8311 Results for: "Magnesium+phosphate+pentahydrate"

Supplier: Bioss

Phosphatidic acid and lysophosphatidic acid are phospholipids involved in lipid biosynthesis and signal transduction. LPAAT-epsilon (lysophosphatidic acid acyltransferase epsilon, also designated 1-AGP acyltransferase 5 (AGPAT5)) catalyzes the synthesis of phosphatidic acid from lysophosphatidic acid. LPAAT-epsilon is a membrane-bound protein belonging to the LPAAT family. Members of the LPAAT family have a well-known role in lipid biosynthesis and they may also play a role in tumor progression. LPAAT-epsilon is expressed in a tissue-specific manner in prostate and testis. LPAAT-epsilon is most closely related to AGPAT8, which is highly expressed in heart.

Supplier: Bioss

Phosphatidic acid and lysophosphatidic acid are phospholipids involved in lipid biosynthesis and signal transduction. LPAAT-epsilon (lysophosphatidic acid acyltransferase epsilon, also designated 1-AGP acyltransferase 5 (AGPAT5)) catalyzes the synthesis of phosphatidic acid from lysophosphatidic acid. LPAAT-epsilon is a membrane-bound protein belonging to the LPAAT family. Members of the LPAAT family have a well-known role in lipid biosynthesis and they may also play a role in tumor progression. LPAAT-epsilon is expressed in a tissue-specific manner in prostate and testis. LPAAT-epsilon is most closely related to AGPAT8, which is highly expressed in heart.

Supplier: Bioss

Phosphatidic acid and lysophosphatidic acid are phospholipids involved in lipid biosynthesis and signal transduction. LPAAT-epsilon (lysophosphatidic acid acyltransferase epsilon, also designated 1-AGP acyltransferase 5 (AGPAT5)) catalyzes the synthesis of phosphatidic acid from lysophosphatidic acid. LPAAT-epsilon is a membrane-bound protein belonging to the LPAAT family. Members of the LPAAT family have a well-known role in lipid biosynthesis and they may also play a role in tumor progression. LPAAT-epsilon is expressed in a tissue-specific manner in prostate and testis. LPAAT-epsilon is most closely related to AGPAT8, which is highly expressed in heart.

Supplier: Bioss

This gene encodes a protein that belongs to the pi3/pi4-kinase family of proteins. The gene product is an enzyme that phosphorylates phosphoinositides on the 3-hydroxyl group of the inositol ring. It is an important modulator of extracellular signals, including those elicited by E-cadherin-mediated cell-cell adhesion, which plays an important role in maintenance of the structural and functional integrity of epithelia. In addition to its role in promoting assembly of adherens junctions, the protein is thought to play a pivotal role in the regulation of cytotoxicity in NK cells. The gene is located in a commonly deleted segment of chromosome 7 previously identified in myeloid leukemias. [provided by RefSeq, Jul 2008].

Supplier: Bioss

Phosphatidic acid and lysophosphatidic acid are phospholipids involved in lipid biosynthesis and signal transduction. LPAAT-epsilon (lysophosphatidic acid acyltransferase epsilon, also designated 1-AGP acyltransferase 5 (AGPAT5)) catalyzes the synthesis of phosphatidic acid from lysophosphatidic acid. LPAAT-epsilon is a membrane-bound protein belonging to the LPAAT family. Members of the LPAAT family have a well-known role in lipid biosynthesis and they may also play a role in tumor progression. LPAAT-epsilon is expressed in a tissue-specific manner in prostate and testis. LPAAT-epsilon is most closely related to AGPAT8, which is highly expressed in heart.

Supplier: Bioss

Phosphatidic acid and lysophosphatidic acid are phospholipids involved in lipid biosynthesis and signal transduction. LPAAT-epsilon (lysophosphatidic acid acyltransferase epsilon, also designated 1-AGP acyltransferase 5 (AGPAT5)) catalyzes the synthesis of phosphatidic acid from lysophosphatidic acid. LPAAT-epsilon is a membrane-bound protein belonging to the LPAAT family. Members of the LPAAT family have a well-known role in lipid biosynthesis and they may also play a role in tumor progression. LPAAT-epsilon is expressed in a tissue-specific manner in prostate and testis. LPAAT-epsilon is most closely related to AGPAT8, which is highly expressed in heart.

Supplier: ProSci Inc.

The de novo synthesis of pyrimidine nucleotides is required for mammalian cells to proliferate. This gene encodes a trifunctional protein which is associated with the enzymatic activities of the first 3 enzymes in the 6-step pathway of pyrimidine biosynthesis: carbamoylphosphate synthetase (CPS II), aspartate transcarbamoylase, and dihydroorotase. This protein is regulated by the mitogen-activated protein kinase (MAPK) cascade, which indicates a direct link between activation of the MAPK cascade and de novo biosynthesis of pyrimidine nucleotides.

Supplier: MIELE

Liquid, acidic citric acid based cleaning concentrate for automated cleaning of laboratory glassware and reusable laboratory material.

