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Product listing: LRP5 (D5G4) Rabbit mAb, UniProt ID O75197 #5440 to MacroH2A1.1 (D5F6N) Rabbit mAb, UniProt ID O75367 #12455

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

Application Methods: Western Blotting

Background: LRP5 and LRP6 are single-pass transmembrane proteins belonging to the low-density lipoprotein receptor (LDLR)-related protein family. Unlike other members of the LDLR family, LRP5 and LRP6 have four EGF and three LDLR repeats in the extracellular domain, and proline-rich motifs in the cytoplasmic domain (1). They function as co-receptors for Wnt and are required for the canonical Wnt/β-catenin signaling pathway (2,3). LRP5 and LRP6 are highly homologous and have redundant roles during development (4,5). The activity of LRP5 and LRP6 can be inhibited by the binding of some members of the Dickkopf (DKK) family of proteins (6,7). Upon stimulation with Wnt, LRP6 is phosphorylated at multiple sites including Thr1479, Ser1490, and Thr1493 by kinases such as GSK-3 and CK1 (8-10). Phosphorylated LRP6 recruits axin to the membrane and presumably activates β-catenin signaling (8-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: LRP5 and LRP6 are single-pass transmembrane proteins belonging to the low-density lipoprotein receptor (LDLR)-related protein family. Unlike other members of the LDLR family, LRP5 and LRP6 have four EGF and three LDLR repeats in the extracellular domain, and proline-rich motifs in the cytoplasmic domain (1). They function as co-receptors for Wnt and are required for the canonical Wnt/β-catenin signaling pathway (2,3). LRP5 and LRP6 are highly homologous and have redundant roles during development (4,5). The activity of LRP5 and LRP6 can be inhibited by the binding of some members of the Dickkopf (DKK) family of proteins (6,7). Upon stimulation with Wnt, LRP6 is phosphorylated at multiple sites including Thr1479, Ser1490, and Thr1493 by kinases such as GSK-3 and CK1 (8-10). Phosphorylated LRP6 recruits axin to the membrane and presumably activates β-catenin signaling (8-10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: LRP5 and LRP6 are single-pass transmembrane proteins belonging to the low-density lipoprotein receptor (LDLR)-related protein family. Unlike other members of the LDLR family, LRP5 and LRP6 have four EGF and three LDLR repeats in the extracellular domain, and proline-rich motifs in the cytoplasmic domain (1). They function as co-receptors for Wnt and are required for the canonical Wnt/β-catenin signaling pathway (2,3). LRP5 and LRP6 are highly homologous and have redundant roles during development (4,5). The activity of LRP5 and LRP6 can be inhibited by the binding of some members of the Dickkopf (DKK) family of proteins (6,7). Upon stimulation with Wnt, LRP6 is phosphorylated at multiple sites including Thr1479, Ser1490, and Thr1493 by kinases such as GSK-3 and CK1 (8-10). Phosphorylated LRP6 recruits axin to the membrane and presumably activates β-catenin signaling (8-10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: LRP5 and LRP6 are single-pass transmembrane proteins belonging to the low-density lipoprotein receptor (LDLR)-related protein family. Unlike other members of the LDLR family, LRP5 and LRP6 have four EGF and three LDLR repeats in the extracellular domain, and proline-rich motifs in the cytoplasmic domain (1). They function as co-receptors for Wnt and are required for the canonical Wnt/β-catenin signaling pathway (2,3). LRP5 and LRP6 are highly homologous and have redundant roles during development (4,5). The activity of LRP5 and LRP6 can be inhibited by the binding of some members of the Dickkopf (DKK) family of proteins (6,7). Upon stimulation with Wnt, LRP6 is phosphorylated at multiple sites including Thr1479, Ser1490, and Thr1493 by kinases such as GSK-3 and CK1 (8-10). Phosphorylated LRP6 recruits axin to the membrane and presumably activates β-catenin signaling (8-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Parkinson’s disease (PD), the second most common neurodegenerative disease after Alzheimer’s, is a progressive movement disorder characterized by rigidity, tremors, and postural instability. The pathological hallmarks of PD are progressive loss of dopaminergic neurons in the substantia nigra of the ventral midbrain and the presence of intracellular Lewy bodies (protein aggregates of α-synuclein, ubiquitin, and other components) in surviving neurons of the brain stem (1). Research studies have shown various genes and loci are genetically linked to PD including α-synuclein/PARK1 and 4, parkin/PARK2, UCH-L1/PARK5, PINK1/PARK6, DJ-1/PARK7, LRRK2/PARK8, synphilin-1, and NR4A2 (2).Leucine-rich repeat kinase 2 (LRRK2) contains amino-terminal leucine-rich repeats (LRR), a Ras-like small GTP binding protein-like (ROC) domain, an MLK protein kinase domain, and a carboxy-terminal WD40 repeat domain. Research studies have linked at least 20 LRRK2 mutations to PD, with the G2019S mutation being the most prevalent (3). The G2019S mutation causes increased LRRK2 kinase activity, which induces a progressive reduction in neurite length that leads to progressive neurite loss and decreased neuronal survival (4). Researchers are currently testing the MLK inhibitor CEP-1347 in PD clinical trials, indicating the potential value of LRRK2 as a therapeutic target for treatment of PD (5).

