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Product listing: PKM1/2 (C5E6) Rabbit mAb, UniProt ID P14618 #3106 to Tom20 (D8T4N) Rabbit mAb, UniProt ID Q15388 #42406

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated PKM2 (D78A4) XP® Rabbit mAb #4053.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PKM2 (D78A4) XP® Rabbit mAb #4053.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

$348
400 µl
This Cell Signaling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated sepharose® beads. PKM2 (D78A4) XP® Rabbit mAb (Sepharose® Bead Conjugate) is useful for the immunoprecipitation of PKM2. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated PKM2 (D78A4) XP® Rabbit mAb #4053.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

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

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

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Phospholipase A2 (PLA2) is a superfamily of enzymes that hydrolyze glycero-3-phosphocholines and release fatty acids and lysophospholipids (1). PLA2G1B is a member of this superfamily in the 1B group that is expressed most highly in the pancreatic acinar cells (2). Evidence suggests that PLA2G1B plays a role in the absorption and storage of extra energy as fats are metabolized (1,2). Lysophospholipids generated by PLA2G1B inhibit fatty acid oxidation in the liver and reduce energy expenditure, leading to diet-induced obesity and type 2 diabetes with a high fat diet (1). Therefore, a potential intervention of obesity and diabetes could target PLA2G1B in the digestive tract (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The placenta-specific gene 8 (Plac8) encodes a chromatin-binding protein that was first identified from placenta and that is highly expressed in plasmacytoid dendritic cells (1,2). Research studies indicate that Plac8 plays a role in immune function and is essential in the differentiation of brown fat (3,4). During brown fat differentiation, Plac8 interacts with the transcription factor C/EBPβ at its promoter sequence to activate the transcription of C/EBPβ (4). Experimental deletion of Plac8 in mice leads to impaired innate immune function, abnormal brown fat function, cold intolerance, and obesity (3,4). Additional studies examining the spread of colorectal carcinoma suggest a possible role for Plac8 in cancer invasion, possibly through promoting the epithelial-to-mesenchymal transition seen during tumor progression (5).

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

Application Methods: Western Blotting

Background: Prdx1 belongs to a family of non-seleno peroxidases that function as H2O2 scavengers. All 6 Prdx isoforms share a conserved N-terminal cysteine (Cys51) that is oxidized by H2O2 to form cysteine-sulfenic acid (Cys51-SOH) and, in turn, reacts with Cys172-SH of another Prdx protein, forming a disulfide dimer and protecting it from degradation (1-3). Abnormally high levels of H2O2 cause Prdx1 to form an oligomeric chaperone that loses its peroxidase activity (4). Prdx family members have been reported to bind to JNK and c-Abl and regulate their kinase activity (5,6). Prdx1 was shown to bind to PTEN and regulate its phosphatase activity in conditions of mild or no cellular stress, hence preventing Akt-driven transformation by protecting PTEN from oxidation-induced inactivation (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Peroxiredoxin 6 (PRDX6) belongs to an antioxidant enzyme family of non-seleno peroxidases. PRDX6 is a unique member of the PRDX family, exhibiting both glutathione peroxidase and phospholipase A2 activities (1,2). PRDX6 regulates phospholipid turnover in addition to protecting cells against oxidative injury. PRDX6 is expressed in all major organs, with a particularly high level in lung, where it regulates lung surfactant phospholipid synthesis and turnover (3-5). Research studies have shown that PRDX6 is aberrantly expressed in various cancers, and can promote cancer cell metastasis and invasion (6,7). Elevated expression of PRDX6 and related PRDX family members has also been shown to contribute to drug resistance in cancer cells (8,9). PRDX6 is also expressed in neutrophils, where it has been shown to activate NADPH oxidase (NOX2) (10-12).

