"4-Nitrophenyl+phosphate"

Supplier: BACHEM BIOCHEMICA

Substrate for trypsin, papain, acrosin, plasmin, cathepsin B, and cathepsin H.

Supplier: ProSci Inc.

ATP2B3 gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. ATP2B3 is the plasma membrane calcium ATPase isoform 3.The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. This gene encodes the plasma membrane calcium ATPase isoform 3. Alternatively spliced transcript variants encoding different isoforms have been identified.

Supplier: ProSci Inc.

ATP2B3 gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. ATP2B3 is the plasma membrane calcium ATPase isoform 3.The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. This gene encodes the plasma membrane calcium ATPase isoform 3. Alternatively spliced transcript variants encoding different isoforms have been identified.

Supplier: Boster Bio

Fatty aldehyde dehydrogenase (or Long-chain-aldehyde dehydrogenase) is an aldehyde dehydrogenase enzyme that in human is encoded in the ALDH3A2 gene on chromosome 17. ALDH3A2 catalyzes the oxidation of long-chain aliphatic aldehydes into fatty acids. It is known to act on a variety of both saturated and unsaturated aliphatic aldehydes between 6 to 24 carbons in length, as well as dihydrophytal, a 20-carbon branched chain aldehyde. It requires NAD+ as a co-factor. The encoded enzyme is responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid. ALD3H2 is expressed in the human liver and has been found to localize the microsome fraction inside the cell.

Supplier: ProSci Inc.

ATP2B4 belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. ATP2B4 is the plasma membrane calcium ATPase isoform 4.The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. This gene encodes the plasma membrane calcium ATPase isoform 4. Alternatively spliced transcript variants encoding different isoforms have been identified.

Supplier: Abcam

Nucleotide involved in the reactions of cellular energy transfers. Acts as an activator of AMP-activated protein kinase (AMPK). Used as a substrate for enzymes such as AMP-thymidine kinase, AMP deaminase and 5'-nucleotidase.

Supplier: Bioss

The GGA family of proteins (Golgi-localized, g-Adaptin ear-containing, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin. Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multi-domain proteins that bind mannose 6-phosphate receptors (MPRs). GGAs have modular structures with an N-terminal VHS (VPS27, Hrs and STAM) domain followed by a GAT (GGA and Tom1) domain, a connecting hinge segment and a C-terminal GAE (g-Adaptin ear) domain. The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences. The human GGA3 gene maps to chromosome 17 and encodes a 723 amino acid protein that shares 46% sequence identity with GGA1 and 38% with GGA2.

Supplier: Bioss

Cytokeratins are proteins of keratin-containing intermediate filaments found in the intracytoplasmic cytoskeleton of epithelial tissue. The cytokeratins are encoded by a family encompassing 30 genes. Among them, 20 are epithelial genes and the remaining 10 are specific for trichocytes.
In the cytoplasm, the keratin filaments conform a complex network which extends from the surface of the nucleus to the cell membrane. Numerous accessory proteins are involved in the genesis and maintenance of such structure. This association between the plasma membrane and the nuclear surface provides important implications for the organization of the cytoplasm and cellular communication mechanisms. Apart from the relatively static functions provided in terms of supporting the nucleus and providing tensile strength to the cell, the cytokeratin networks undergo rapid phosphate exchanges mediated depolymerization, with important implications in the more dynamic cellular processes such as mitosis and post-mitotic period, cell movement and differentiation. Cytokeratins interact with desmosomes and hemidesmosomes, thus collaborating to cell-cell adhesion and basal cell-underlying connective tissue connection.

Supplier: Bioss

The tRNA-splicing endonuclease complex is responsible for identifying and cleaving pre-tRNA at both 5’ and 3’ splice sites, thereby releasing introns and free tRNA molecules with 2',3' cyclic phosphates and 5'-OH termini. In addition to its role in pre-tRNA splicing, the heterotetrameric endonuclease complex participates in mRNA processing and, via its association with pre-mRNA processing factors, is thought to link pre-tRNA and pre-mRNA splicing events. TSEN2 (tRNA-splicing endonuclease subunit Sen2), also known as tRNA-intron endonuclease Sen2, is a 465 amino acid nuclear protein that constitutes one of the two catalytic subunits of the tRNA-splicing endonuclease complex. There are three isoforms of TSEN2 that are produced as a result of alternative splicing events. Isoform 1 seems to carry the active site for 5’-splice site cleavage. Defects in the gene encoding TSEN2 are the cause of pontocerebellar hypoplasia type 2B, which is characterized by progressive microencephaly with epilepsy, extrapyramidal dyskinesia and chorea without spinal cord findings.

