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Monoclonal Antibody Western Blotting Genitalia Development

$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: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated β-Catenin (D10A8) XP® Rabbit mAb #8480.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

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

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

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$141
20 µl
$348
100 µl
APPLICATIONS
REACTIVITY
Dog, Human, Monkey, Mouse, Rat, Zebrafish

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

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$134
20 µl
$336
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CHD7 belongs to the chromodomain helicase DNA-binding (CHD) family of ATP-dependent chromatin remodeling proteins (1). The CHD family of proteins has been shown to play an important role in regulating gene expression by altering the chromatin structure at target genes (1,2). The nine members of the CHD family are characterized by the presence of two tandem chromodomains in the N-terminal region and an SNF2-like ATPase domain near the central region of the protein (2-4). The CHD proteins can be further divided into three subgroups based on the presence of additional conserved functional domains. CHD7 belongs to the third subgroup of CHD proteins together with CHD6, 8, and 9, which are distinguished by the presence of three conserved region (CR) domains, a switching-defective protein 3, adaptor 2, nuclear receptor co-repressor, transcription factor IIB (SANT) like domain, two brahma and kismet (BRK) domains, and a DNA binding domain (2). CHD7 regulates embryonic stem cell (ESC) specific gene expression together with ESC master regulators Oct-4, Sox2 and nanog, and is necessary for neural stem cell development and formation of the neural crest (5-7). Research studies have shown that CHD7 mutations are frequently found in patients with CHARGE syndrome (coloboma of the eye, heart defects, atresia of the choanae, retardation of growth/development, genital/urinary abnormalities, and ear abnormalities and deafness) (8).

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

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

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (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 β-Catenin (D10A8) XP® Rabbit mAb #8480.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Wilms' Tumor 1 (WT1) is a transcription factor named from Wilms' Tumor 1, an embryonal malignancy of the kidneys that is caused by mutations in the WT1 gene (1). It is highly important in development, particularly of the genitourinary system, and mutations and dysregulation of expression of WT1 result in a variety of syndromes affecting the genitourinal system and other tissues (2-5).WT1 has a myriad of biological functions and a host of interacting partners and target genes (6). It can behave as a transcriptional activator, or a repressor, and can act as an oncogene or a tumor suppressor (7). It exerts influence over the epigenetic landscape, and also has post translational influence of gene expression through RNA interactions (8). The diverse biological roles of WT1 have been attributed to the existence of multiple isoforms and post translation modifications of the protein (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Wilms' Tumor 1 (WT1) is a transcription factor named from Wilms' Tumor 1, an embryonal malignancy of the kidneys that is caused by mutations in the WT1 gene (1). It is highly important in development, particularly of the genitourinary system, and mutations and dysregulation of expression of WT1 result in a variety of syndromes affecting the genitourinal system and other tissues (2-5).WT1 has a myriad of biological functions and a host of interacting partners and target genes (6). It can behave as a transcriptional activator, or a repressor, and can act as an oncogene or a tumor suppressor (7). It exerts influence over the epigenetic landscape, and also has post translational influence of gene expression through RNA interactions (8). The diverse biological roles of WT1 have been attributed to the existence of multiple isoforms and post translation modifications of the protein (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: DHCR24/Seladin-1 was identified as a molecular basis for desmosterolosis (1). It encodes for 24-dehydrocholesterol reductase (3β-hydroxysterol Δ-24-reductase). This enzyme reduces desmosterol in cholesterol biosynthesis (1). Recessive mutations in this gene in desmosterolosis patients lead to a defective enzyme resulting in increased levels of desmosterol (1). DHCR24/Seladin-1 is induced upon oxidative stress and was found to mediate Ras-induced senescence resulting from increased reactive oxygen species (2). Studies further indicate that the level of DHCR24/Seladin-1 is induced in the acute response and reduced in the chronic response to oxidative stress in a cholesterol dependent manner (3). Moreover, overexpression of DHCR24/Seladin-1 bearing two mutations that abolish its reductase acitivity causes the cells to lose protection from oxidative stress (3). These findings thus link the reductase activity of DHCR24/Seladin-1 to its protective role in oxidative stress. This enzyme has also been demonstrated to be a hydrogen peroxide scavenger (4).

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

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

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

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

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Bone morphogenetic proteins (BMPs) were first identified as molecules that can induce ectopic bone and cartilage formation (1,2). BMPs belong to the TGF-β superfamily, playing many diverse functions during development (3). BMPs are synthesized as precursor proteins and then processed by cleavage to release the C-terminal mature BMP. BMPs initiate signaling by binding to a receptor complex containing type I and type II serine/threonine receptor kinases that then phosphorylate Smad (mainly Smad1, 5, and 8), resulting in the translocation of Smad into the nucleus. BMP was also reported to activate MAPK pathways in some systems (3,4).

$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).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Wnt family includes several secreted glycoproteins that play important roles in animal development (1). There are 19 Wnt genes in the human genome that encode functionally distinct Wnt proteins (2). Wnt members bind to the Frizzled family of seven-pass transmembrane proteins and activate several signaling pathways (3). The canonical Wnt/β-catenin pathway also requires a coreceptor from the low-density lipoprotein receptor family (4). Aberrant activation of Wnt signaling pathways is involved in several types of cancers (5).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis (1). In addition to p53, mammalian cells contain two p53 family members, p63 and p73, which are similar to p53 in both structure and function (2). While p63 can induce p53-responsive genes and apoptosis, mutation of p63 rarely results in tumors (2). Research investigators frequently observe amplification of the p63 gene in squamous cell carcinomas of the lung, head and neck (2,3). The p63 gene contains an alternative transcription initiation site that yields a truncated ΔNp63 lacking the transactivation domain, and alternative splicing at the carboxy-terminus yields the α, β, and γ isoforms (3,4).