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Product listing: NaPi2b/SLC34A2 (D6W2G) Rabbit mAb, UniProt ID O95436 #42299 to NEDD4 (D82F4) Rabbit mAb, UniProt ID P46934 #5344

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The sodium-dependent phosphate transport protein 2B (NaPi-2b, SLC34A2) is a sodium dependent inorganic phosphate (Pi) transporter that regulates phosphate homeostasis in various organs, including the small intestine, lung, liver, and testis (1). In the small intestine, NaPi-2b localizes to the intestinal brush border membrane to mediate Pi reabsorption (2). In the lung, NaPi-2b is expressed in the apical membrane of type II alveolar cells and is involved in the synthesis of surfactant (3). Mutations in the corresponding SLC34A2 gene causes pulmonary alveolar microlithiasis, a rare autosomal recessive disorder characterized by the deposition of calcium phosphate microliths throughout the lungs (4). Research studies show aberrant expression of NaPi-2b in various type of cancer, including ovarian, breast, and lung cancer (5). Chromosomal rearrangements involving SLC34A2-ROS1 are seen in gastric carcinoma and non-small cell lung cancer and result in the formation of a SLC34A2-ROS1 chimeric protein that retains a constitutive kinase activity (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Napsin A is an aspartic proteinase that is expressed in normal lung and kidney (1). In the lung, napsin A is expressed by type II pneumocytes and alveolar macrophages, where it plays a role in processing surfactant protein B (2). Napsin A is expressed in lung adenocarcinomas, where it can be used to identify primary and metastatic lesions with greater sensitivity compared to TTF-1 (3,4). Napsin A expression has also been described in other types of cancer, such as kidney and thyroid cancer (5).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Napsin A is an aspartic proteinase that is expressed in normal lung and kidney (1). In the lung, napsin A is expressed by type II pneumocytes and alveolar macrophages, where it plays a role in processing surfactant protein B (2). Napsin A is expressed in lung adenocarcinomas, where it can be used to identify primary and metastatic lesions with greater sensitivity compared to TTF-1 (3,4). Napsin A expression has also been described in other types of cancer, such as kidney and thyroid cancer (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Voltage gated sodium channels are composed of a large alpha subunit and auxiliary beta subunits. The alpha subunit has 4 homologous domains, with each domain containing 6 transmembrane segments. These segments function as the voltage sensor and sodium permeable pore. Upon change of membrane potential, the sodium channel is activated, which allows sodium ions to flow through (1,2). When associated with beta subunits or other accessory proteins, the alpha subunit is regulated at the level of cell surface expression, kinetics, and voltage dependence (3,4).There are 9 mammalian alpha subunits, named Nav1.1-Nav1.9 (5). These alpha subunits differ in tissue specificity and biophysical functions (6,7). Seven of these subunits are essential for the initiation and propagation of action potentials in the central and peripheral nervous system while Nav1.4 and Nav1.5 are mainly expressed in skeletal muscle and cardiac muscle (8,9). Mutations in these alpha channel subunits have been identified in patients with epilepsy, seizure, ataxia, sensitivity to pain, and cardiomyopathy (reviewed in 10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Voltage gated sodium channels are composed of a large alpha subunit and auxiliary beta subunits. The alpha subunit has 4 homologous domains, with each domain containing 6 transmembrane segments. These segments function as the voltage sensor and sodium permeable pore. Upon change of membrane potential, the sodium channel is activated, which allows sodium ions to flow through (1,2). When associated with beta subunits or other accessory proteins, the alpha subunit is regulated at the level of cell surface expression, kinetics, and voltage dependence (3,4).There are 9 mammalian alpha subunits, named Nav1.1-Nav1.9 (5). These alpha subunits differ in tissue specificity and biophysical functions (6,7). Seven of these subunits are essential for the initiation and propagation of action potentials in the central and peripheral nervous system while Nav1.4 and Nav1.5 are mainly expressed in skeletal muscle and cardiac muscle (8,9). Mutations in these alpha channel subunits have been identified in patients with epilepsy, seizure, ataxia, sensitivity to pain, and cardiomyopathy (reviewed in 10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Voltage gated sodium channels are composed of a large alpha subunit and auxiliary beta subunits. The alpha subunit has 4 homologous domains, with each domain containing 6 transmembrane segments. These segments function as the voltage sensor and sodium permeable pore. Upon change of membrane potential, the sodium channel is activated, which allows sodium ions to flow through (1,2). When associated with beta subunits or other accessory proteins, the alpha subunit is regulated at the level of cell surface expression, kinetics, and voltage dependence (3,4).There are 9 mammalian alpha subunits, named Nav1.1-Nav1.9 (5). These alpha subunits differ in tissue specificity and biophysical functions (6,7). Seven of these subunits are essential for the initiation and propagation of action potentials in the central and peripheral nervous system while Nav1.4 and Nav1.5 are mainly expressed in skeletal muscle and cardiac muscle (8,9). Mutations in these alpha channel subunits have been identified in patients with epilepsy, seizure, ataxia, sensitivity to pain, and cardiomyopathy (reviewed in 10).