$305
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 LRRK2 (D18E12) Rabbit mAb #13046.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Parkinson’s disease (PD), the second most common neurodegenerative disease after Alzheimer’s, is a progressive movement disorder characterized by rigidity, tremors, and postural instability. The pathological hallmarks of PD are progressive loss of dopaminergic neurons in the substantia nigra of the ventral midbrain and the presence of intracellular Lewy bodies (protein aggregates of α-synuclein, ubiquitin, and other components) in surviving neurons of the brain stem (1). Research studies have shown various genes and loci are genetically linked to PD including α-synuclein/PARK1 and 4, parkin/PARK2, UCH-L1/PARK5, PINK1/PARK6, DJ-1/PARK7, LRRK2/PARK8, synphilin-1, and NR4A2 (2).Leucine-rich repeat kinase 2 (LRRK2) contains amino-terminal leucine-rich repeats (LRR), a Ras-like small GTP binding protein-like (ROC) domain, an MLK protein kinase domain, and a carboxy-terminal WD40 repeat domain. Research studies have linked at least 20 LRRK2 mutations to PD, with the G2019S mutation being the most prevalent (3). The G2019S mutation causes increased LRRK2 kinase activity, which induces a progressive reduction in neurite length that leads to progressive neurite loss and decreased neuronal survival (4). Researchers are currently testing the MLK inhibitor CEP-1347 in PD clinical trials, indicating the potential value of LRRK2 as a therapeutic target for treatment of PD (5).

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

Application Methods: Western Blotting

Background: Leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1, hTAL1) is a multi-domain-containing E3 ubiquitin-ligase involved in the regulation of cell adhesion. The LSRAM1 protein contains amino-terminal leucine-rich repeats (LRR), an ezrin-radixin-moesin (ERM) domain, a coiled-coil region, a sterile alpha motif (SAM) domain, and a carboxy-terminal RING finger domain. Research studies demonstrate that LRSAM1 participates in the endosomal sorting of proteins by regulating the ubiquitination of Tsg101, a component of the ESCRT-I endosomal sorting complex (1). LSRAM1 ubiquitin ligase activity plays a critical role in promoting the ubiquitin-dependent autophagic clearance of pathogenic bacteria (2). Mutations in the corresponding LRSAM1 gene can contribute to a form of Charcot-Marie-Tooth (CMT2P) disease that is characterized by peripheral nervous system axonal neuropathy (3,4).

