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Product listing: MRP6/ABCC6 (D9D1F) Rabbit mAb, UniProt ID O95255 #10666 to MUC5AC (E3O9I) XP® Rabbit mAb, UniProt ID P98088 #61193

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The multidrug resistance-associated protein 6 (MRP6, ABCC6) is a member of ATP-binding cassette (ABC) family transporters that move drugs and hydrophobic compounds across cell membranes. The MRP6 protein is expressed mainly in liver and kidney, and in other tissues to a lesser extent (1). Identified MRP6 substrates include the glutathione conjugate of N-ethylmaleimide (NEM-GS) and leukotriene C4 (LTC4), with more tentative MRP6 substrates under investigation (2,3). Research studies show that increased MRP6 expression correlates with induced cholesterol biosynthesis, which suggests that MRP6 may be involved in lipid and cholesterol homeostasis (4). A small isoform of MRP6 is up-regulated in HBV infected hepatocytes and protects the cells from apoptosis mediated by caspase 3 and caspase 8 (5,6). Mutations in the corresponding ABCC6 gene cause pseudoxanthoma elasticum (PXE), an autosomal recessive disorder that is characterized by the accumulation of mineralized and fragmented elastic fibers in the skin, eyes, and arteries (7,8). Mutations in ABCC6 also result in generalized arterial calcification of infancy, an ectopic calcification disease that lies along a spectrum of similar disorders with PXE (9).

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

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

Background: A subset of mitochondrial proteins are synthesized on the ribosomes within mitochondria (1). The 55S mammalian mitochondrial ribosomes are composed of a 28S small subunit and a 39S large subunit (1). Over 40 protein components have been identified from the large subunit of the human mitochondrial ribosome (1). The mitochondrial ribosomal protein L11 (MRPL11) is one such component (1). In animals, plants and fungi, this protein is translated from a gene in the nuclear genome (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The DNA mismatch repair system (MMR) repairs post-replication DNA, inhibits recombination between non-identical DNA sequences and induces both checkpoint and apoptotic responses following certain types of DNA damage (1). MSH2 (MutS homologue 2) forms the hMutS-α dimer with MSH6 and is an essential component of the mismatch repair process. hMutS-α is part of the BRCA1-associated surveillance complex (BASC), a complex that also contains BRCA1, MLH1, ATM, BLM, PMS2 proteins and the Rad50-Mre11-NBS1 complex (2).Mutations in MSH2 have been found in a large proportion of hereditary non-polyposis colorectal cancer (Lynch Syndrome), the most common form of inherited colorectal cancer in the Western world (3). Mutations have also been associated with other sporadic tumors.

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

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

Background: The DNA mismatch repair system (MMR) repairs post-replication DNA, inhibits recombination between non-identical DNA sequences and induces both checkpoint and apoptotic responses following certain types of DNA damage (1). MSH2 (MutS homologue 2) forms the hMutS-α dimer with MSH6 and is an essential component of the mismatch repair process. hMutS-α is part of the BRCA1-associated surveillance complex (BASC), a complex that also contains BRCA1, MLH1, ATM, BLM, PMS2 proteins and the Rad50-Mre11-NBS1 complex (2).Mutations in MSH2 have been found in a large proportion of hereditary non-polyposis colorectal cancer (Lynch Syndrome), the most common form of inherited colorectal cancer in the Western world (3). Mutations have also been associated with other sporadic tumors.