$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 NBR1 (D2E6) Rabbit mAb #9891.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: Next to BRCA1 gene 1 (NBR1) protein is known for its encoding gene proximity to the BRCA1 tumor suppressor gene (1,2). N-terminal Phox and Bem1p (PB1) domains of NBR1 mediate its interaction with muscle specific titin kinase (3,4) and scaffolding protein p62 (4). NBR1 plays a role in autophagy by facilitating the autophagosomal degradation of ubiquitinated proteins independently and also in concert with p62 (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Next to BRCA1 gene 1 (NBR1) protein is known for its encoding gene proximity to the BRCA1 tumor suppressor gene (1,2). N-terminal Phox and Bem1p (PB1) domains of NBR1 mediate its interaction with muscle specific titin kinase (3,4) and scaffolding protein p62 (4). NBR1 plays a role in autophagy by facilitating the autophagosomal degradation of ubiquitinated proteins independently and also in concert with p62 (5,6).

$260
200 µl
APPLICATIONS
REACTIVITY
Human

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

Background: NCAM (neural cell adhesion molecule, CD56) is an adhesion glycoprotein with five extracellular immunoglobulin-like domains followed by two fibronectin type III repeats. Structural diversity is introduced by alternative splicing resulting in different cytoplasmic domains (1). NCAM mediates neuronal attachment, neurite extension and cell-cell interactions through homo and heterophilic interactions. PSA (polysialic acid) post-translationally modifies NCAM and increases the metastatic potential of small cell lung carcinoma, Wilms+ tumor, neuroblastoma and rhabdomyosarcoma (2). CD56 and CD16 are commonly used to identify NK cells although some cells with the T cell markers CD3 and CD4 also express CD56 (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Neural cell adhesion molecule L1 (NCAM-L1/L1CAM) is a single pass transmembrane glycoprotein member of the immunoglobulin superfamily, containing six amino-terminal extracellular Ig-like domains followed by five fibronectin type-III domains (1). NCAM-L1 is mainly expressed in the brain, and plays an important role in the developing nervous system, with involvement in neurite fasciculation and outgrowth, myelination, neuronal migration, and neuronal cell adhesion (2). Mutations in the NCAM-L1 gene cause varying degrees of neurological disease including X-linked hydrocephalus, MASA syndrome, spastic paraplegia type 1, and X-linked corpus callosum agenesis, together known as L1 syndrome (3). Apart from the nervous system, NCAM-L1 is overexpressed in many cancers and supports a poor prognosis by facilitating aggressive tumor growth, metastasis and chemoresistance (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Neural cell adhesion molecule L1 (NCAM-L1/L1CAM) is a single pass transmembrane glycoprotein member of the immunoglobulin superfamily, containing six amino-terminal extracellular Ig-like domains followed by five fibronectin type-III domains (1). NCAM-L1 is mainly expressed in the brain, and plays an important role in the developing nervous system, with involvement in neurite fasciculation and outgrowth, myelination, neuronal migration, and neuronal cell adhesion (2). Mutations in the NCAM-L1 gene cause varying degrees of neurological disease including X-linked hydrocephalus, MASA syndrome, spastic paraplegia type 1, and X-linked corpus callosum agenesis, together known as L1 syndrome (3). Apart from the nervous system, NCAM-L1 is overexpressed in many cancers and supports a poor prognosis by facilitating aggressive tumor growth, metastasis and chemoresistance (4,5).