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

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin)

Background: Glucose homeostasis is regulated by a variety of hormones including glucagon. Glucagon is synthesized as the precursor molecule proglucagon and is proteolytically processed to yield the mature peptide in α cells of the pancreatic islets. Glucagon causes the release of glucose from glycogen and stimulates gluconeogenesis in the liver (1,2).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: The pyruvate dehydrogenase complex catalyzes the conversion of pyruvate and CoA into acetyl-CoA and CO2 in the presence of NAD+. Acetyl-CoA then goes into the citric acid cycle where it reacts with oxaloacetate to form citrate. Acetyl-CoA is also used for fatty acid and cholesterol biosynthesis. The reaction of oxidative decarboxylation of pyruvate therefore serves as a critical link between glycolysis and the citric acid cycle and lipid metabolism. In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix (1). This complex is comprised of three enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3). Pyruvate dehydrogenase (E1) consists of two subunits: α and β. This enzyme catalyzes the removal of CO2 from pyruvate. Mutations in the α subunits of pyruvate dehydrogenase (E1) lead to congenital defects that are usually associated with lactic acidosis, neurodegeneration and early death (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Stearoyl-CoA desaturase 1 (SCD1) is a key lipogenic enzyme found in the endoplasmic reticulum that catalyzes the conversion of palmitoyl–CoA and stearoyl–CoA to palmitoleoyl–CoA (16:1) and oleoyl–CoA (18:1) (1-3). Palmitoleate and oleate are the major components of triglycerides, membrane phospholipids and cholesterol esters (1). SCD1-knockout mice show improved insulin sensitivity and reduced body fat (1). Disruption of SCD1 in mouse brown adipose tissue strengthens insulin signaling and results in increased translocation of Glut4 to plasma membrane and enhanced uptake of glucose (4). Furthermore, SCD1 is essential for the onset of diet-induced body weight gain (1) and insulin resistance in the liver (5).

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

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

Background: Succinate dehydrogenase (SDH), also known as Complex II or succinate:quinone oxidoreductase, is a key component of the citric acid cycle and the electron transport chain (1). Specifically, it is involved in the oxidation of succinate (2). SDH consists of four subunits: SDHA, SDHB, SDHC, and SDHD (3). Research studies have shown that defects in SDHA cause complex II deficiency (2). In addition, investigators have observed reduction of SDHA in the striatum of patients with Huntington’s disease (3), and reduction of SDHB, SDHC, and SDHD in paragangliomas and phenochromocytomas (4,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Serine hydroxymethyltransferases 1 and 2 (SHMT1, SHMT2) are cytoplasmic and mitochondrial serine hydroxylmethyltransferases, respectively (1,2). They catalyze the conversion of serine to glycine with the transfer of β-carbon from serine to tetrahydrofolate (THF) to form 5, 10-methylene-THF (1, 2). Research studies indicate that SHMT1 hemizygosity is associated with higher risk of intestinal cancer in mice of a certain genetic background (3). Suppression of SHMT2 was shown to block cell proliferation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Salt-inducible kinase 1 (SIK1) was originally identified as a serine/threonine kinase from adrenocortical tissues of rats on a high salt diet (1). SIK1 is a SNF1/AMPK family kinase capable of autophosphorylation (1). SIK2 is an isoform of SIK1 and is specifically expressed in adipose tissues where it is induced during adipocyte differentiation (2). Studies suggest that SIK2 can phosphorylate human insulin receptor substrate (IRS-1) at Ser794. Along with evidence that SIK2 expression and activity are increased in white adipocytes of diabetic mice, this finding suggests a possible role for SIK2 in regulating insulin signaling in adipocytes and in the development of insulin resistance (2,3). Insulin triggers Akt2-mediated phosphorylation of SIK2 at Ser358 and the resultant kinase activation during post-fasting feeding (4). The activated SIK2 then induces the phosphorylation of Torc2 at Ser171 resulting in translocation of this transcriptional coactivator from the nucleus to cytoplasm where it is degraded through the ubiquitin pathway, leading to inhibition of gluconeogenic gene expression (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: SNAT1/SLC38A1 belongs to the system A transporters that mediate Na+-dependent transport of short-chain neutral amino acids such as alanine, serine, and glutamine. SNAT1/SLC38A1 mediates the uptake of glutamine in neurons and plays a crucial role in glutamate-glutamine cycle. Steep concentration gradients across the plasma membrane are achieved by coupling of the electrochemical sodium gradient to amino acid transport. This allows a unidirectional mode of transport for SNAT1/SLC38A1. Upregulation of SNAT1/SLC38A1 by neurotrophic factors is key to dendritic growth and branching of cortical neurons. High expression of SNAT1/SLC38A1 is found in cerebral cortex primarily in neurons and to a lesser extent in astrocytes (1-4). Elevated SNAT1/SLC38A1 expression is prominent in human solid tumors including gliomas, hepatocellular carcinomas and human breast cancer (5-8). Research studies show that an aberrant SNAT1/SLC38A1 expression profile correlates with solid tumor recurrence and poor prognosis in patients with cholangiocarcinoma (9).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Manganese superoxide dismutase (MnSOD or SOD2) is a mitochondrial detoxification enzyme that catalyzes the conversion of superoxide to hydrogen peroxide (1,2). Hydrogen peroxide is then decomposed to water by catalase, glutathione peroxidase, or peroxiredoxins (2). MnSOD/SOD2 and other enzymes involved in antioxidant defense protect cells from reactive oxygen species (ROS) (2). Calorie restriction leads to SIRT3-mediated deacetylation of MnSOD/SOD2 and the subsequent increase of its antioxidant activity (3). MnSOD/SOD2 also plays an essential role in mediating the protective effect of mTOR inhibition to reduce epithelial stem cell senescence (4).

