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DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.

The recombinant Protein A/G is a genetically engineered protein comprised of 7 IgG-binding domains EDABC-C1C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

Acyl-coenzyme A thioesterase 13 (ACOT13) belongs to the thioesterase subfamily of esterase family. ACOT13 is highly expressed in the kidney with moderate expression in the brain, liver and intestines. ACOT13 contains a hotdog-fold and is thought to co-localize with microtubules, possibly having a role in cellular proliferation events. Deletion of a segment of the q arm of chromosome 6 is linked to early onset intestinal cancer, suggesting the presence of a cancer susceptibility locus.

NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.

COMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to catechol substrates such as the neurotransmitters. This O-methylation results in one of the main degradative pathways of the catecholamine transmitters. COMT COMT is located in the postsynaptic neuron and is involved in the metabolism of catechol estrogen drugs used in the treatment of hypertension, asthma, Parkinson disease and the inactivation of catecholamine neurotransmitters though enzymatic degradation. COMT appears in tissues in 2 forms, a soluble form and a membrane-bound form which differ in their N-termini. COMT inhibitors increase its availability and are used in the treatment of patients with Parkinson's disease.

FARSB, also known as Phenylalanyl-TRNA Synthetase Beta is a member of the phenylalanyl-tRNA synthetase beta subunit family. FARSB is composed tetramer of two alpha and two beta subunits. In the presence of ATP, this tetramer is accountable for attaching L-phenylalanine to the terminal adenosine of the appropriate tRNA.

APRT is part of the purine/pyrimidine phosphoribosyltransferase family. APRT enzyme catalyzes the formation of AMP and inorganic pyrophosphate from adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP). APRT produces adenine as a by-product of the polyamine biosynthesis pathway. A homozygous deficiency in APRT causes 2,8-dihydroxyadenine urolithiasis. APRT catalyzes a salvage reaction resulting in the formation of AMP.

Uridine 5'-monophosphate synthase (UMPS), is a bifunctional enzyme that catalyzes the ultimate two steps of the de novo pyrimidine biosynthetic pathway. UMPS in eukaryotes links the orotate phosphoribosyltransferase and the orotidine-5’-monophosphate (OMP) decarboxylase activities into a single protein. The harmony of these 2 enzymes is assumed to be stabilized the catalytic centers as a result of the low molar concentration of the protein in mammalian cells.mutations in this gene are the reason of inherited orotic aciduria disease.

PHOSPHO1 is involved in mineralization process & plays a role in bone and cartilage matrix mineralization.
PHOSPHO1 is expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix.
Orphan-1 is collagen type -2 is specific for cartilaginous tissues. Orphan1 is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
Phosphoethanolamine (2-O3POCH2CH2NH3) is a key intermediate in the formation of cephalins, it is formed in liver and brain by phosphorylation of ethanolamine.
PHOSPHO2 and PHOSPHO1 suggest subtle differences in the charge distributions around the putative substrate entry site and in the location of potential H-bond donors.
PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. PHOSPHO1 has been implicated in the generation of Pi for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho).

Histidyl-tRNA synthetase (HARS) functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids. HARS is a member of the class II family of aminoacyl-tRNA synthetases. HARS is responsible for the synthesis of histidyl-transfer RNA, which is vital for the incorporation of histidine into proteins. HARS is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.

Carbonic anhydrase 1 is a zinc metalloenzyme that catalyses reversible hydration of CO2 (CO2 + H2O ? HCO3- + H+). Carbonic anhydrase 1 is essential to many biological processes such as cellular respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, salvia, and gastric acid. Carbonic anhydrase 1 is abundant in erythrocytes and an early marker for erythroid differentiation.