$259
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to APC and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: NCAM (neural cell adhesion molecule, CD56) is an adhesion glycoprotein with five extracellular immunoglobulin-like domains followed by two fibronectin type III repeats. Structural diversity is introduced by alternative splicing resulting in different cytoplasmic domains (1). NCAM mediates neuronal attachment, neurite extension and cell-cell interactions through homo and heterophilic interactions. PSA (polysialic acid) post-translationally modifies NCAM and increases the metastatic potential of small cell lung carcinoma, Wilms+ tumor, neuroblastoma and rhabdomyosarcoma (2). CD56 and CD16 are commonly used to identify NK cells although some cells with the T cell markers CD3 and CD4 also express CD56 (3).

$229
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to FITC and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: NCAM (neural cell adhesion molecule, CD56) is an adhesion glycoprotein with five extracellular immunoglobulin-like domains followed by two fibronectin type III repeats. Structural diversity is introduced by alternative splicing resulting in different cytoplasmic domains (1). NCAM mediates neuronal attachment, neurite extension and cell-cell interactions through homo and heterophilic interactions. PSA (polysialic acid) post-translationally modifies NCAM and increases the metastatic potential of small cell lung carcinoma, Wilms+ tumor, neuroblastoma and rhabdomyosarcoma (2). CD56 and CD16 are commonly used to identify NK cells although some cells with the T cell markers CD3 and CD4 also express CD56 (3).

$229
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to PE and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: NCAM (neural cell adhesion molecule, CD56) is an adhesion glycoprotein with five extracellular immunoglobulin-like domains followed by two fibronectin type III repeats. Structural diversity is introduced by alternative splicing resulting in different cytoplasmic domains (1). NCAM mediates neuronal attachment, neurite extension and cell-cell interactions through homo and heterophilic interactions. PSA (polysialic acid) post-translationally modifies NCAM and increases the metastatic potential of small cell lung carcinoma, Wilms+ tumor, neuroblastoma and rhabdomyosarcoma (2). CD56 and CD16 are commonly used to identify NK cells although some cells with the T cell markers CD3 and CD4 also express CD56 (3).