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The DNA mismatch repair system (MMR) repairs post-replication DNA, inhibits recombination between nonidentical DNA sequences, and induces both checkpoint and apoptotic responses following certain types of DNA damage (1). MSH2 (MutS homologue 2) forms the hMutS-α dimer with MSH6 and is an essential component of the mismatch repair process. hMutS-α is part of the BRCA1-associated surveillance complex (BASC), a complex that also contains BRCA1, MLH1, ATM, BLM, PMS2 proteins, and the Rad50-Mre11-NBS1 complex (2). Mutations in MSH6 and other MMR proteins have been found in a large proportion of hereditary nonpolyposis colorectal cancer (Lynch Syndrome), the most common form of inherited colorectal cancer in the Western world (3). Mutations in MSH6 have been shown to occur in glioblastoma in response to temozolomide therapy and to promote temozolomide resistance (4).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The DNA mismatch repair system (MMR) repairs post-replication DNA, inhibits recombination between nonidentical DNA sequences, and induces both checkpoint and apoptotic responses following certain types of DNA damage (1). MSH2 (MutS homologue 2) forms the hMutS-α dimer with MSH6 and is an essential component of the mismatch repair process. hMutS-α is part of the BRCA1-associated surveillance complex (BASC), a complex that also contains BRCA1, MLH1, ATM, BLM, PMS2 proteins, and the Rad50-Mre11-NBS1 complex (2). Mutations in MSH6 and other MMR proteins have been found in a large proportion of hereditary nonpolyposis colorectal cancer (Lynch Syndrome), the most common form of inherited colorectal cancer in the Western world (3). Mutations in MSH6 have been shown to occur in glioblastoma in response to temozolomide therapy and to promote temozolomide resistance (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: MSK1, a mitogen and stress activated protein kinase, is activated by Erk as well as p38 MAPK in response to growth factors and cellular stress, respectively (1). MSK1 resembles RSK because it has two kinase domains connected by a regulatory linker region (2). Phosphorylation of RSK1 at Ser364 and Ser381 is critical for RSK1 activity (3). These sites are analogous to Ser360 and Ser376 of MSK1, which may be important for MSK1 activity as well.

