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Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.

Erythrocyte acylphosphatase (ACYP1) is a cytosolic enzyme which catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates. There are two acylphophatase isoenzymes: ACYP1 and ACYP2. These isoenzymes share 60% homology and have the same substrate specificity, even though ACYP1 has a higher catalytic activity than ACYP2.

Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.

IMPA2 is a member of the inositol monophosphatase family. IMPA2 catalyzes the dephosphoylration of inositol monophosphate and has a significant role in phosphatidylinositol signaling. IMPA2 can use the myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. IMPA2 is a pharmacological target for lithium Li(+) action in brain. IMPA2 is considered to have a role in schizophrenia and bipolar disorder.

Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.

Serine/threonine/tyrosine-interacting protein (STYX) is a member of the protein-tyrosine phosphatase family. STYX contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which makes it catalytically inactive as a phosphatase. On the other hand, the binding pocket is adequately preserved to bind phosphorylated substrates, and may protect them from phosphatases. STYX may have a role in spermiogenesis. STYX is a possible pseudophosphatase.

Deoxyuridine Triphosphatase (DUT) is a ubiquitous enzyme that functions in nucleotide metabolism. Deoxyuridine Triphosphatase, in the presence of magnesium ions, is responsible for hydrolyzing dUTP to dUMP and diphosphate. This reaction is imperative for keeping the intracellular dUTP concentration low so that uracil does not become incorporated into DNA. Extensive integration of uracil into DNA can eventually lead to cell death. This suggests that DUT is crucial for cell viability, further implying that it is a prospective target for anticancer therapy.

Protein Phosphatase 1F (PPM1F) is a part of the PP2C family of Ser/Thr protein phosphatases whose members are known to be negative regulators of cell stress response pathways. PPM1F interacts with Rho guanine nucleotide exchange factors (PIX), and as a result blocks the effects of p21-activated kinase 1 (PAK), a protein kinase mediating biological effects downstream of Rho GTPases. Calcium/calmodulin-dependent protein kinase II gamma (CAMK2G/CAMK-II) is one of the substrates of PPM1F. PPM1F is found to be an apoptosis Promoter.

Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as theimmunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which areinvolved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. SIRPA can bephosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part insignal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand forSIRPA.

Inositol monophosphatase 3 (IMPAD1) belongs to the inositol monophosphatase family. IMPAD1 is restricted to the Golgi apparatus and catalyzes the hydrolysis of phosphoadenosine phosphate (PAP) to adenosine monophosphate (AMP). IMPAD1 gene mutations cause the GRAPP type chondrodysplasia with joint dislocations, and a pseudogene of the IMPAD1 gene is located on the long arm of chromosome 1.

Tyrosyl-DNA phosphodiesterase 1 ( TDP1) is required for repairing stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis of the phosphodiester bond between the tyrosine residue of topoisomerase I and the 3-prime phosphate of DNA. TDP1 also detach glycolate from single-stranded DNA having 3-prime phosphoglycolate, suggesting a role in repair of free-radical mediated DNA double-strand breaks.

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.

RNA Guanylyltransferase And 5'-Phosphatase also known as RNGTT is a bifunctional mRNA-capping enzyme which exhibits RNA 5'-triphosphatase activity in the N-terminal section and mRNA guanylyltransferase activity in the C-terminal section. In addition, RNGTT catalyzes the first two steps of cap formation, through removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and also by transferring the gmp moiety of GTP to the 5'-diphosphate terminus.

THTPA enzyme is part of the THTPase family. THTPA is localized to the cytoplasm and expressed at small quantities in a variety of tissues, including testis, uterus, prostate, bladder, lung and kidney. THTPA is a hydrolase that catalyzes the H2O-dependent hydrolysis of thiamine triphosphate (THTP) to thiamine diphosphate (THDP), the main form of thiamine within the cell. THTPA occurs as a monomer and is activated at an optimal pH of 8.5.

Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as the immunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which are involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes.
SIRPA can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part in signal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA.

GDP-fucose protein O-fucosyltransferase 1 (POUFUT1), belongs to the glycosyltransferase O-Fuc family. POUFUT1 encodes a member of the glycosyltransferase O-Fuc family and Expressed mainly in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle.POUFUT1 adds O-fucose through an O-glycosidic linkage to Preserve serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and emitted proteins. POUFUT1 is involved in ligand-induced receptor signaling. Alternative splicing of this gene results in 2 transcript variants encoding different isoforms.POFUT1 participates in Notch signaling, as Notch ligands can use as POFUT1 substrates.

Phosphoribosyltransferase domain-containing protein 1 (PRTFDC1) is a member of the purine/pyrimidine phosphoribosyltransferase family. PRTFDC1 has a low, barely measurable phosphoribosyltransferase activity (in vitro). PRTFDC1 can bind GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). PRTFDC1 is not expected to impact purine metabolism or GMP salvage.

Proline-Serine-Threonine Phosphatase Interacting Protein 1 (PSTPIP1) which is a scaffold protein and a regulator of the actin cytoskeleton binds ABL1, PTPN18, WAS, CD2AP, and PTPN12. PSTPIP1 also binds to the cytoplasmic tail of CD2, an effector of T cell activation and adhesion, negatively affecting CD2-triggered T cell activation. Mutations in PSTPIP1 are a cause of PAPA syndrome.

PINK1 is a serine/threonine protein kinase which is found in the mitochondria. PINK1 shields cells from stress-induced mitochondrial dysfunction. Mutations results in one form of autosomal recessive early-onset Parkinson disease.

PPP3CA (aka Calcineurin A) is a major soluble calmodulin binding protein in the brain and a Ca2+/calmodulin dependent serine/threonine protein phosphatase, with a relatively limited substrate specificity. PPP3CA activates the T cells of the immune system and can be blocked by drugs. PPP3CA activates NFATc (a transcription factor) by dephosphorylating it. The activated NFATc is subsequently translocated into the nucleus, where it upregulates the expression of interleukin 2.

CPPED1 which is a part of the metallophosphoesterase superfamily takes part in glucose uptake by adipocytes. CPPED1 binds two divalent metal cations and is transactivated by the great envelope protein of the hepatitis B virus.

Metallophosphoesterase domain containing 2 (MPPED2) is a member of the UPF0046 family. MPPED2 displays low metallophosphoesterase activity, in vitro. In addition, MPPED2 encodes a metallophosphoesterase. MPPED2 may take part in the development of the nervous system, brain development. Among the diseases associated with MPPED2 are wagr syndrome, and aniridia.