You Searched For: Pyridoxine+hydrochloride

Catalog Number: (10671-506)

Supplier: Bioss

Description: Pyridoxal kinase belongs to the pyridoxine kinase family and phosphorylates vitamin B6, a step necessary for the conversion of vitamin B6 to pyridoxal 5’ phosphate (PLP), the active form of vitamin B6. PLP acts as a coenzyme and functions to maintain homeostasis. Pyridoxal kinase is a 312-amino acid cytoplasmic protein that may act as a homodimer and is expressed ubiquitously. There are three known isoforms of pyridoxal kinase, and isoform 3 expression is observed in adult testis and spermatozoa. The optimum pH for pyridoxal kinase is between 5.5 and 6.0. PDXK, the gene that encodes the pyridoxal kinase protein, maps to chromosome 21q22.3 and may be a candidate gene for autoimmune polyglandular disease type 1, a genetic disorder that has been mapped to the same region on chromosome 21.

Catalog Number: (10495-622)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (10671-510)

Supplier: Bioss

Description: Pyridoxal kinase belongs to the pyridoxine kinase family and phosphorylates vitamin B6, a step necessary for the conversion of vitamin B6 to pyridoxal 5’ phosphate (PLP), the active form of vitamin B6. PLP acts as a coenzyme and functions to maintain homeostasis. Pyridoxal kinase is a 312-amino acid cytoplasmic protein that may act as a homodimer and is expressed ubiquitously. There are three known isoforms of pyridoxal kinase, and isoform 3 expression is observed in adult testis and spermatozoa. The optimum pH for pyridoxal kinase is between 5.5 and 6.0. PDXK, the gene that encodes the pyridoxal kinase protein, maps to chromosome 21q22.3 and may be a candidate gene for autoimmune polyglandular disease type 1, a genetic disorder that has been mapped to the same region on chromosome 21.

Catalog Number: (10495-618)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (10495-624)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (10495-628)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (10495-620)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (10490-584)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (10490-586)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (10490-588)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (76110-770)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentiation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (76109-752)

Supplier: Bioss

Description: Pyridoxal kinase belongs to the pyridoxine kinase family and phosphorylates vitamin B6, a step necessary for the conversion of vitamin B6 to pyridoxal 5? phosphate (PLP), the active form of vitamin B6. PLP acts as a coenzyme and functions to maintain homeostasis. Pyridoxal kinase is a 312-amino acid cytoplasmic protein that may act as a homodimer and is expressed ubiquitously. There are three known isoforms of pyridoxal kinase, and isoform 3 expression is observed in adult testis and spermatozoa. The optimum pH for pyridoxal kinase is between 5.5 and 6.0. PDXK, the gene that encodes the pyridoxal kinase protein, maps to chromosome 21q22.3 and may be a candidate gene for autoimmune polyglandular disease type 1, a genetic disorder that has been mapped to the same region on chromosome 21.

Catalog Number: (76109-750)

Supplier: Bioss

Description: Pyridoxal kinase belongs to the pyridoxine kinase family and phosphorylates vitamin B6, a step necessary for the conversion of vitamin B6 to pyridoxal 5? phosphate (PLP), the active form of vitamin B6. PLP acts as a coenzyme and functions to maintain homeostasis. Pyridoxal kinase is a 312-amino acid cytoplasmic protein that may act as a homodimer and is expressed ubiquitously. There are three known isoforms of pyridoxal kinase, and isoform 3 expression is observed in adult testis and spermatozoa. The optimum pH for pyridoxal kinase is between 5.5 and 6.0. PDXK, the gene that encodes the pyridoxal kinase protein, maps to chromosome 21q22.3 and may be a candidate gene for autoimmune polyglandular disease type 1, a genetic disorder that has been mapped to the same region on chromosome 21.

Catalog Number: (10490-568)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (10495-606)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.

Catalog Number: (10490-582)

Supplier: Bioss

Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.