Supplier: Bioss

Increase in fetal surfactant synthesis and lung maturity is caused by the glucocorticoidal induction of enzymes required for phosphatidylcholine synthesis towards the end of gestation (1). The regulation of gestational age-dependent induction of phosphatidylcholine synthesis by glucocorticoids is still unclear (1). The rate-controlling enzyme in the phosphatidylcholine biosynthetic pathway is CTP-phosphocholine cytidylyltransferase A (CCT A) (2–4). In cultured eukaryotic cells, this enzyme is essential for survival (3). The alpha isoform is located in the nucleus and is regulated by reversible phosphorylation and membrane association (3). There is significant identity between the alpha-helical membrane-binding domains of CCT A and soybean oleosin (2). Expressed CCT A has lipid-dependent cytidylyltransferase activity (5). The gene which encodes CCT A maps to human chromosome 3q (4).

Supplier: Bioss

Increase in fetal surfactant synthesis and lung maturity is caused by the glucocorticoidal induction of enzymes required for phosphatidylcholine synthesis towards the end of gestation (1). The regulation of gestational age-dependent induction of phosphatidylcholine synthesis by glucocorticoids is still unclear (1). The rate-controlling enzyme in the phosphatidylcholine biosynthetic pathway is CTP-phosphocholine cytidylyltransferase A (CCT A) (2–4). In cultured eukaryotic cells, this enzyme is essential for survival (3). The alpha isoform is located in the nucleus and is regulated by reversible phosphorylation and membrane association (3). There is significant identity between the alpha-helical membrane-binding domains of CCT A and soybean oleosin (2). Expressed CCT A has lipid-dependent cytidylyltransferase activity (5). The gene which encodes CCT A maps to human chromosome 3q (4).

Supplier: Bioss

Increase in fetal surfactant synthesis and lung maturity is caused by the glucocorticoidal induction of enzymes required for phosphatidylcholine synthesis towards the end of gestation (1). The regulation of gestational age-dependent induction of phosphatidylcholine synthesis by glucocorticoids is still unclear (1). The rate-controlling enzyme in the phosphatidylcholine biosynthetic pathway is CTP-phosphocholine cytidylyltransferase A (CCT A) (2–4). In cultured eukaryotic cells, this enzyme is essential for survival (3). The alpha isoform is located in the nucleus and is regulated by reversible phosphorylation and membrane association (3). There is significant identity between the alpha-helical membrane-binding domains of CCT A and soybean oleosin (2). Expressed CCT A has lipid-dependent cytidylyltransferase activity (5). The gene which encodes CCT A maps to human chromosome 3q (4).

Supplier: Bioss

Increase in fetal surfactant synthesis and lung maturity is caused by the glucocorticoidal induction of enzymes required for phosphatidylcholine synthesis towards the end of gestation (1). The regulation of gestational age-dependent induction of phosphatidylcholine synthesis by glucocorticoids is still unclear (1). The rate-controlling enzyme in the phosphatidylcholine biosynthetic pathway is CTP-phosphocholine cytidylyltransferase A (CCT A) (2–4). In cultured eukaryotic cells, this enzyme is essential for survival (3). The alpha isoform is located in the nucleus and is regulated by reversible phosphorylation and membrane association (3). There is significant identity between the alpha-helical membrane-binding domains of CCT A and soybean oleosin (2). Expressed CCT A has lipid-dependent cytidylyltransferase activity (5). The gene which encodes CCT A maps to human chromosome 3q (4).

Supplier: CUSTOM MADE CHEMICALS LAB

11 COMPONENTS MIX 1 * 500 mL

Supplier: Bioss

Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.

Supplier: Bioss

Increase in fetal surfactant synthesis and lung maturity is caused by the glucocorticoidal induction of enzymes required for phosphatidylcholine synthesis towards the end of gestation (1). The regulation of gestational age-dependent induction of phosphatidylcholine synthesis by glucocorticoids is still unclear (1). The rate-controlling enzyme in the phosphatidylcholine biosynthetic pathway is CTP-phosphocholine cytidylyltransferase A (CCT A) (2–4). In cultured eukaryotic cells, this enzyme is essential for survival (3). The alpha isoform is located in the nucleus and is regulated by reversible phosphorylation and membrane association (3). There is significant identity between the alpha-helical membrane-binding domains of CCT A and soybean oleosin (2). Expressed CCT A has lipid-dependent cytidylyltransferase activity (5). The gene which encodes CCT A maps to human chromosome 3q (4).