$299
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to PE-Cy7® and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: NCAM (neural cell adhesion molecule, CD56) is an adhesion glycoprotein with five extracellular immunoglobulin-like domains followed by two fibronectin type III repeats. Structural diversity is introduced by alternative splicing resulting in different cytoplasmic domains (1). NCAM mediates neuronal attachment, neurite extension and cell-cell interactions through homo and heterophilic interactions. PSA (polysialic acid) post-translationally modifies NCAM and increases the metastatic potential of small cell lung carcinoma, Wilms+ tumor, neuroblastoma and rhabdomyosarcoma (2). CD56 and CD16 are commonly used to identify NK cells although some cells with the T cell markers CD3 and CD4 also express CD56 (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The structural maintenance of chromosomes 2 (SMC2) and 4 (SMC4) proteins are condensin complex subunits that enable chromosome condensation and compaction during migration to opposite poles during anaphase (1,2). Condensin is a general regulator of chromosome architecture that may also regulate gene expression and DNA repair. Condensin complex subunits SMC2 and SMC4 form a functional ATPase essential for chromatin condensation, while three auxiliary subunits regulate ATPase activity. Both SMC2 and SMC4 are found within two distinct condensin complexes (condensin I and II) in higher eukaryotes. Condensin I contains auxiliary subunits NCAPD2, NCAPG, and NCAPH, while condensin II contains related auxiliary proteins NCAPD3, NCAPG2, and NCAPH2 (1,2).Each condensin complex exhibits different localization patterns during the cell cycle and provides for distinct functions during mitosis (3-5). Condensin I is cytoplasmic during interphase and binds chromatin following the breakdown of the nuclear envelope at the end of prophase. Condensin I is required for complete dissociation of cohesin from chromosome arms, for chromosome shortening, and for normal timing of progression through pro-metaphase and metaphase. Mutations in corresponding condensin I genes result in cytokinesis defects due to the persistence of anaphase fibers. Condensin II is nuclear during interphase, but does not bind to chromatin until early prophase where it remains bound until the end of telophase. Condensin II is required for initial chromatin condensation during early prophase. Mutations in corresponding condensin II genes produce high numbers of anaphase bridges resulting from incomplete chromosome segregation. Condensin II complex subunit D3 (NCAPD3) plays a pivotal role in the loading of condensin II onto chromatin and the regulation of chromatin condensation (6,7). NCAPD3 protein contains HEAT repeat clusters that bind to mono-methyl histone H4 Lys20, a histone mark prevalent during mitosis and important for DNA repair and chromatin condensation (6). Increased mono-methyl histone H4 Lys20 levels caused by dissociation of the histone demethylase PHF8 from chromatin and increased expression of the methyltransferase SET8, leads to increased binding of NCAPD3 and condensin II to chromosomes early in mitosis (6). Phosphorylation of NCAPD3 at Thr1415 by CDK1 kinase (cdc2) leads to the recruitment of PLK1 kinase, which hyperphosphorylates condensin II and facilitates mitotic chromosome assembly (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Nuclear