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

Application Methods: Western Blotting

Background: Manganese superoxide dismutase (MnSOD or SOD2) is a mitochondrial detoxification enzyme that catalyzes the conversion of superoxide to hydrogen peroxide (1,2). Hydrogen peroxide is then decomposed to water by catalase, glutathione peroxidase, or peroxiredoxins (2). MnSOD/SOD2 and other enzymes involved in antioxidant defense protect cells from reactive oxygen species (ROS) (2). Calorie restriction leads to SIRT3-mediated deacetylation of MnSOD/SOD2 and the subsequent increase of its antioxidant activity (3). MnSOD/SOD2 also plays an essential role in mediating the protective effect of mTOR inhibition to reduce epithelial stem cell senescence (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The Sprouty (Spry) family of proteins are antagonists of receptor tyrosine kinase (RTK)-induced signaling (1, 2). The Spry proteins play crucial roles in regulating growth and development of living organisms. Since originally discovered in Drosophila, four human orthologs of Spry proteins (Spry1-4) have been identified. All human Spry proteins possess a conserved carboxyl-terminal cysteine-rich SPR domain, which harbors a signal for protein translocation from cytosol to membrane ruffles (3,4). The SPR domain also enables the Spry proteins to form homo- or hetero-dimers and to interact with other proteins including kinases and phosphatases. The SPR domain is essential for the inhibitory modulation of Spry proteins on RTK signaling (1,2).

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

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

Background: Steroidogenic acute regulatory protein (StAR) plays a significant role in cholesterol transport from the cytoplasmic outer membrane to the inner mitochondrial membrane (1). The 37 kDa precursor is cleaved to generate an active 28 kDa protein capable of facilitating cholesterol metabolism into pregnenolone (2,3). StAR is prevalently expressed in mitochondria of steroid-producing adrenal and gonadal tissue (3). Abnormalities in StAR gene expression are impacted in autosomal Lipoid Congenial Adrenal Hyperplasia (LCAH) resulting in defects in pregnenolone and cortisol synthesis (4). The mechanism of cholesterol binding to StAR has yet to be elucidated (4).

