Search results

MMP9 is part of the matrix metalloproteinase family. MMP enzymes take part in the dismantle of extracellular matrix in different physiological pathways, for instance wound healing, bone development, reproduction etc. the enzyme is also involved in pathological pathways: metastasis, arthritis and intracerebral hemorrhage.

Placental alkaline phosphatase also known as PLAP is a membranal siaglycoprotein enzyme typicallyfoundin high concentration in syncytiotrophoblasts in the placenta amid the 3th trimester of gestation. The expression of PLAP was at firstconsidered to be onlyin the term placenta, though, a human PLAP-like variant has been found,thathas more than 85% homology with PLAP itself. PLAP is expressed strictly in normal term placenta, endocervix & fallopian tube and in ovarian and proximal gastrointestinal tumors. It is also widely expressed in germ cell tumors and more recently found in seminomas.

Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.

Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.

Glycerol dehydrogenase (GldA) catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). The GldA protein allows microorganisms to use glycerol as a source of carbon under anaerobic conditions. Furthermore, in E.coli GldA has an imperative role by regulating the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. GldA possesses an extensive substrate specificity, due to its ability to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively.

MAT2A is an important enzyme in cellular metabolism and catalyzes the formation of S-adenosylmethionine (SAMe) from L-methionine and ATP. MAT2A is expressed in extrahepatic tissues. In liver, MAT2A expression associates with growth, dedifferentiation, and cancer. NF-kappa B and AP-1 are necessary for basal MAT2A expression in HepG2 cells and mediate the increase in MAT2A expression in response to TNF-alpha. Up-regulation of MAT2A provides growth improvement and s-adenosylmethionine and methylthioadenosine thus can block mitogenic signaling in colon cancer cells. Lower expression of both MAT2A and MAT2beta and interfere with leptin signaling in liver cancer cells.

APEX1 is in charge of the incision of DNA basic sites during base excision repair. APEX1 also stimulates the DNA binding activity of numerous transcription factors which take part in cancer promotion and progression. APEX1 is part of the cellular response to oxidative stress and protects cells from the genotoxic and cytotoxic effect of oxidizing agents.

Formylglutathione hydrolase (Esterase D) is a member of the esterase D family. Esterase D is a serine hydrolase involved in the detoxification of formaldehyde. Esterase D is active toward various substrates including O-acetylated sialic acids, and it may possibly be involved in the recycling of sialic acids. Esterase D is used as a genetic marker for retinoblastoma and Wilson's disease.

Ubiquitin-conjugating enzyme E2S (UBE2S) belongs to the ubiquitin-conjugating enzyme family. UBE2S is able to form a thiol ester linkage with ubiquitin in a ubiquitin activating enzyme-dependent manner, a typical property of ubiquitin carrier proteins. UBE2S catalyzes the covalent attachment of ubiquitin to other proteins. UBE2S acts as a crucial factor of the anaphase promoting complex/cyclosome (APC/C), which is a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. UBE2S acts by purposely elongating ''Lys-11''-linked polyubiquitin chains initiated by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, augmenting the degradation of APC/C substrates by the proteasome and promoting mitotic exit. UBE2S also acts by elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in vitro; it is nevertheless uncertain whether UBE2D1/UBCH5 acts as an E2 enzyme for the APC/C in vivo. UBE2S is also involved in ubiquitination and consequent degradation of VHL, resu

Dengue fever is affected by 1 of 4 closely linked virus serotypes of the genus Flavivirus, family Flaviviridae. One might have dengue fever infected by the different serotype virus after the primary infection. Detection of particular antibodies to dengue viruses is used for the diagnosis in clinic. Recently, lateral flow rapid test products have become a most suitable and known method in the clinical diagnosis. Though, there is difficulty for manufacturers to have the dengue antigens with a whole coverage for Dengue IgG & IgM recognition for all 4 serotype infections as well as with colloid gold binding ability. 8 dengue antigens have been established for the lateral flow products which are well defined for their coverage of dengue IgG & IgM recognition. The researcher can select the products below based on their own specific application.

Short/branched chain specific acyl-CoA dehydrogenase (ACADSB) belongs to the acyl-CoA dehydrogenase family of enzymes which catalyze the dehydrogenation of acyl-CoA derivatives in the metabolism of fatty acids or branch chained amino acids. ACADSB catalyzes the degradation of L-isoleucine while having the highest affinity for (s)-2-methylbutyryl-CoA, isobutyryl-CoA and 2-methylhexanoyl-CoA as substrates. ACADSB may use valproyl-CoA as substrate. ACADSB gene defects cause the short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD), which is an autosomal recessive disorder characterized by an increase of 2-methylbutyrylglycine and 2-methylbutyrylcarnitine in blood and urine.

Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form.
Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collagens, acting preferentially on collagen type I.
Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes.

Glutamine--Fructose-6-Phosphate Transaminase 1 (GFPT1) participates in the hexosamine pathway and controls the glucose fluidity into the hexosamine pathway. GFPT1 regulates the availability of precursors for N- and O-linked glycosylation of proteins. GFPT1 controls the circadian expression of clock genes ARNTL/BMAL1 and CRY1.

Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

EYA2 belongs to tyrosine phosphatase family which specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). EYA2 promotes effective DNA mending by dephosphorylating H2AX, promoting the enlistment of DNA repair complexes having MDC1. EYA2 role as histone phosphatase can explain its part in transcription regulation during organogenesis.

Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso- PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.

PRDX5 belongs to the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides with reducing equivalents supplied through the thioredoxin system. PRDX5 has an antioxidant protective function in different tissues under normal conditions and during inflammatory processes. Peroxiredoxin-5 interacts with peroxisome receptor 1 and is involved in intracellular redox signaling. PRDX5 is involved in intracellular redox signaling. Peroxiredoxin-5 is a significant antioxidant protein of lung epithelial cells for its expression in the human lung increases during inflammation. PRDX5 expression is upregulated in osteoarthritis. PRDX5 may be significant in mitochondrial genome stability. Peroxiredoxin-5 has a protective role in human tendon cells against oxidative stress by reducing apoptosis and upholding collagen synthesis.

Methionine aminopeptidase 1 (METAP1) is a member of the peptidase M24A family. METAP1 removes the amino-terminal methionine from nascent proteins. METAP1 releases N-terminal amino acids, preferentially methionine, from peptides and arylamides. METAP1 is essential for normal progression through the cell cycle. The active site of METAP1 contains 2 adjacent divalent metal ions linked by a water molecule or hydroxide ion.

CYP2E1, also known as Cytochrome P450 2E1 belongs to the cytochrome P450 mixed-function oxidase system which is involved in the metabolism of xenobiotics in the body. While CYP2E1 is implicated in the oxidative metabolism of small range substrates, commonly small polar molecules, there are many significant drug interactions which are mediated by CYP2E1.

NADH Dehydrogenase Fe-S Protein 6 (NDUFS6) is a subunit of the NADH: ubiquinone oxidoreductase (complex I), which is the 1st enzyme complex in the electron transport chain of the mitochondria. This complex operates in the transfer of electrons from NADH to the respiratory chain. NDUFS6 is one of seven subunits in the iron-sulfur protein segment. DNA alterations in NDUFS6 are the cause for mitochondrial complex I deficiency, a disease which results in an extensive assortment of clinical disorders, like adult-onset neurodegenerative disorders and neonatal disease.

Eukaryotic translation initiation factor 3, subunit I (EIF3I) is part of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is essential for numerous steps in the initiation of protein synthesis. The eIF-3 complex links with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2: GTP: methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also essential for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3I are clonorchiasis, and tonsillitis.

NUDT10 belongs to the Nudix hydrolase family of pyrophosphatases. Nudix hydrolases contain a characteristic Nudix domain and are responsible for catalyzing the hydrolysis of nucleoside diphosphate derivatives. NUDT10 functions as a manganese-dependent polyphosphate phosphohydrolase with an optimum pH of 8.5. NUDT10 protein specifically metabolizes diadendosine-polyphosphates and, to a lesser extent, diphosphoinositol polyphosphates.

NUDT5 is part of the nudix hydrolase family which remove toxic nucleotide derivatives from the cell. NUDT5 hydrolyzes ADP-ribose and ADP-mannose in the presence of magnesium, and in addition hydrolyzes nucleotide sugars with decreasing activity such as ADP-glucose and diadenosine diphosphate. As a nudix hydrolase, NUDT5 holds a central nudix motif and functions to eliminate toxic nucleotide metabolites from the cell while maintaining the levels of signaling nucleotides.
NUDT5 is broadly expressed but is most abundant in liver as a homodimer.

GMP synthase (GMPS) is involved in purine biosynthesis. GMPS, which is a homodimer, catalyzes the last step in the GMP synthesis pathway, specifically the ATP-dependent amination of XMP to GMP. GMPS is comprised of one GMP-binding domain and one glutamine amidotransferase type-1 domain through which it communicates its catalytic activity. GMPS is engaged in the de novo synthesis of nucleotides which are not only vital for DNA and RNA synthesis, but also supply GTP, which is involved in sevral cellular processes important for cell division. GMPS gene chromosomal translocations are linked with acute myeloid leukemias, suggesting a possible role for GMPS in carcinogenesis.