cap-binding protein subunit 1 (NCBP1), also known as cap-binding protein 80 (CBP80), plays a role in nuclear pre-mRNA splicing (1,2). It has also been shown to function in the nonsense-mediated decay (NMD) of mRNAs where translation is prematurely terminated (3). NCBP1/CBP80 increases the efficiency of NMD by promoting the interaction of two active NMD components Upf1 and Upf2 (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: NCK1 (also known as NCK or NCKα) is a broadly expressed oncogenic adapter protein consisting of three SH3 domains and one SH2 domain (1-3). NCK1 becomes phosphorylated upon activation of variety of cell surface receptors and is involved in actin cytoskeletal organization induced by many stimuli (4-6). NCK2 (also known as NCKβ), a homolog of NCK1, has an overlapping expression pattern and redundant functions with NCK1 (7).

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

Application Methods: Western Blotting

Background: NCK1 (also known as NCK or NCKα) is a broadly expressed oncogenic adapter protein consisting of three SH3 domains and one SH2 domain (1-3). NCK1 becomes phosphorylated upon activation of variety of cell surface receptors and is involved in actin cytoskeletal organization induced by many stimuli (4-6). NCK2 (also known as NCKβ), a homolog of NCK1, has an overlapping expression pattern and redundant functions with NCK1 (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The most well characterized nuclear receptor corepressors are SMRT (silencing mediator for retinoic acid and thyroid hormone receptors) and its close paralog NCoR1 (nuclear receptor corepressor) (1,2). NCoR1 functions to transcriptionally silence various unliganded, DNA bound non-steroidal nuclear receptors by serving as a large molecular scaffold that bridges the receptors with multiple chromatin remodeling factors that repress nuclear receptor-mediated gene transcription, in part, through deacetylation of core histones surrounding target promoters. Indeed, the N-terminal portion of NCoR1 possesses multiple distinct transcriptional repression domains (RDs) reponsible for the recruitment of additional components of the corepressor complex such as HDACs, mSin3, GPS2, and TBL1/TBLR1. In between the RDs lies a pair of potent repressor motifs known as SANT motifs (SWI3, ADA2, N-CoR, and TFIIIB), which recruit HDAC3 and histones to the repressor complex in order to enhance HDAC3 activity (3). The C-terminal portion of NCoR1 contains multiple nuclear receptor interaction domains (NDs), each of which contains a conserved CoRNR box (or L/I-X-X-I/V-I) motif that allow for binding to various unliganded nuclear hormone receptors such as thyroid hormone (THR) and retinoic acid (RAR) receptors (4,5).Recent genetic studies in mice have not only corroborated the wealth of biochemical studies involving NCoR1 but have also provided significant insight regarding the function of NCoR1 in mammalian development and physiology. Although it has been observed that loss of Ncor1 does not affect early embyonic development, likely due to compensation by Smrt, embryonic lethality ultimately results during mid-gestation, largely due to defects in erythropoesis and thymopoesis (6). Another study demonstrated that the NDs of NCoR1 are critical for its ability to function in a physiological setting as a transcriptional repressor of hepatic THR and Liver X Receptor (LXR) (7).