Supplier: Bioss

Increase in fetal surfactant synthesis and lung maturity is caused by the glucocorticoidal induction of enzymes required for phosphatidylcholine synthesis towards the end of gestation (1). The regulation of gestational age-dependent induction of phosphatidylcholine synthesis by glucocorticoids is still unclear (1). The rate-controlling enzyme in the phosphatidylcholine biosynthetic pathway is CTP-phosphocholine cytidylyltransferase A (CCT A) (2–4). In cultured eukaryotic cells, this enzyme is essential for survival (3). The alpha isoform is located in the nucleus and is regulated by reversible phosphorylation and membrane association (3). There is significant identity between the alpha-helical membrane-binding domains of CCT A and soybean oleosin (2). Expressed CCT A has lipid-dependent cytidylyltransferase activity (5). The gene which encodes CCT A maps to human chromosome 3q (4).

Supplier: ProSci Inc.

Neomycin phosphotransferase II (nptII) gene is used in selection of transformed organisms. It was initially isolated from the transposon Tn5 that was present in the bacterium strain Escherichia coli K12. The gene codes for the aminoglycoside 3'-phosphotransferase (denoted aph(3')-II or NPTII) enzyme. NPTII is probably the most widely used selectable marker for plant transformation. It is also used in gene expression and regulation studies in different organisms in part because N-terminal fusions can be constructed that retain enzymatic activity. In animal cells, G418 and neomycin are used as selectable agents.

Supplier: Bioss

Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.

Supplier: Shimadzu Diagnostics Europe

CompactDry Swabs for surfaces, meat, fish and poultry. New design with swabs pre immersed in 1 ml buffer, ready for use with a self-standing tube and a high visibility blue cap and swab.

Supplier: Bioss

Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.

Supplier: Bioss

Increase in fetal surfactant synthesis and lung maturity is caused by the glucocorticoidal induction of enzymes required for phosphatidylcholine synthesis towards the end of gestation (1). The regulation of gestational age-dependent induction of phosphatidylcholine synthesis by glucocorticoids is still unclear (1). The rate-controlling enzyme in the phosphatidylcholine biosynthetic pathway is CTP-phosphocholine cytidylyltransferase A (CCT A) (2–4). In cultured eukaryotic cells, this enzyme is essential for survival (3). The alpha isoform is located in the nucleus and is regulated by reversible phosphorylation and membrane association (3). There is significant identity between the alpha-helical membrane-binding domains of CCT A and soybean oleosin (2). Expressed CCT A has lipid-dependent cytidylyltransferase activity (5). The gene which encodes CCT A maps to human chromosome 3q (4).

Supplier: Bioss

Increase in fetal surfactant synthesis and lung maturity is caused by the glucocorticoidal induction of enzymes required for phosphatidylcholine synthesis towards the end of gestation (1). The regulation of gestational age-dependent induction of phosphatidylcholine synthesis by glucocorticoids is still unclear (1). The rate-controlling enzyme in the phosphatidylcholine biosynthetic pathway is CTP-phosphocholine cytidylyltransferase A (CCT A) (2–4). In cultured eukaryotic cells, this enzyme is essential for survival (3). The alpha isoform is located in the nucleus and is regulated by reversible phosphorylation and membrane association (3). There is significant identity between the alpha-helical membrane-binding domains of CCT A and soybean oleosin (2). Expressed CCT A has lipid-dependent cytidylyltransferase activity (5). The gene which encodes CCT A maps to human chromosome 3q (4).

Supplier: Bioss

Increase in fetal surfactant synthesis and lung maturity is caused by the glucocorticoidal induction of enzymes required for phosphatidylcholine synthesis towards the end of gestation (1). The regulation of gestational age-dependent induction of phosphatidylcholine synthesis by glucocorticoids is still unclear (1). The rate-controlling enzyme in the phosphatidylcholine biosynthetic pathway is CTP-phosphocholine cytidylyltransferase A (CCT A) (2–4). In cultured eukaryotic cells, this enzyme is essential for survival (3). The alpha isoform is located in the nucleus and is regulated by reversible phosphorylation and membrane association (3). There is significant identity between the alpha-helical membrane-binding domains of CCT A and soybean oleosin (2). Expressed CCT A has lipid-dependent cytidylyltransferase activity (5). The gene which encodes CCT A maps to human chromosome 3q (4).

Supplier: Bioss

Increase in fetal surfactant synthesis and lung maturity is caused by the glucocorticoidal induction of enzymes required for phosphatidylcholine synthesis towards the end of gestation (1). The regulation of gestational age-dependent induction of phosphatidylcholine synthesis by glucocorticoids is still unclear (1). The rate-controlling enzyme in the phosphatidylcholine biosynthetic pathway is CTP-phosphocholine cytidylyltransferase A (CCT A) (2–4). In cultured eukaryotic cells, this enzyme is essential for survival (3). The alpha isoform is located in the nucleus and is regulated by reversible phosphorylation and membrane association (3). There is significant identity between the alpha-helical membrane-binding domains of CCT A and soybean oleosin (2). Expressed CCT A has lipid-dependent cytidylyltransferase activity (5). The gene which encodes CCT A maps to human chromosome 3q (4).

Supplier: Bioss

Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.

Supplier: Bioss

Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.

Supplier: Bioss

Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.

Supplier: Bioss

Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.

Supplier: Bioss

Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.

Supplier: Bioss

Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.