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

Application Methods: Western Blotting

Background: Lysine-specific demethylase 1 (LSD1; also known as AOF2 and BHC110) is a nuclear amine oxidase homolog that acts as a histone demethylase and transcription cofactor (1). Gene activation and repression is specifically regulated by the methylation state of distinct histone protein lysine residues. For example, methylation of histone H3 at Lys4 facilitates transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (2,3). In contrast, methylation of histone H3 at Lys9 facilitates transcriptional repression by recruiting HP1 (4,5). LSD1 is a component of the CoREST transcriptional co-repressor complex that also contains CoREST, CtBP, HDAC1 and HDAC2. As part of this complex, LSD1 demethylates mono-methyl and di-methyl histone H3 at Lys4 through a FAD-dependent oxidation reaction to facilitate neuronal-specific gene repression in non-neuronal cells (1,6,7). In contrast, LSD1 associates with androgen receptor in human prostate cells to demethylate mono-methyl and di-methyl histone H3 at Lys9 and facilitate androgen receptor-dependent transcriptional activation (8). Therefore, depending on gene context LSD1 can function as either a transcriptional co-repressor or co-activator. LSD1 activity is inhibited by the amine oxidase inhibitors pargyline, deprenyl, clorgyline and tranylcypromine (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Lysine-specific demethylase 1 (LSD1; also known as AOF2 and BHC110) is a nuclear amine oxidase homolog that acts as a histone demethylase and transcription cofactor (1). Gene activation and repression is specifically regulated by the methylation state of distinct histone protein lysine residues. For example, methylation of histone H3 at Lys4 facilitates transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (2,3). In contrast, methylation of histone H3 at Lys9 facilitates transcriptional repression by recruiting HP1 (4,5). LSD1 is a component of the CoREST transcriptional co-repressor complex that also contains CoREST, CtBP, HDAC1 and HDAC2. As part of this complex, LSD1 demethylates mono-methyl and di-methyl histone H3 at Lys4 through a FAD-dependent oxidation reaction to facilitate neuronal-specific gene repression in non-neuronal cells (1,6,7). In contrast, LSD1 associates with androgen receptor in human prostate cells to demethylate mono-methyl and di-methyl histone H3 at Lys9 and facilitate androgen receptor-dependent transcriptional activation (8). Therefore, depending on gene context LSD1 can function as either a transcriptional co-repressor or co-activator. LSD1 activity is inhibited by the amine oxidase inhibitors pargyline, deprenyl, clorgyline and tranylcypromine (8).

$305
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 LSD1 (C69G12) Rabbit mAb #2184.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Lysine-specific demethylase 1 (LSD1; also known as AOF2 and BHC110) is a nuclear amine oxidase homolog that acts as a histone demethylase and transcription cofactor (1). Gene activation and repression is specifically regulated by the methylation state of distinct histone protein lysine residues. For example, methylation of histone H3 at Lys4 facilitates transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (2,3). In contrast, methylation of histone H3 at Lys9 facilitates transcriptional repression by recruiting HP1 (4,5). LSD1 is a component of the CoREST transcriptional co-repressor complex that also contains CoREST, CtBP, HDAC1 and HDAC2. As part of this complex, LSD1 demethylates mono-methyl and di-methyl histone H3 at Lys4 through a FAD-dependent oxidation reaction to facilitate neuronal-specific gene repression in non-neuronal cells (1,6,7). In contrast, LSD1 associates with androgen receptor in human prostate cells to demethylate mono-methyl and di-methyl histone H3 at Lys9 and facilitate androgen receptor-dependent transcriptional activation (8). Therefore, depending on gene context LSD1 can function as either a transcriptional co-repressor or co-activator. LSD1 activity is inhibited by the amine oxidase inhibitors pargyline, deprenyl, clorgyline and tranylcypromine (8).