$293
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

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

Background: According to affinity and function, calcium-binding proteins are separated into two classes: calcium buffers and calcium sensors. Calmodulin is a well-studied calcium sensor with well-established roles in synaptic plasticity. Neuronal calcium-sensor 1 (NCS1) is also a member of the calcium sensor family, however, its role in synaptic plasticity remains under investigation. NCS1 contains multiple EF-hand calcium-binding motifs and an amino-terminal myristoyl group (1). NCS1 has a large number of binding partners. Most of these protein interactions are calcium-dependent (e.g. dopamine D2 receptor), although some are calcium-independent (e.g. IP3 receptor) (2). In murine dentate gyrus, NCS1 promotes synaptic plasticity and rapid acquisition of spatial memory (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: NCX1 (Na+/Ca2+ exchanger, isoform 1) belongs to a conserved family of sodium-calcium membrane antiporter proteins that play a fundamental role in regulating intracellular calcium levels (1). NCX1 facilitates transmembrane transport of Ca2+ ions in exchange for Na+ ions in response to electrochemical gradients (2). Due to its relatively low affinity for calcium, NCX1 most commonly functions to export Ca2+ under acute conditions of high intracellular Ca2+. Notably however, NCX1 is a reversible antiporter, and can thus facilate Ca2+ influx under specialized physiological circumstances (3). Research studies have shown that NCX1 is particularly important for regulating intracellular Ca2+ levels in excitatory cell types (e.g., neurons, cardiac muscle). For example, conditional knockout of NCX1 in mouse cardiac pacemaker cells identified a critical role for NCX1 in the initiation and maintenance of cardiac rhythm (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: NDP52 (CALCOCO2) is ubiquitously expressed and composed of an amino-terminal SKICH domain, followed by a coiled-coil domain, and two zinc finger domains (1). It has recently been reported to act as an autophagy receptor that binds cytosolic ubiquitinated bacteria, leading to autophagy activation and pathogen clearance (1-3). NDP52 binds ubiquitin through its zinc finger domain and simultaneously binds LC3, which directs the bacteria into autophagosomes. In addition, NDP52 interacts with Nap1 and SINTBAD to recruit TBK1 to ubiquitinated bacteria (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: N-myc downstream-regulated gene 1 (NDRG1), also termed Cap43, Drg1, RTP/rit42, and Proxy-1, is a member of the NDRG family, which is composed of four members (NDRG1-4) that function in growth, differentiation, and cell survival (1-5). NDRG1 is ubiquitously expressed and highly responsive to a variety of stress signals including DNA damage (4), hypoxia (5), and elevated levels of nickel and calcium (2). Expression of NDRG1 is elevated in N-myc defective mice and is negatively regulated by N- and c-myc (1,6). During DNA damage, NDRG1 is induced in a p53-dependent fashion and is necessary for p53-mediated apoptosis (4,7). Research studies have shown that NDRG1 may also play a role in cancer progression by promoting differentiation, inhibiting growth, and modulating metastasis and angiogenesis (3,4,6,8,9). Nonsense mutation of the NDRG1 gene has been shown to cause hereditary motor and sensory neuropathy-Lom (HMSNL), which is supported by studies demonstrating the role of NDRG1 in maintaining myelin sheaths and axonal survival (10,11). NDRG1 is up-regulated during mast cell maturation and its deletion leads to attenuated allergic responses (12). Both NDRG1 and NDRG2 are substrates of SGK1, although the precise physiological role of SGK1-mediated phosphorylation is not known (13). NDRG1 is phosphorylated by SGK1 at Thr328, Ser330, Thr346, Thr356, and Thr366. Phosphorylation by SGK1 primes NDRG1 for phosphorylation by GSK-3.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: N-myc downstream-regulated gene 1 (NDRG1), also termed Cap43, Drg1, RTP/rit42, and Proxy-1, is a member of the NDRG family, which is composed of four members (NDRG1-4) that function in growth, differentiation, and cell survival (1-5). NDRG1 is ubiquitously expressed and highly responsive to a variety of stress signals including DNA damage (4), hypoxia (5), and elevated levels of nickel and calcium (2). Expression of NDRG1 is elevated in N-myc defective mice and is negatively regulated by N- and c-myc (1,6). During DNA damage, NDRG1 is induced in a p53-dependent fashion and is necessary for p53-mediated apoptosis (4,7). Research studies have shown that NDRG1 may also play a role in cancer progression by promoting differentiation, inhibiting growth, and modulating metastasis and angiogenesis (3,4,6,8,9). Nonsense mutation of the NDRG1 gene has been shown to cause hereditary motor and sensory neuropathy-Lom (HMSNL), which is supported by studies demonstrating the role of NDRG1 in maintaining myelin sheaths and axonal survival (10,11). NDRG1 is up-regulated during mast cell maturation and its deletion leads to attenuated allergic responses (12). Both NDRG1 and NDRG2 are substrates of SGK1, although the precise physiological role of SGK1-mediated phosphorylation is not known (13). NDRG1 is phosphorylated by SGK1 at Thr328, Ser330, Thr346, Thr356, and Thr366. Phosphorylation by SGK1 primes NDRG1 for phosphorylation by GSK-3.