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Mitogen- and stress-activated protein kinase 1 (MSK1) and MSK2 are serine/threonine kinases that promote immediate early gene transcription in stress- or mitogen-induced cells (1-4,7, 8) and LPS-stimulated macrophages (9). MSK2, also known as RSKB, contains two catalytic domains and has been shown to interact directly with p38 MAP kinase (10). MSK2 is phosphorylated and activated in response to tumor necrosis factor, epidermal growth factor or phorbol ester in HeLa cells or murine embryonic fibroblasts (MEFs) in a p38- and ERK-dependent manner (8,11). Phosphorylation on residues Ser196 and Thr568 within the activation loop of both catalytic domains is required for full kinase activation (11). Both MSK1 and MSK2 contain a functional nuclear localization sequence that is sufficient and required for nuclear targeting (10). Consistent with their nuclear localization, these kinases play an important role in regulating transcriptional responses to stress and mitogens. Activation of MSK2 in HeLa cells or MEFs results in rapid phosphorylation of histone H3, HMG-14, CREB and ATF1 and acetylation of histone H3 associated with immediate early gene transcription (3,4,6,7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Male-specific lethal 2-homolog (MSL2) is a component of the male-specific lethal (MSL) histone acetyltransferase complex, which contains MSL1, MSL2, MSL3, and MYST1. MYST1, also known as mammalian male absent on the first (MOF) and lysine acetyltransferase 8 (KAT8), is a member of the MYST (MOZ, YBF2, SAS2, and Tip60) family of histone acetyltransferases (1,2) and functions as the catalytic subunit of the MSL complex. The MSL complex is responsible for the majority of acetylation on histone H4 lysine 16 (3-5). In addition, as part of the MSL complex, MSL1 and MSL2 function as an E3 ubiquitin ligase to mono-ubiquitylate histone H2B on lysine 34 (6). The MSL complex plays a critical role in the regulation of transcription, DNA repair, autophagy, apoptosis, and embryonic stem cell pluripotency and differentiation (1,2,6,7). Loss of MSL activity leads to a global reduction in histone H4 lysine 16 acetylation, a common hallmark found in many human cancers. In particular, the reduction of MYST1 protein levels and histone H4 lysine 16 acetylation is associated with poor prognosis in breast, renal, colorectal, gastric, and ovarian cancers (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Macrophage Scavenger receptor types I and II (MSR1, and also known as SCARA1) are members of the class A macrophage scavenger receptor family. These proteins bind large quantities of modified lipoproteins and promote endocytosis. Upregulation of MSR1 in infiltrating myeloid cells may mediate clearance of specific damage signals in response to tissue injury, including ischemic stroke (1). MSR1 germ line mutations are also associated with increased prostate cancer susceptibility in some patient cohorts (2). MSR1 is observed to be upregulated in differentiated THP-1 cells (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Mammalian sterile-20-like (MST) kinases are upstream regulators of mitogen-activated protein kinase (MAPK) signaling pathways that regulate multiple cellular processes, including proliferation, apoptosis, migration, and cytoskeletal rearrangement (1). This family of serine/threonine kinases includes MST1 (STK4) and MST2 (STK3), two functionally related proteins with conserved amino-terminal kinase domains and carboxy-terminal regulatory domains that contain nuclear export signals (1-3). During apoptosis, caspase-mediated cleavage of MST1/2 removes the inhibitory regulatory domain, triggering autophosphorylation and activation of the kinase domain, which is translocated to the nucleus. Nuclear translocation of the active kinase induces chromatin condensation and other events associated with apoptotic progression (4).Research studies indicate that MST1/2 are orthologous to Drosophila Hippo (Hpo), one of the core regulatory proteins in the Hippo signaling pathway. This evolutionarily conserved program controls tissue growth and organ size by regulating cell proliferation, apoptosis, and stem cell self-renewal. The mammalian Hippo signaling pathway involves a kinase cascade, where the MST1/2 kinases and the SAV1 scaffold protein form a complex that leads to phosphorylation and activation of LATS1/2. The LATS1/2 kinases phosphorylate YAP and TAZ, promoting cytoplasmic sequestration and inhibition of these transcription coactivators (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The matrix metalloproteinase (MMP) family of proteases are a group of zinc-dependent enzymes that target extracellular proteins, including growth factors, cell surface receptors, adhesion molecules, and other proteases (1). Matrix metalloproteinases can be broadly categorized based on function and cellular localization, and include six distinct membrane-type (MT) metalloproteinases that share a transmembrane domain and short cytoplasmic tail (2). Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP14) is involved in regulating development, angiogenesis, tissue remodeling, and tumor progression (3-6). MT1-MMP and other metalloproteinases promote tumor cell invasion by accumulating in specialized structures known as invadopodia, which remodel the ECM and allow tumor cells to breach the basement membrane (7). The abundance and presence of MT1-MMP at the cell surface is controlled by targeted endocytosis, which may be regulated by the MT1-MMP cytoplasmic domain (8). MT1-MMP protease activity can be further regulated through homodimer formation, autocatalytic processing, domain shedding and the interaction with inhibitory proteins. Activation of the MT1-MMP proenzyme results from cleavage of full-length MT1-MMP by furin in the trans-Golgi network, which removes the inhibitory propeptide domain (9). At the cell surface, MT1-MMP can be found in a protein complex with the soluble metalloproteinase MMP2 and the MMP inhibitor TIMP2. MT1-MMP mediated cleavage and activation of MMP2 generates the active MMP2 collagenase, which plays important roles in ECM remodeling and tumor invasion (10). MT1-MMP interacts with a large number of substrates in addition to MMP2, including interstitial collagens, adhesive glycoproteins (i.e. laminin), and cell surface receptors (11).