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

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

Background: Lysine-specific demethylase 1 (LSD1; also known as AOF2 and BHC110) is a nuclear amine oxidase homolog that acts as a histone demethylase and transcription cofactor (1). Gene activation and repression is specifically regulated by the methylation state of distinct histone protein lysine residues. For example, methylation of histone H3 at Lys4 facilitates transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (2,3). In contrast, methylation of histone H3 at Lys9 facilitates transcriptional repression by recruiting HP1 (4,5). LSD1 is a component of the CoREST transcriptional co-repressor complex that also contains CoREST, CtBP, HDAC1 and HDAC2. As part of this complex, LSD1 demethylates mono-methyl and di-methyl histone H3 at Lys4 through a FAD-dependent oxidation reaction to facilitate neuronal-specific gene repression in non-neuronal cells (1,6,7). In contrast, LSD1 associates with androgen receptor in human prostate cells to demethylate mono-methyl and di-methyl histone H3 at Lys9 and facilitate androgen receptor-dependent transcriptional activation (8). Therefore, depending on gene context LSD1 can function as either a transcriptional co-repressor or co-activator. LSD1 activity is inhibited by the amine oxidase inhibitors pargyline, deprenyl, clorgyline and tranylcypromine (8).

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

Application Methods: Western Blotting

Background: Lysine-specific demethylase 2 (LSD2; also known as AOF1) is a nuclear amine oxidase homolog that acts as a histone demethylase and transcription cofactor protein (1,2). LSD2 functions as a co-repressor protein by demethylating mono-methyl and di-methyl histone H3 Lys4, two marks associated with actively transcribed genes (1,2). LSD2-mediated demethylation of histone H3 Lys4 is required for establishing proper DNA methylation imprints during oogenesis (3). In addition, LSD2 appears to be overexpressed in malignant breast cancers, where it contributes to DNA methylation and repression of multiple tumor suppressor genes (4,5). Furthermore, LSD2 also contains E3 ubiquitin ligase activity that targets O-GlcNac transferase (OGT) for proteosomal degradation (6). A549 lung cancer cell growth is dependent on this E3 ubiquitin ligase activity, suggesting that this function of LSD2 is also important for proper gene regulation (6).

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

Application Methods: Western Blotting

Background: LSm proteins are members of an ancient family of RNA binding proteins that function in RNA metabolism (1,2). Two LSm complexes or rings have been identified based on protein composition: LSm1-7 and LSm2-8 (1). The cytoplasmic LSm1-7 complex is involved in mRNA degradation (3) while the LSm2-8 ring is required for pre-tRNA and rRNA maturation (4,5) and regulation of pre-mRNA splicing through its association with U6 snRNA (6). Recent studies show that LSm2-8 complex functions in the biogenesis of telomerase RNA (1).

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

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

Background: The lipolysis-stimulated lipoprotein receptor (LSR, LISCH) is an immunoglobulin superfamily member and single pass transmembrane protein that binds the apolipoprotein B (ApoB) and apolipoprotein E (ApoE) lipoproteins (1). LSR is responsible for the cellular uptake of triacylglyceride-rich lipoproteins and supports lipid distribution between the liver and peripheral tissues (1,2). The LSR protein is expressed at the cell membrane as a heterodimer consisting of α and β subunits, which are produced as alternative splice variants from a single gene (3). Research studies suggest that LSR acts as the host cell surface receptor for multiple Clostridium toxins (4) and participates in the formation of tricellular tight junctions in epithelial cells (5). Additional studies demonstrate that LSR expression is up-regulated in several cancer types, including breast, bladder, and colorectal cancer, which could lead to pro-tumorigenic changes in metabolism (6-8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Lunatic Fringe (Beta-1,3-N-acetylglucosaminyltransferase, LFNG) is a single-pass type II Golgi membrane glycosyltransferase that catalyzes the elongation of O-linked fucose residues on EGF-like repeats of Notch signaling molecules. Fucosylation of EGF-like repeats serves to fine-tune Notch ligand-receptor interactions, thereby modulating downstream Notch pathway activity (1). Studies in genetic mouse models have shown that Lunatic Fringe-mediated Notch regulation is critical for somite patterning during vertebrate embryogenesis (2-4). Consistent with this, loss-of-function mutations in human LFNG are associated with spondylocostal dysostoses, a heritable skeletal growth disorder characterized by malformations of the spinal column and thoracic structures (5). Lunatic Fringe continues to modulate Notch signaling postnatally (6), and is implicated as a putative tumor suppressor in multiple Notch-related cancers (7, 8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Western Blotting