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

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

Background: N-myc downstream-regulated gene 1 (NDRG1), also termed Cap43, Drg1, RTP/rit42, and Proxy-1, is a member of the NDRG family, which is composed of four members (NDRG1-4) that function in growth, differentiation, and cell survival (1-5). NDRG1 is ubiquitously expressed and highly responsive to a variety of stress signals including DNA damage (4), hypoxia (5), and elevated levels of nickel and calcium (2). Expression of NDRG1 is elevated in N-myc defective mice and is negatively regulated by N- and c-myc (1,6). During DNA damage, NDRG1 is induced in a p53-dependent fashion and is necessary for p53-mediated apoptosis (4,7). Research studies have shown that NDRG1 may also play a role in cancer progression by promoting differentiation, inhibiting growth, and modulating metastasis and angiogenesis (3,4,6,8,9). Nonsense mutation of the NDRG1 gene has been shown to cause hereditary motor and sensory neuropathy-Lom (HMSNL), which is supported by studies demonstrating the role of NDRG1 in maintaining myelin sheaths and axonal survival (10,11). NDRG1 is up-regulated during mast cell maturation and its deletion leads to attenuated allergic responses (12). Both NDRG1 and NDRG2 are substrates of SGK1, although the precise physiological role of SGK1-mediated phosphorylation is not known (13). NDRG1 is phosphorylated by SGK1 at Thr328, Ser330, Thr346, Thr356, and Thr366. Phosphorylation by SGK1 primes NDRG1 for phosphorylation by GSK-3.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The NDRG (N-Myc downstream-regulated gene) family consisting of NDRG1, NDRG2, NDRG3, and NDRG4 are structurally related proteins with roles in cell proliferation, differentiation, apoptosis, stress responses, and cell migration/metastasis (1-3). NDRG1 was originally identified as a protein that was upregulated in N-Myc knockout mice (1). Proteins in the NDRG family, particularly NDRG1 and NDRG2, have been reported to be down-regulated in various cancer tissues and have been suggested to function as a tumor suppressors (4,5).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Nectin-2, also known as CD112 and poliovirus receptor-related 2 (PVRL2), is a single-pass type I membrane glycoprotein ubiquitously expressed on various human tissues (1). It is a calcium independent cell adhesion molecule known to interact with several cell surface receptors, including DNAM-1 (CD226), LFA-1 (CD11a), Nectin-3 (CD113), TIGIT (VSTM3), and PVRIG (CD112R) (2-7). It is one of the major constituents of adherins junctions, and therefore plays a central role in a number of cellular processes, including adhesion, migration, and proliferation (2-8). Within the immune system, Nectin-2 modulates immune cell signaling. Upon interaction with DNAM-1 expressed on T and NK cells, Nectin-2 stimulates proliferation and cytokine production (4). Upon interaction with PVRIG, Nectin-2 inhibits proliferation (7). Thus, Nectin-2 can be either a co-stimulator or a co-inhibitor of immune cell function depending on competitive receptor interactions. Nectin-2 also serves as an entry for certain mutant strains of herpes simplex virus and pseudorabies virus, and it is involved in cell to cell spreading of these viruses (8,9). Alternate transcriptional splice variants, encoding different isoforms, have been characterized (10,11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Neural precursor expressed, developmentally down-regulated protein 4 (NEDD4) was originally identified as a gene that is highly expressed in the early mouse embryonic central nervous system (1). Subsequently, a family of NEDD4-like proteins have been defined that includes seven members in humans (2). NEDD4 and NEDD4-like (NEDD4L) proteins contain multiple functional domains including a calcium-dependent phospholipid and membrane binding domain (C2 domain), two to four protein binding domains (WW domains), and an E3 ubiquitin-protein ligase domain (HECT domain). NEDD4 and NEDD4L have been shown to downregulate both neuronal voltage-gated Na+ channels (NaVs) and epithelial Na+ channels (ENaCs) in response to increased intracellular Na+ concentrations (3,4). The WW domains of NEDD4 bind to PY motifs (amino acid sequence PPXY) found in multiple NaV and ENaC proteins; ubiquitination of these proteins is mediated by the HECT domain of NEDD4 and results in their internalization and removal from the plasma membrane. Research studies have shown that mutation of the PY motifs in ENaC proteins is associated with Liddle's syndrome, an autosomal dominant form of hypertension (5). In addition to targeting sodium channels, NEDD4L has also been shown to negatively regulate TGF-β signaling by targeting Smad2 for degradation (6). Mouse and human NEDD4 are rapidly cleaved by caspase proteins during apoptosis, although the significance of this cleavage is not clear (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Neural precursor expressed, developmentally down-regulated protein 4 (NEDD4) was originally identified as a gene that is highly expressed in the early mouse embryonic central nervous system (1). Subsequently, a family of NEDD4-like proteins have been defined that includes seven members in humans (2). NEDD4 and NEDD4-like (NEDD4L) proteins contain multiple functional domains including a calcium-dependent phospholipid and membrane binding domain (C2 domain), two to four protein binding domains (WW domains), and an E3 ubiquitin-protein ligase domain (HECT domain). NEDD4 and NEDD4L have been shown to downregulate both neuronal voltage-gated Na+ channels (NaVs) and epithelial Na+ channels (ENaCs) in response to increased intracellular Na+ concentrations (3,4). The WW domains of NEDD4 bind to PY motifs (amino acid sequence PPXY) found in multiple NaV and ENaC proteins; ubiquitination of these proteins is mediated by the HECT domain of NEDD4 and results in their internalization and removal from the plasma membrane. Research studies have shown that mutation of the PY motifs in ENaC proteins is associated with Liddle's syndrome, an autosomal dominant form of hypertension (5). In addition to targeting sodium channels, NEDD4L has also been shown to negatively regulate TGF-β signaling by targeting Smad2 for degradation (6). Mouse and human NEDD4 are rapidly cleaved by caspase proteins during apoptosis, although the significance of this cleavage is not clear (7).