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: MTA1 (metastasis associated gene 1) was identified in a differential screening of a cDNA library of metastatic and nonmetastatic adenocarcinoma cell lines (1), and was subsequently found to be an integral member of the nucleosome remodeling and deacetylation (NuRD) complex (2,3). MTA1 expression is upregulated under hypoxic conditions and found to enhance angiogenesis through stabilization of HIF-1α (4,5). MTA1 is overexpressed in a wide range of human cancers, and its expression is associated with malignancy and tumor progression (6). MTA1 is an essential downstream effector of c-Myc transformation (7). Recently, MTA1 was demonstrated to play a role in DNA damage response (8,9).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: MTA1 (metastasis associated gene 1) was identified in a differential screening of a cDNA library of metastatic and nonmetastatic adenocarcinoma cell lines (1), and was subsequently found to be an integral member of the nucleosome remodeling and deacetylation (NuRD) complex (2,3). MTA1 expression is upregulated under hypoxic conditions and found to enhance angiogenesis through stabilization of HIF-1α (4,5). MTA1 is overexpressed in a wide range of human cancers, and its expression is associated with malignancy and tumor progression (6). MTA1 is an essential downstream effector of c-Myc transformation (7). Recently, MTA1 was demonstrated to play a role in DNA damage response (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: MTAP is an enzyme that is essential for the salvage pathway for both adenine and methionine synthesis. MTAP catalyzes the cleavage of 5’-methylthioadenosine into adenine and 5-methylthio-D-ribose-1-phosphate. Adenine is then used to generate AMP whereas 5-methylthio-D-ribose-1-phosphate is converted into methionine (1,2). MTAP is expressed in all normal cells and tissues, although frequently lost in different human tumors including pancreatic adenocarcinoma, neuroendocrine tumors, non-small cell lung carcinoma and breast carcinoma. MTAP is usually codeleted with p16 (cdkN2a/ARF) (3-5). MTAP overexpression in breast cancer cells inhibits their ability to form colonies in soft agar, thereby implicating its function as a tumor suppressor (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: MutT Homolog 1 (MTH1), an oxidized purine nucleoside triphosphatase, hydrolyzes potentially mutagenic oxidized nucleotide triphosphates, preventing their accumulation in nucleotide pools and their incorporation into DNA and RNA (1). In addition to its function in sanitizing the cell’s nucleotide pool, MTH1 has been shown to have anti-proliferative effects in RAS-transformed tumors (2). Researchers have shown that, while not essential in normal cells, MTH1 is required for cancer cell survival due to increased oxidative damage, and that inhibition of MTH1 activity suppresses cancer growth (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: NADP+ dependent methylenetetrahydrofolate dehydrogenase 1-like (MTHFD1L) is a mitochondrial enzyme that catalyzes the production of formate from 10-formyl-tetrahydrofolate, the last step in one-carbon (1-C) flow from mitochondria to cytoplasm (1,2). These one-carbon end products are required for de novo synthesis of thymidylate and purines. In the mitochondria, these essential one-carbon products are formed by a series of reactions catalyzed by a pair of enzymes (MTHFD2 and MTHFD1L), but by the trifunctional MTHFD1 enzyme in the cytoplasm (3). The 10-formyl-tetrahydrofolate synthetase MTHFD1L is widely expressed in most adult tissues and at all stages of mammalian embryonic development (1). Research studies using MTHFD1L knockout mice indicate that MTHFD1L plays an essential role in neural tube formation; mice lacking MTHFD1L displayed neural tube and craniofacial defects leading to embryonic lethality (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MTHFD2 is a bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase involved in mitochondrial folate metabolism (1). MTHFD2 expression is developmentally regulated, as it is expressed in embryos but not in most adult tissues. Recent research studies have shown that MTHFD2 is consistently overexpressed in many cancer types and correlated with poor survival in breast cancer (2-5). Overexpression of MTHFD2 promotes cell proliferation while its depletion induces cell death in human cancer cells (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Methylenetetrahydrofolate reductase (MTHFR), a key enzyme in one-carbon metabolism, catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate. 5-methyltetrahydrofolate donates its methyl group for remethylation of homocysteine to methionine. Methionine is further converted to S-adenosylmethionine (SAM), a major reactive methyl carrier. DNA methyltransferases and histone methyltransferases use SAM to methylate DNA and histones with concomitant conversion of SAM to S-adenosylhomocysteine (SAH) (1, 2). In addition, MTHFR is inhibited by SAM and this feedback inhibition is partially reduced by SAH (3). Metabolically regulated levels of SAM and SAM/SAH ratio are shown to predict histone methylation levels, indicating the important role of enzymes in one-carbon metabolism including MTHFR in determining histone methylation status (4).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated mTOR (7C10) Rabbit mAb #2983.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometry in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated mTOR (7C10) Rabbit mAb #2983.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