Background: Liver X receptors LXR-α and LXR-β are nuclear hormone receptor superfamily members responsible for regulating expression of target genes that control cholesterol transport and metabolism (1). When bound by the oxidized derivatives of cholesterol (oxysterols), activated LXR receptors function as sterol sensors to regulate transcription of the genes involved in the cholesterol homeostasis (1,2). The LXR-α protein is expressed at high levels in rat liver, kidney, intestine, adipose, and spleen; LXR-β is more ubiquitously expressed within rat tissues (1,3). Research studies indicate that glucose binds and up-regulates the transcriptional activity of LXR-α and LXR-β (4). LXR-α and LXR-β are putative glucose sensors that integrate glucose metabolism and fatty acid biosynthesis in the liver (4). Additional studies show that female mice deficient in LXR-β develop gallbladder cancer (5). In addition, LXR-β plays a role in protecting dopaminergic neurons in a Parkinson disease model (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Lyn, one of the Src family members, is predominantly expressed in hematopoietic cells (1). Two tyrosine residues have been reported to play a crucial role in the regulation of protein tyrosine kinases of the Src family. Autophosphorylation of Tyr396 (equivalent to Tyr416 of Src), located in the catalytic domain, correlates with enzyme activation. Csk-mediated phosphorylation of the carboxy-terminal Tyr507 (equivalent to Tyr527 of Src) inactivates the kinase. Tyrosine phosphorylation and activation of Lyn occurs upon association with cell surface receptors such as the B cell Ag receptor (BCR) and CD40 (2-4). Studies using knockout mice have shown that the net effect of Lyn deficiency is to render B cells hypersensitive to BCR stimulation (5-7), suggesting that the most critical role for Lyn in vivo is in the down-regulation of B cell responses. Lyn is also involved in controlling the migration and development of specific B cell populations (8).

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

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

Background: Lyn, one of the Src family members, is predominantly expressed in hematopoietic cells (1). Two tyrosine residues have been reported to play a crucial role in the regulation of protein tyrosine kinases of the Src family. Autophosphorylation of Tyr396 (equivalent to Tyr416 of Src), located in the catalytic domain, correlates with enzyme activation. Csk-mediated phosphorylation of the carboxy-terminal Tyr507 (equivalent to Tyr527 of Src) inactivates the kinase. Tyrosine phosphorylation and activation of Lyn occurs upon association with cell surface receptors such as the B cell Ag receptor (BCR) and CD40 (2-4). Studies using knockout mice have shown that the net effect of Lyn deficiency is to render B cells hypersensitive to BCR stimulation (5-7), suggesting that the most critical role for Lyn in vivo is in the down-regulation of B cell responses. Lyn is also involved in controlling the migration and development of specific B cell populations (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

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

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

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

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

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

Background: Lysyl-tRNA synthetase (LysRS) is a multifunctional protein that has both regular and mitochondrial forms. The regular form of LysRS belongs to a family of aminoacyl-tRNA synthetases (aaRSs) that catalyze amino acid attachment to its cognate tRNA. In mammalian systems, LysRS forms a multisystem complex (MSC) with several other aaRSs (1-3). In addition to its conventional function, LysRS regulates diadenosine tetraphosphate (Ap4A) production (3). Cellular and metabolic stress increases the level of Ap4A, which functions as a cellular alarm system (3-5). Following FcεRI aggregation in mast cells, MAPK/Erk kinase (MEK) phosphorylates LysRS at Ser207 (5). Serine phosphorylation of LysRS leads to the release of LysRS from MSC and its translocation into the nucleus (5), as well as increased synthesis of Ap4A (5,6). LysRS binds to microphthalmia transcription factor (MITF) and MITF repressor Hint-1. Upon binding of Ap4A, Hint-1 is released from the complex that in turn allows the transcription of MITF-responsive genes (5-7). LysRS is also involved in HIV viral assembly through incorporation into HIV-1 virions via an interaction with HIV-1 Gag (8). Research studies have shown that in the presence of mutant Cu,Zn-superoxide dismutase (SOD1), mitochondrial LysRS tends to be misfolded and degraded by proteasomal degradation, contributing to mitochondrial dysfunction in Amyotrophic Lateral Sclerosis (ALS) (9). LysRS is also secreted and has cytokine-like functions (10). LysRS was also found to be an autoantigen in autoimmune responses (11).

