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N-6 Adenine-Specific DNA Methyltransferase 1, also known as N6AMT1 is part of the methyltransferase family. N6AMT1 is implicated in the methylation of release factor I during translation termination. In addition, N6AMT1 is involved in converting the arsenic metabolite monomethylarsonous acid to the less toxic dimethylarsonic acid.

Aldo-keto reductase family 1 member D1 (AKR1D1) belongs to the AKR superfamily. The AKR family proteins are soluble NADPH oxidoreductases, which have vital roles in the metabolism of drugs, carcinogens and reactive aldehydes. AKR1D1 is also responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones that carry a delta (4)-3-1 structure. AKR1D1 is highly expressed in the liver, colon and testis. Deficiency of the AKR1D1 enzyme may contribute to hepatic dysfunction.

Iduronate 2-Sulfatase also known as IDS, belongs to the highly-conserved sulfatase family of enzymes which catalyze the hydrolysis of O-sulfate and N-salfate esters from a variety of substrates. IDS is essential for the lysosomal degradation of the glycosaminoglycans (GAG) heparan sulfate as well as dermatan sulfate. Furthermore, IDS hydrolyzes the 2-sulfate group of the IDS units of the GAG.

Betaine-Homocysteine Methyltransferase 2 (BHMT2) is involved in the regulation of homocysteine metabolism. Homocysteine is a sulfur-containing amino acid which has a key role in methylation reactions. Transfer of the methyl group from betaine to homocysteine generates methionine, which donates the methyl group to methylate DNA, proteins, lipids, and other intracellular metabolites. BHMT2 is one of two methyl transferases which can catalyze the transfer of the methyl group from betaine to homocysteine. BHMT2 converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor. Homocysteine metabolism anomalies are implicated in disorders varying from vascular disease to neural tube birth defects such as spina bifida.

TOP1 is an important nuclear enzyme that interconverts supercoiled DNA to the necessary topological conformations for standard DNA replication and transcription. TOP1 is the target antigen for TOP1 autoantibodies. TOP1 antibodies are a specific marker in scleroderma patients (specificity 98-100%) and are related with the existence of diffuse skin involvement and pulmonary fibrosis. In human tissues top1 enzyme is primarily synthesized as a protein with a molecular weight of 100-kDa. Most of this precursor is then proteolytically processed to a 70-kDa size, from which the TOP1 antigen has derived its name.

Lipase Endothelial (LIPG) has extensive phospholipase activity and may be involved in lipoprotein metabolism and vascular biology. The LIPG protein is considered a member of the TG lipase family through its sequence and characteristic lid region which provides substrate specificity for enzymes of the TG lipase family. In addition, the LIPG has triglyceride lipase activities. LIPG hydrolyzes HDLs more efficiently than other lipoproteins. LIPG also binds heparin.

Deoxyribonuclease I Bovine (bDNase), an enzyme which selectively cleaves DNA. Bovine Dnase is an endonuclease enzyme which splits phosphodiester linkages within polynucleotides, acting primarely on single stranded DNA (ssDNA), double stranded DNA (ddDNA) and chromatin. Dnase is activated by bivalent metals such as Mg+2 and Ca+2 .
Dnase enzymes are common reagents used in biochemical methods requiring diestion of DNA and recovery of RNA, or where DNA is to be removed without affecting structural proteins or enzymes. Dnase enzymes are also used in tissue culture to digest DNA from damaged cells, resulting in reduced viscosity, and for removal of membrane-bound DNA fragments.

Aldo-keto reductase family 1 member C3 isoform 1 or AKR1C3 is an enzyme, part of the aldo-keto reductase family that promotes conversion of ketones & aldehydes to the alcohol forms while using cofactors such as NADPH & NADH. AKR1C3 promotes the reduction of PG molecule (prostaglandin), PQ (phenanthrenequinone) & PGH2. Another role is oxidation of 9 alpha, 11 beta-PGF2 to PGD2. AKR1C3 holds a crucial part in the pathogenesis of allergic diseases like asthma and can also take part in the regulation of cell growth and differentiation.

The three isoenzymes (MM, MB, and BB) are found in muscle, cardiac and brain tissues. These recombinant proteins are ideal for calibrating diagnostic instruments and researching neuromuscular diseases. Creatine Kinases can be used for indications in many neuromuscular applications. These disorders include cardiac disease, mitochondrial disorders, inflammatory myopathies, myasthenia, polymyositis, McArdle's disease, NMJ disorders, muscular dystrophy, ALS, hypo and hyperthyroid disorders, central core disease, acid maltase deficiency, myoglobinuria, rhabdomyolysis, motor neuron diseases, rheumatic diseases, and other that create elevated or reduced levels of Creatine Kinases.