$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 mTOR (7C10) Rabbit mAb #2983.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

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

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

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

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

Application Methods: Western Blotting

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

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

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

Background: Metastasis suppressor 1 (MTSS1) is a multi-functional scaffold protein that was initially discovered using a differential display technique that identified proteins missing from bladder cancer cell lines (1,2). MTSS1 (also known as Missing in Metastasis or MIM) is a cytoskeletal remodeling protein that contains a C-terminal WH2 actin-binding motif (1,3). Presence of an IMD (IRSp53/MIM homology) domain allows MTSS1 to induce F-actin bundling and filopodia formation in cells (4). MTSS1 binds to and activates Rac, a protein known to promote the formation of filopodia and lamellipodia (5). The receptor tyrosine phosphatase δ (PTPRD) is associated with MTSS1 and is required for MTSS1-dependent cytoskeletal change (6,7). MTSS1 is a SHH responsive gene that can help regulate GLI-dependent transcriptional activity (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 MUC1 (D9O8K) XP® Rabbit mAb #14161.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Mucins represent a family of glycoproteins characterized by repeat domains and dense O-glycosylation (1). MUC1 (or mucin 1) is aberrantly overexpressed in most human carcinomas. Increased expression of MUC1 in carcinomas reduces cell-cell and cell-ECM interactions. MUC1 is cleaved proteolytically, and the large ectodomain can remain associated with the small 25 kDa carboxy-terminal domain that contains a transmembrane segment and a 72-residue cytoplasmic tail (1). MUC1 interacts with ErbB family receptors and potentiates ERK1/2 activation (2). MUC1 also interacts with β-catenin, which is regulated by GSK-3β, PKCγ, and Src through phosphorylation at Ser44, Thr41, and Tyr46 of the MUC1 cytoplasmic tail (3-5). Overexpression of MUC1 potentiates transformation (6) and attenuates stress-induced apoptosis through the Akt or p53 pathways (7,8).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Mucins represent a family of glycoproteins characterized by repeat domains and dense O-glycosylation (1). MUC1 (or mucin 1) is aberrantly overexpressed in most human carcinomas. Increased expression of MUC1 in carcinomas reduces cell-cell and cell-ECM interactions. MUC1 is cleaved proteolytically, and the large ectodomain can remain associated with the small 25 kDa carboxy-terminal domain that contains a transmembrane segment and a 72-residue cytoplasmic tail (1). MUC1 interacts with ErbB family receptors and potentiates ERK1/2 activation (2). MUC1 also interacts with β-catenin, which is regulated by GSK-3β, PKCγ, and Src through phosphorylation at Ser44, Thr41, and Tyr46 of the MUC1 cytoplasmic tail (3-5). Overexpression of MUC1 potentiates transformation (6) and attenuates stress-induced apoptosis through the Akt or p53 pathways (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Mucins represent a family of glycoproteins characterized by repeat domains and dense O-glycosylation (1). MUC1 (or mucin 1) is aberrantly overexpressed in most human carcinomas. Increased expression of MUC1 in carcinomas reduces cell-cell and cell-ECM interactions. MUC1 is cleaved proteolytically, and the large ectodomain can remain associated with the small 25 kDa carboxy-terminal domain that contains a transmembrane segment and a 72-residue cytoplasmic tail (1). MUC1 interacts with ErbB family receptors and potentiates ERK1/2 activation (2). MUC1 also interacts with β-catenin, which is regulated by GSK-3β, PKCγ, and Src through phosphorylation at Ser44, Thr41, and Tyr46 of the MUC1 cytoplasmic tail (3-5). Overexpression of MUC1 potentiates transformation (6) and attenuates stress-induced apoptosis through the Akt or p53 pathways (7,8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Mucins represent a family of glycoproteins characterized by repeat domains and dense O-glycosylation (1). MUC1 (or mucin 1) is aberrantly overexpressed in most human carcinomas. Increased expression of MUC1 in carcinomas reduces cell-cell and cell-ECM interactions. MUC1 is cleaved proteolytically, and the large ectodomain can remain associated with the small 25 kDa carboxy-terminal domain that contains a transmembrane segment and a 72-residue cytoplasmic tail (1). MUC1 interacts with ErbB family receptors and potentiates ERK1/2 activation (2). MUC1 also interacts with β-catenin, which is regulated by GSK-3β, PKCγ, and Src through phosphorylation at Ser44, Thr41, and Tyr46 of the MUC1 cytoplasmic tail (3-5). Overexpression of MUC1 potentiates transformation (6) and attenuates stress-induced apoptosis through the Akt or p53 pathways (7,8).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Mucins are a family of macromolecules that line and protect the respiratory epithelium from microbes and pollutants in the local environment. Of the family members that are known to date, some are produced in a cell type and tissue-specific manner, suggesting distinct biological roles for members. Some members polymerize after secretion to form gel-like substances that coat the epithelial layer. MUC5AC and MUC5B are members of the family that polymerize in this manner. Others do not polymerize, and others yet, have a transmembrane domain and remain physically attached to the epithelia (1). While it is known that mucins are protective to the respiratory epithelium, it has been reported that changes in expression of mucins are associated with several forms of lung disease such as cystic fibrosis, COPD, asthma, pulmonary fibrosis, and others (2,3,4,1). Multiple epithelial malignancies have been described to show changes in expression, localization, and glycosylation of MUC5AC. This wide association with multiple malignancy types has led to the emergence of MUC5AC as both a prognostic and therapeutic target for cancer (5).