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

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

Background: Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

$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 M-CSF Receptor (D3O9X) XP® Rabbit mAb #67455.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Macrophage-colony stimulating factor (M-CSF, CSF-1) receptor is an integral membrane tyrosine kinase encoded by the c-fms proto-oncogene. M-CSF receptor is expressed in monocytes (macrophages and their progenitors) and drives growth and development of this blood cell lineage. (1-3). Binding of M-CSF to its receptor induces receptor dimerization, activation, and autophosphorylation of cytoplasmic tyrosine residues used as docking sites for SH2-containing signaling proteins (4). There are at least five major tyrosine autophosphorylation sites. Tyr723 (Tyr721 in mouse) is located in the kinase insert (KI) region. Phosphorylated Tyr723 binds the p85 subunit of PI3 kinase as well as PLCγ2 (5). Phosphorylation of Tyr809 provides a docking site for Shc (5). Overactivation of this receptor can lead to a malignant phenotype in various cell systems (6). The activated M-CSF receptor has been shown to be a predictor of poor outcome in advanced epithelial ovarian carcinoma (7) and breast cancer (8).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Macrophage-colony stimulating factor (M-CSF, CSF-1) receptor is an integral membrane tyrosine kinase encoded by the c-fms proto-oncogene. M-CSF receptor is expressed in monocytes (macrophages and their progenitors) and drives growth and development of this blood cell lineage. (1-3). Binding of M-CSF to its receptor induces receptor dimerization, activation, and autophosphorylation of cytoplasmic tyrosine residues used as docking sites for SH2-containing signaling proteins (4). There are at least five major tyrosine autophosphorylation sites. Tyr723 (Tyr721 in mouse) is located in the kinase insert (KI) region. Phosphorylated Tyr723 binds the p85 subunit of PI3 kinase as well as PLCγ2 (5). Phosphorylation of Tyr809 provides a docking site for Shc (5). Overactivation of this receptor can lead to a malignant phenotype in various cell systems (6). The activated M-CSF receptor has been shown to be a predictor of poor outcome in advanced epithelial ovarian carcinoma (7) and breast cancer (8).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Macrophage-colony stimulating factor (M-CSF, CSF-1) receptor is an integral membrane tyrosine kinase encoded by the c-fms proto-oncogene. M-CSF receptor is expressed in monocytes (macrophages and their progenitors) and drives growth and development of this blood cell lineage. (1-3). Binding of M-CSF to its receptor induces receptor dimerization, activation, and autophosphorylation of cytoplasmic tyrosine residues used as docking sites for SH2-containing signaling proteins (4). There are at least five major tyrosine autophosphorylation sites. Tyr723 (Tyr721 in mouse) is located in the kinase insert (KI) region. Phosphorylated Tyr723 binds the p85 subunit of PI3 kinase as well as PLCγ2 (5). Phosphorylation of Tyr809 provides a docking site for Shc (5). Overactivation of this receptor can lead to a malignant phenotype in various cell systems (6). The activated M-CSF receptor has been shown to be a predictor of poor outcome in advanced epithelial ovarian carcinoma (7) and breast cancer (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Macrophage-colony stimulating factor (M-CSF, CSF-1) receptor is an integral membrane tyrosine kinase encoded by the c-fms proto-oncogene. M-CSF receptor is expressed in monocytes (macrophages and their progenitors) and drives growth and development of this blood cell lineage. (1-3). Binding of M-CSF to its receptor induces receptor dimerization, activation, and autophosphorylation of cytoplasmic tyrosine residues used as docking sites for SH2-containing signaling proteins (4). There are at least five major tyrosine autophosphorylation sites. Tyr723 (Tyr721 in mouse) is located in the kinase insert (KI) region. Phosphorylated Tyr723 binds the p85 subunit of PI3 kinase as well as PLCγ2 (5). Phosphorylation of Tyr809 provides a docking site