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

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

Background: Succinyl-CoA synthetase α subunit (SUCLG1) catalyzes the conversion of succinate to succinyl-CoA and plays a key role in the citric acid cycle (1,2). Deficiency of this enzyme leads to a variety of diseases including fatal infantile lactic acidosis (3) and mitochondrial hepatoencephalomyopathy (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Insulin binds to and activates its receptor and initiates a signaling cascade that eventually induces the translocation of the Glut4 glucose transporter from its intracellular locations to the plasma membrane. Initiating this pathway facilitates glucose uptake in fat and skeletal muscle cells (1). Synip and Syntaxin 4 are two proteins thought to be involved in the recruitment of Glut4-containing vesicles to plasma membrane (2,3). Synip associates with Syntaxin 4 when insulin is absent. Insulin signaling triggers the dissociation of the two proteins and allows Syntaxin 4 to complex with VAMP2, which is essential for Glut4 translocation to plasma membrane (2-4). Overexpression of a dominant-negative form of Synip prevents Glut4 from translocating to plasma membrane in response to insulin stimulation (3). Synip together with Syntaxin 4, therefore, regulates Glut 4 transport to plasma membrane.

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: TBC1D1 is a paralog of AS160 (1) and both proteins share about 50% identity (2). TBC1D1 was shown to be a candidate gene for severe obesity (3). It plays a role in Glut4 translocation through its GAP activity (2,4). Studies indicate that TBC1D1 is highly expressed in skeletal muscle (1). Insulin, AICAR, and contraction directly regulate TBC1D1 phosphorylation in this tissue (1). Three AMPK phosphorylation sites (Ser231, Ser660, and Ser700) and one Akt phosphorylation site (Thr590) were identified in skeletal muscle (5). Muscle contraction or AICAR treatment increases phosphorylation on Ser231, Ser660, and Ser700 but not on Thr590; insulin increases phosphorylation on Thr590 only (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Thioredoxin is a small redox protein found in many eukaryotes and prokaryotes. A pair of cysteines within a highly conserved, active site sequence can be oxidized to form a disulfide bond that is then reduced by thioredoxin reductase (1). Multiple forms of thioredoxin have been identified, including cytosolic thioredoxin 1 (TRX1) and mitochondrial thioredoxin 2 (TRX2). Thioredoxin participates in many cellular processes including redox signaling, response to oxidative stress, and protein reduction (1). A potential role of thioredoxin in human disorders such as cancer, aging, and heart disease is currently under investigation (2). Thioredoxin can play a key role in cancer progression, because it acts as a negative regulator of the proapoptotic kinase ASK1 (3). Changes in thioredoxin expression have been associated with meningococcal septic shock and acute lung injury (4,5).

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

Application Methods: Western Blotting

Background: Thioredoxin is a small redox protein found in many eukaryotes and prokaryotes. A pair of cysteines within a highly conserved, active site sequence can be oxidized to form a disulfide bond that is then reduced by thioredoxin reductase (1). Multiple forms of thioredoxin have been identified, including cytosolic thioredoxin 1 (TRX1) and mitochondrial thioredoxin 2 (TRX2). Thioredoxin participates in many cellular processes including redox signaling, response to oxidative stress, and protein reduction (1). A potential role of thioredoxin in human disorders such as cancer, aging, and heart disease is currently under investigation (2). Thioredoxin can play a key role in cancer progression, because it acts as a negative regulator of the proapoptotic kinase ASK1 (3). Changes in thioredoxin expression have been associated with meningococcal septic shock and acute lung injury (4,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) is an essential step in the formation of thymine nucleotides (1,2, reviewed in 3). This process is catalyzed by thymidylate synthase (TS or TYMS), a homodimer composed of two 30 kDa subunits. TS is an intracellular enzyme that provides the sole de novo source of thymidylate, making it a required enzyme in DNA biosynthesis with activity highest in proliferating cells (1). Being the exclusive source of dTMP, investigators have concluded that TS is also an important target for anticancer agents such as 5-fluorouracil (5-FU) (1-5). 5-FU acts as a TS inhibitor and is active against solid tumors such as colon, breast, head, and neck. Research studies have demonstrated that patients with metastases expressing lower levels of TS have a higher response rate to treatment with 5-FU than patients with tumors that have increased levels of TS (5). Researchers continue to investigate TS expression in different types of cancers (6-10).