Caspase 3 Apoptosis-Related Cysteine Peptidase (CASP3) belongs to the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a key role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to generate 2 subunits, large and small, that dimerize to create the active enzyme. CASP3 protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. CASP3 is the leading caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is linked with neuronal death in Alzheimer's disease. In addition, CASP3 is involved in the cleavage of huntingtin. CASP3 also cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. CASP3 initiates cell adhesion in sympathetic neurons through RET cleavage.

Argininosuccinate lyase (ASL) is a member of the lyase 1 family. ASL is an enzyme which catalyzes the reversible breakdown of Argininosuccinate (ASA) yielding the amino acids arginine and fumarate. ASL which is located in the liver cytosol is the 4th enzyme of the urea cycle and involved in the biosynthesis of arginine in all species and the production of urea in ureotelic species. While Argininosuccinate synthetase (ASS) catalyzes the formation of argininosuccinate from citrulline and aspartate, ASL breaks down the newly formed argininosuccinate into L-arginine and fumarate. L-arginine continues within the urea cycle to form urea and orinthine, whereas fumarate can enter the citric acid cycle. ASL gene Mutations result in the autosomal recessive disorder argininosuccinic aciduria, or argininosuccinic acid lyase deficiency.

Phosphoglucomutase-1 also known as PGM1 is a member of the phosphohexose mutase family. There are more than a few PGM isozymes, which catalyze the transfer of phosphate between the 1&6positions of glucose. In nearly all cell types, PGM1 isozymes predominate, representing around 90% of total PGM activity. It has been found that defects in PGM1 are the cause of glycogen storage disease type 14.

PRDX1 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX1 is an important protector of red blood cells against reactive oxygen species and in tumor prevention.
PRDX1 is antioxidant protective in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX1 has a proliferative effect and is involved in cancer development or progression.
Peroxiredoxin-1 is plays a role in redox regulation of the cell. Peroxiredoxin decreases peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. Peroxiredoxin is involved in eliminating peroxides generated during metabolism. Peroxiredoxin participates in the signaling cascades of growth factors and TNF-alpha by regulating the intracellular concentrations of h(2)o(2).

Protein modification with ubiquitin is an essential cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s) ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). Ubiquitin-Conjugating Enzyme E2G (UBE2G1) belongs to the E2 ubiquitin-conjugating enzyme family and catalyzes the covalent attachment of ubiquitin to other proteins. UE2G1 protein is involved in degradation of muscle-specific proteins.

Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.

Urokinase (UK) is a serine protease, which is one of biological plasminogen activators.
It is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing.
It can be obtained from human urine or kidney cell culture.

CKMT1A is in charge of the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. CKMT1A is a member of the creatine kinase isoenzyme family and exists as two isoenzymes, sarcomeric MtCK and ubiquitous MtCK, encoded by separate genes. Mitochondrial creatine kinase arises in two different oligomeric forms: dimers and octamers, unlike the exclusively dimeric cytosolic creatine kinase isoenzymes. Numerous malignant cancers with poor prognosis have displayed overexpression of ubiquitous mitochondrial creatine kinase which is linked to high energy turnover and inability to remove cancer cells through apoptosis.

DARS uses a 2 step reaction to catalyze the specific attachment of an amino acid to its cognate tRNA: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.

This gene is a member of the ADAR (adenosine deaminase acting on RNA) family. Using site-specific adenosine modification, proteins encoded by these genes participate in the pre-mRNA editing of nuclear transcripts. The protein encoded by this gene, tRNA-specific adenosine deaminase 1, is responsible for the deamination of adenosine 37 to inosine in eukaryotic tRNA.

Paraoxonase 2 (PON2) is a member of a multigene family whose genes share 65% identity at the amino acid level, and is expressed in a variety of tissues, including the pancreas. PON2 overexpression has been shown to lower the intracellular oxidative state and reduce the cells ability to oxidize LDL. PON2 is therefore implicated in the modulation of oxidative stress.

DNA polymerase beta (POLB) is a member of the DNA polymerase type-X family. In eukaryotic cells, POLB performs base excision repair necessary for DNA maintenance, replication, recombination, and drug resistance. POLB has 2 separate domains; the larger is the polymerase domain itself, whereas a small basic N-terminal domain contains an AP lyase activity which excises the abasic sugar-phosphate residue at the strand break. POLB fills single nucleotide gaps in DNA produced by the base excision repair pathway of mammalian cells. POLB overexpression, as seen in some human tumors, could convene an increase in spontaneous mutagenesis.

Prostatic Acid Phosphatase or ACPP is part of a family of proteins called histidine acid phosphatase. ACPP enhances the hydrolyzation of many phosphate monoesters and proteins that are phosphorylated. In order to function best, ACPP needs a range of range of 4-6 pH, furthermore, L(+)-tartrate inhibits ACPP’s catalyzation. This enzyme can act as a lipid phosphatase as well and can inhibit lysophosphatidic acid in seminal plasma.