Supplier: Bioss

The tRNA-splicing endonuclease complex is responsible for identifying and cleaving pre-tRNA at both 5and 3 splice sites, thereby releasing introns and free tRNA molecules with 2',3' cyclic phosphates and 5'-OH termini. In addition to its role in pre-tRNA splicing, the heterotetrameric endonuclease complex participates in mRNA processing and, via its association with pre-mRNA processing factors, is thought to link pre-tRNA and pre-mRNA splicing events. TSEN2 (tRNA-splicing endonuclease subunit Sen2), also known as tRNA-intron endonuclease Sen2, is a 465 amino acid nuclear protein that constitutes one of the two catalytic subunits of the tRNA-splicing endonuclease complex. There are three isoforms of TSEN2 that are produced as a result of alternative splicing events. Isoform 1 seems to carry the active site for 5-splice site cleavage. Defects in the gene encoding TSEN2 are the cause of pontocerebellar hypoplasia type 2B, which is characterised by progressive microencephaly with epilepsy, extrapyramidal dyskinesia and chorea without spinal cord findings.

Supplier: USP

USP Reference Standards are specified for use in conducting official USP–NF tests and assays. USP also provides Reference Standards specified in the Food Chemicals Codex as well as authentic substances—high-quality chemical samples—as a service to analytical, clinical, pharmaceutical and research laboratories. To confirm accuracy and reproducibility, USP Reference Standards are rigorously tested and evaluated by multiple independent laboratories including USP, commercial, regulatory, and academic labs. USP also provide publicly available, official documentary standards for pharmaceutical ingredients in the USP–NF that link directly with our primary reference standards.

Supplier: Bioss

The tRNA-splicing endonuclease complex is responsible for identifying and cleaving pre-tRNA at both 5’ and 3’ splice sites, thereby releasing introns and free tRNA molecules with 2',3' cyclic phosphates and 5'-OH termini. In addition to its role in pre-tRNA splicing, the heterotetrameric endonuclease complex participates in mRNA processing and, via its association with pre-mRNA processing factors, is thought to link pre-tRNA and pre-mRNA splicing events. TSEN2 (tRNA-splicing endonuclease subunit Sen2), also known as tRNA-intron endonuclease Sen2, is a 465 amino acid nuclear protein that constitutes one of the two catalytic subunits of the tRNA-splicing endonuclease complex. There are three isoforms of TSEN2 that are produced as a result of alternative splicing events. Isoform 1 seems to carry the active site for 5’-splice site cleavage. Defects in the gene encoding TSEN2 are the cause of pontocerebellar hypoplasia type 2B, which is characterized by progressive microencephaly with epilepsy, extrapyramidal dyskinesia and chorea without spinal cord findings.

Supplier: Bioss

Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.

Supplier: Bioss

Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognised as specific for DNA; it was the first DNase to be crystallised; and it was the first DNase for which a specific protein inhibitor was characterised. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesised in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.

Supplier: Bioss

The GGA family of proteins (Golgi-localized, g-Adaptin ear-containing, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin. Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multi-domain proteins that bind mannose 6-phosphate receptors (MPRs). GGAs have modular structures with an N-terminal VHS (VPS27, Hrs and STAM) domain followed by a GAT (GGA and Tom1) domain, a connecting hinge segment and a C-terminal GAE (g-Adaptin ear) domain. The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences. The human GGA3 gene maps to chromosome 17 and encodes a 723 amino acid protein that shares 46% sequence identity with GGA1 and 38% with GGA2.

Supplier: Bioss

Deoxyribonuclease I gene is approximately 3.2 kb long with 9 exons separated by 8 introns. In the form of a bovine pancreatic enzyme preparation, it occupies an important place in the history of protein chemistry and enzymology: it was the first enzyme to be recognized as specific for DNA; it was the first DNase to be crystallized; and it was the first DNase for which a specific protein inhibitor was characterized. DNase I is a Ca2+ and Mg2+ dependant endonuclease. DNase I is synthesized in the pancreas and stored in zymogen granules. It has been used to reduce the viscosity of cystic fibrosis sputum. A DNase I-like enzyme appears to catalyze the degradation of chromatin to oligo- and mononucleosomes during apoptosis. A recent study has demonstrated an endonuclease with activity and antigenicity indistinguishable from DNase I in thymocytes, cells susceptible to apoptosis. DNase I is an endonuclease that hydrolyzes double-stranded or single stranded DNA preferentially at sites adjacent to pyrimidine nucleotides. The product of hydrolysis is a complex mixture of 5'-phosphate mononucleotides and oligonucleotides. In the presence of Mg ion, DNase I attacks each strand of DNA independently and the cleavage sites are random.