DNA toposisomerase I is a key nuclear enzyme that interconverts supercoiled DNA to the required topological conformations for normal DNA replication and transcription. This enzyme is the target antigen for the so-called Scl-70 autoantibodies. Scl-70 antibodies are a specific marker in Scleroderma patients (specificity 98-100%) and are associated with the presence of diffuse skin involvement and pulmonary fibrosis.
In human tissues the DNA topoisomerase I is initially synthesized as a protein with 100 kDa molecular weight. Most of this precursor is then proteolytically processed to a species with 70 kDa molecular weight from which the Scl-70 antigen has derived its name.

BPNT1 belongs to the magnesium-dependent, lithium-sensitive phosphomono-esterase superfamily. BPNT1 catalyzes the conversion of PAPS (adenosine 3'-phosphate 5' phosphosulfate) to APS (adenosine 5'-phosphosulfate) and the conversion of PAP (3'(2')-phosphoadenosine 5' phosphate) to AMP (adenosine 5'-phosphate) using magnesium as a cofactor. BPNT1 is expressed everywhere but at maximum levels in brain and kidney. BPNT1 is potently inhibited by lithium, a drug used for the treatment of manic depression and bipolar affective disorder, which suggests that BPNT1 has a possible role in the etiology of mood disorders.

AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.

L-lactate dehydrogenase (lldD) is present in a various organisms, including plants and animals. lldD is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concurrent interconversion of NADH and NAD+. Seeing that lldD can catalyze the oxidation of hydroxybutyrate, it is occasionally called Hydroxybutyrate Dehydrogenase (HBD).

Beta-secretase 1 or BACE1 or beta-site amyloid precursor protein cleaving enzyme 1, is a protein that is encoded by the BACE1 gene in humans. Expression of BACE1 is seen primarily in neurons as it is crucial for the creation of myelin sheats in the peripheric nervous system. Beta-secretase 1 is a proteas that is located in the cell membrane (transmembrane). The enzyme consists of 2 active sites (aspartate residues) in the extracellular domain that can act as a dimer.

Glutamate-cysteine ligase (GCLM) is the first rate limiting enzyme of glutathione synthesis. The GCLM enzyme is comprised of 2 subunits, a heavy catalytic subunit and a light regulatory subunit. GCLM deficiency is associated with some forms of hemolytic anemia.

Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.

GSTK1 is involved in cellular detoxification. GSTK1 is localized to the peroxisome and catalyzes the conjugation of the thiol group of glutathione (GSH) to the electrophilic groups of a broad range of hydrophobic substrates, leading to an easier removal of the latter from the cells.

Myristate, a rare 14-carbon saturated fatty acid, is co-translationally attached by an amide linkage to the N-terminal glycine residue of cellular & viral proteins with various functions. N-Myristoyltransferase 1, also known as NMT1 catalyzes the transfer of myristate from CoA to proteins. NMT1 seems to be irreversible and is essential for full expression of the biologic activities of several N-myristoylated proteins, as well as the alpha subunit of the signal-transducing guanine nucleotide-binding protein, G protein.

Phosphopantothenate-cysteine ligase (PPCS) catalyzes the first step in the biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5), which is a vital universal pathway in prokaryotes and eukaryotes. PPCS, being one of the last enzymes in this pathway, converts phosphopantothenate to phosphopantothenoylcysteine.

Flavokinase is a transferases family member, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. Flavokinase is an enzyme that catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), which is an obligatory step in vitamin B2 utilization and flavin cofactor synthesis. It has been proposed that TNF, through the activation of the RFK gene, enhances the incorporation of FAD in NADPH oxidase enzymes, which is a critical step for the assembly and activation of NADPH oxidase.

Glutamate Decarboxylase 1 (GAD1) is one of several forms of glutamic acid decarboxylase. GAD1 is responsible for catalyzing the production of gamma-aminobutyric acid from L-glutamic acid. A pathogenic role for the GAD1 enzyme has been identified in the human pancreas since it has been detected as an autoantigen and an autoreactive T cell target type II diabetes. The GAD1 protein may also have a role in the stiff man syndrome. GAD1 enzyme deficiency leads to pyridoxine dependency with seizures. GAD1 also catalyzes the production of GABA.