubiquitin ligase. It was initially identified as an inhibitor of TGF-β/BMP signaling by targeting R-Smads and TGF type I receptor for ubiquitination and degradation (1-3). Subsequent studies have revealed its role in neuronal and planar cell polarity, as well as in the senescence response and suppression of tumorigenesis (4-8). Smurf2 has a broad range of substrates including RUNX2, AMSH, Rap1B, and RNF11 (5,9-11). Smurf2 is widely expressed in various tissues. The C2 domain of Smurf2 inhibits its catalytic activity by interacting with the HECT domain (12). Research studies have shown that Smurf2 functions as a tumor suppressor by maintaining genomic stability through targeting RNF20 (13).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Snail is a zinc-finger transcription factor that can repress E-cadherin transcription. Downregulation of E-cadherin is associated with epithelial-mesenchymal transition during embryonic development, a process also exploited by invasive cancer cells (1-3). Indeed, loss of E-cadherin expression is correlated with the invasive properties of some tumors and there is a considerable inverse correlation between Snail and E-cadherin mRNA levels in epithelial tumor cell lines (4,5). In addition, Snail blocks the cell cycle and confers resistance to cell death (6). Phosphorylation of Snail by GSK-3 and PAK1 regulates its stability, cellular localization and function (7-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Snail is a zinc-finger transcription factor that can repress E-cadherin transcription. Downregulation of E-cadherin is associated with epithelial-mesenchymal transition during embryonic development, a process also exploited by invasive cancer cells (1-3). Indeed, loss of E-cadherin expression is correlated with the invasive properties of some tumors and there is a considerable inverse correlation between Snail and E-cadherin mRNA levels in epithelial tumor cell lines (4,5). In addition, Snail blocks the cell cycle and confers resistance to cell death (6). Phosphorylation of Snail by GSK-3 and PAK1 regulates its stability, cellular localization and function (7-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Snail is a zinc-finger transcription factor that can repress E-cadherin transcription. Downregulation of E-cadherin is associated with epithelial-mesenchymal transition during embryonic development, a process also exploited by invasive cancer cells (1-3). Indeed, loss of E-cadherin expression is correlated with the invasive properties of some tumors and there is a considerable inverse correlation between Snail and E-cadherin mRNA levels in epithelial tumor cell lines (4,5). In addition, Snail blocks the cell cycle and confers resistance to cell death (6). Phosphorylation of Snail by GSK-3 and PAK1 regulates its stability, cellular localization and function (7-10).