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

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

Background: The methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) is an essential step in the formation of thymine nucleotides (1,2, reviewed in 3). This process is catalyzed by thymidylate synthase (TS or TYMS), a homodimer composed of two 30 kDa subunits. TS is an intracellular enzyme that provides the sole de novo source of thymidylate, making it a required enzyme in DNA biosynthesis with activity highest in proliferating cells (1). Being the exclusive source of dTMP, investigators have concluded that TS is also an important target for anticancer agents such as 5-fluorouracil (5-FU) (1-5). 5-FU acts as a TS inhibitor and is active against solid tumors such as colon, breast, head, and neck. Research studies have demonstrated that patients with metastases expressing lower levels of TS have a higher response rate to treatment with 5-FU than patients with tumors that have increased levels of TS (5). Researchers continue to investigate TS expression in different types of cancers (6-10).

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

Application Methods: Western Blotting

Background: The methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) is an essential step in the formation of thymine nucleotides (1,2, reviewed in 3). This process is catalyzed by thymidylate synthase (TS or TYMS), a homodimer composed of two 30 kDa subunits. TS is an intracellular enzyme that provides the sole de novo source of thymidylate, making it a required enzyme in DNA biosynthesis with activity highest in proliferating cells (1). Being the exclusive source of dTMP, investigators have concluded that TS is also an important target for anticancer agents such as 5-fluorouracil (5-FU) (1-5). 5-FU acts as a TS inhibitor and is active against solid tumors such as colon, breast, head, and neck. Research studies have demonstrated that patients with metastases expressing lower levels of TS have a higher response rate to treatment with 5-FU than patients with tumors that have increased levels of TS (5). Researchers continue to investigate TS expression in different types of cancers (6-10).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Tom20 (D8T4N) Rabbit mAb #42406.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Mitochondria play a central role in cellular energy metabolism and are essential organelles in eukaryotes. In humans, 13 proteins are encoded by the mitochondrial genome while the vast majority of mitochondrial proteins are encoded by the nuclear genome. As a result, most mitochondrial proteins are synthesized as precursors in the cytoplasm and imported across mitochondrial membranes by one or more translocase protein complexes (1). The translocase of the outer mitochondrial membrane (TOM complex) facilitates the import of proteins through the outer mitochondrial membrane, while the complementary translocase of the inner membrane (TIM complex) is responsible for protein transport to the mitochondrial matrix. The TOM complex consists of the receptors Tom20, Tom22, and Tom70, and the channel-forming protein Tom40 (1). Tom20 is localized in the outer mitochondrial membrane and initially recognizes precursors with a presequence to facilitate protein import across the outer mitochondrial membrane (2). In a sequential process, recognition of the presequence by Tom20 is followed by tethering of the presequence to the Tom40 protein complex for efficient protein import (3).

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

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

Background: Mitochondria play a central role in cellular energy metabolism and are essential organelles in eukaryotes. In humans, 13 proteins are encoded by the mitochondrial genome while the vast majority of mitochondrial proteins are encoded by the nuclear genome. As a result, most mitochondrial proteins are synthesized as precursors in the cytoplasm and imported across mitochondrial membranes by one or more translocase protein complexes (1). The translocase of the outer mitochondrial membrane (TOM complex) facilitates the import of proteins through the outer mitochondrial membrane, while the complementary translocase of the inner membrane (TIM complex) is responsible for protein transport to the mitochondrial matrix. The TOM complex consists of the receptors Tom20, Tom22, and Tom70, and the channel-forming protein Tom40 (1). Tom20 is localized in the outer mitochondrial membrane and initially recognizes precursors with a presequence to facilitate protein import across the outer mitochondrial membrane (2). In a sequential process, recognition of the presequence by Tom20 is followed by tethering of the presequence to the Tom40 protein complex for efficient protein import (3).