for Shc (5). Overactivation of this receptor can lead to a malignant phenotype in various cell systems (6). The activated M-CSF receptor has been shown to be a predictor of poor outcome in advanced epithelial ovarian carcinoma (7) and breast cancer (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Myosin phosphatase-rho interacting protein (M-RIP), also known as p116RIP, RIP3, and MPRIP, localizes to actin-myosin filaments regulating cytoskeletal dynamics (1-3). M-RIP contains amino-terminal pleckstrin homology domains, carboxyl-terminal coiled-coil domains, and was originally identified to associate with the myosin phosphatase complex. M-RIP binds to MBS/MYRT, the myosin binding subunit of myosin phosphatase, as well as RhoA (1-3). Phosphorylation of MYRT by Rho-associated kinase (ROCK) inhibits myosin phosphatase activity, resulting in increased levels of phosphorylation on myosin light chain, and enhanced contractility (4,5). M-RIP may function as a scaffolding protein for the complex between the myosin phosphatase complex, Rho/ROCK, and actin (2,6). Silencing of M-RIP results in disassembly of the complex, increased phosphorylation of myosin light chain, and changes to cytoskeletal dynamics (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Myosin phosphatase-rho interacting protein (M-RIP), also known as p116RIP, RIP3, and MPRIP, localizes to actin-myosin filaments regulating cytoskeletal dynamics (1-3). M-RIP contains amino-terminal pleckstrin homology domains, carboxyl-terminal coiled-coil domains, and was originally identified to associate with the myosin phosphatase complex. M-RIP binds to MBS/MYRT, the myosin binding subunit of myosin phosphatase, as well as RhoA (1-3). Phosphorylation of MYRT by Rho-associated kinase (ROCK) inhibits myosin phosphatase activity, resulting in increased levels of phosphorylation on myosin light chain, and enhanced contractility (4,5). M-RIP may function as a scaffolding protein for the complex between the myosin phosphatase complex, Rho/ROCK, and actin (2,6). Silencing of M-RIP results in disassembly of the complex, increased phosphorylation of myosin light chain, and changes to cytoskeletal dynamics (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The gene encoding metastasis-associated in colon cancer-1 (MACC1) was identified based on its overexpression in metastatic colon carcinoma (1), and was later shown to be overexpressed in multiple human cancers, including hepatocellular carcinoma, gastric cancer, head and neck cancer, and breast cancer (2-5). MACC1 regulates HGF/MET and β-catenin signaling, resulting in increased proliferation, migration and invasion, and initiation of the epithelial-mesenchymal transition (EMT) (2). Researchers have shown that MACC1 can be used as a prognostic indicator in solid tumors, and that it has potential as a therapeutic target (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Histone macroH2A1 and macroH2A2 comprise a family of variant histone H2A proteins. MacroH2A1 exists as two distinct isoforms due to alternative splicing of a single gene; macroH2A1.1 levels accumulate throughout differentiation and development while macroH2A1.2 shows a constant level of expression (1). MacroH2A1 and macroH2A2 are encoded by completely distinct genes located on separate chromosomes (2,3). Both macroH2A1 and macroH2A2 proteins contain an amino-terminal histone-like region with 64% sequence identity to canonical histone H2A, in addition to a carboxy-terminal “macro” domain (1-3). MacroH2A1 and macroH2A2 are enriched in facultative heterochromatin, including inactivated X chromosomes in mammalian females and senescence-associated heterochromatin foci (2-5). Both act to repress gene transcription by inhibiting the binding of transcription factors to chromatin, the acetylation of histones by p300, and the chromatin-remodeling activities of SWI/SNF and ACF (6,7). The macro domain of macroH2A1.1 binds to ADP-ribose and functions to recruit macroH2A1.1 to activated PARP at sites of DNA damage, where it mediates chromatin rearrangements to locally regulate the DNA damage response (8). MacroH2A1.2 and macroH2A2 do not bind poly-ADP-ribose and are not recruited to sites of activated PARP (8).