735 Results for: "Ferric+pyrophosphate"

Supplier: Bioss

By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity and function.

Supplier: Bioss

By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity and function.

Supplier: Bioss

By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity and function.

Supplier: Apollo Scientific

Ethylene Diamine Tetraacetic Acid Ferric Sodium Salt Trihydrate 500g pack 1 * 500 g

Supplier: ProSci Inc.

RABGGTB catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A and RAB5A respectively.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: MP Biomedicals

Ferric sulphate is used in dyeing as a mordant, and as a coagulant for industrial wastes. It is also used in pigments, and in pickling baths for aluminum and steel. Medically it is used as an astringent and styptic. It also acts as an important oxidative agent.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: MP Biomedicals

Potassium ferrocyanide trihydrate is a salt of the Fe(CN)₆^4- ferrocyanide ion. Ferrocyanide is a reducing iron species, being oxidised from ferrous Fe(II) to ferric Fe(III).

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: Bioss

Phosphoribosyl pyrophosphate amidotransferase (PPAT) is a regulatory allosteric enzyme that catalyzes the first step of de novo purine nucleotide biosynthesis. The genes for PPAT and PAICS/AIRC, (a bifunctional enzyme catalyzing steps six and seven in the purine nucleotide biosynthesis pathway), are located in close proximity on chromosome 4.

Supplier: Thermo Fisher Scientific

Hemin derived from porcine is an iron-containing prosthetic group present in some proteins and can be an alternative source of iron within the host that contains a porphyrin ring containing a Fe2+ ion.
Hemin is a protoporphyrin IX containing a ferric iron (Fe3+) ion with a coordinating chloride ligand

Supplier: ProSci Inc.

Ferritin is a large, iron-storage heteropolymeric protein,which is expressed in most kinds of cells and co-assemble in different proportion in a tissue-specific manner. Ferritin has oligomer of 24 subunits and two types of subunits including light chain(FTL) and heavy chain. Ferritin can remove Fe (Ⅱ) from solution in the presence of oxygen and is very important for iron homeostasis. Iron is absorbed in the ferrous form and deposited as ferric hydroxides after oxidation. Iron is first oxidised to the ferric state for storage as ferric oxyhdroxide whithin the protein shell of ferritin. Thus, ferritin removes excess iron from the cell sap where it could otherwise participate in peroxidation mechanisms. Ferritin also plays a role in delivery of iron to cells and mediates iron uptake in capsule cells of the developing kidney.

Supplier: OriGene

PRPS2 (Myc-DDK-tagged)-Human phosphoribosyl pyrophosphate synthetase 2 (PRPS2), transcript variant 1 1 * 10 µG

Supplier: Bioss

ILVBL is a 632 amino acid single-pass membrane protein that belongs to the TPP enzyme family. Expressed in the majority of tissues, ILVBL has the highest level of expression in heart, pancreas and placenta. ILVBL is highly homologous to several bacterial enzymes, including the B isozyme of the large catalytic subunit of E. coli acetohydroxy-acid synthase (AHAS) and the oxalyl-coA decarboxylase of O. formigenes, that utilize thiamine pyrophosphate as a cofactor. ILVBL binds one magnesium ion and one thiamine pyrophosphate per subunit, and may catalyse the initial step in branched-chain amino acid biosynthesis. The gene encoding ILVBL maps to human chromosome 19p13.12 and mouse chromosome 10 C1.

Supplier: Bioss

ILVBL is a 632 amino acid single-pass membrane protein that belongs to the TPP enzyme family. Expressed in the majority of tissues, ILVBL has the highest level of expression in heart, pancreas and placenta. ILVBL is highly homologous to several bacterial enzymes, including the B isozyme of the large catalytic subunit of E. coli acetohydroxy-acid synthase (AHAS) and the oxalyl-coA decarboxylase of O. formigenes, that utilize thiamine pyrophosphate as a cofactor. ILVBL binds one magnesium ion and one thiamine pyrophosphate per subunit, and may catalyze the initial step in branched-chain amino acid biosynthesis. The gene encoding ILVBL maps to human chromosome 19p13.12 and mouse chromosome 10 C1.

Supplier: Bioss

Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).

Supplier: Bioss

ILVBL is a 632 amino acid single-pass membrane protein that belongs to the TPP enzyme family. Expressed in the majority of tissues, ILVBL has the highest level of expression in heart, pancreas and placenta. ILVBL is highly homologous to several bacterial enzymes, including the B isozyme of the large catalytic subunit of E. coli acetohydroxy-acid synthase (AHAS) and the oxalyl-coA decarboxylase of O. formigenes, that utilize thiamine pyrophosphate as a cofactor. ILVBL binds one magnesium ion and one thiamine pyrophosphate per subunit, and may catalyze the initial step in branched-chain amino acid biosynthesis. The gene encoding ILVBL maps to human chromosome 19p13.12 and mouse chromosome 10 C1.

Supplier: Bioss

Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity).

Supplier: Bioss

ILVBL is a 632 amino acid single-pass membrane protein that belongs to the TPP enzyme family. Expressed in the majority of tissues, ILVBL has the highest level of expression in heart, pancreas and placenta. ILVBL is highly homologous to several bacterial enzymes, including the B isozyme of the large catalytic subunit of E. coli acetohydroxy-acid synthase (AHAS) and the oxalyl-coA decarboxylase of O. formigenes, that utilize thiamine pyrophosphate as a cofactor. ILVBL binds one magnesium ion and one thiamine pyrophosphate per subunit, and may catalyze the initial step in branched-chain amino acid biosynthesis. The gene encoding ILVBL maps to human chromosome 19p13.12 and mouse chromosome 10 C1.

Supplier: Bioss

ILVBL is a 632 amino acid single-pass membrane protein that belongs to the TPP enzyme family. Expressed in the majority of tissues, ILVBL has the highest level of expression in heart, pancreas and placenta. ILVBL is highly homologous to several bacterial enzymes, including the B isozyme of the large catalytic subunit of E. coli acetohydroxy-acid synthase (AHAS) and the oxalyl-coA decarboxylase of O. formigenes, that utilize thiamine pyrophosphate as a cofactor. ILVBL binds one magnesium ion and one thiamine pyrophosphate per subunit, and may catalyze the initial step in branched-chain amino acid biosynthesis. The gene encoding ILVBL maps to human chromosome 19p13.12 and mouse chromosome 10 C1.

Supplier: Bioss

ILVBL is a 632 amino acid single-pass membrane protein that belongs to the TPP enzyme family. Expressed in the majority of tissues, ILVBL has the highest level of expression in heart, pancreas and placenta. ILVBL is highly homologous to several bacterial enzymes, including the B isozyme of the large catalytic subunit of E. coli acetohydroxy-acid synthase (AHAS) and the oxalyl-coA decarboxylase of O. formigenes, that utilize thiamine pyrophosphate as a cofactor. ILVBL binds one magnesium ion and one thiamine pyrophosphate per subunit, and may catalyze the initial step in branched-chain amino acid biosynthesis. The gene encoding ILVBL maps to human chromosome 19p13.12 and mouse chromosome 10 C1.