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Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
Placental Lactogen Goat is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

Threonyl-tRNA Synthetase is a member of the aminoacyl-tRNA synthetase family, key enzymes of protein biosynthesis which charge tRNA molecules with the respective amino acids. This 83 kDa protein is an autoantigen recognized by PL-7 antibodies which occur in a subset of patients with polymyositis and dermatomyositis. Preliminary data suggest that PL-7 antibodies (similar to Jo-1 antibodies) indicate an increased risk for lung involvement, but this needs to be confirmed for a larger number of cases.

Hemoglobin Subunit Zeta (Hbz) or Hba-x is a alpha-like hemoglobin and part of the globin family. The protein is expressed and produced in the the yolk sac in early stages of embryonic development. Hemoglobin subunit zeta has 2 pseudogenes and 5 functional genes.

SHMT1 is a member of the SHMT family. SHMT1 is the cellular form of serine hydroxymethyltransferase, a pyridoxal phosphate-containing enzyme which catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and 5 10-methylene tetrahydrofolate. In addition, SHMT1 specifically provides one-carbon units for thymidylate biosynthesis, reduces methylenetetrahydrofolate pools for S-adenosylmethionine (SAM) synthesis by synthesizing serine, sequesters 5-methyltetrahydrofolate and inhibits SAM synthesis.

Spermine synthase (SMS) is amember of the spermidine/spermine synthase family. SMS is an enzyme which converts spermidine into spermine. The SMS enzyme is essential for normal viability, growth and fertility involved in polyamine metabolism. Defects in the SMS gene are the cause of Snyder-Robinson syndrome (SRS), also known as X-linked mental retardation Snyder-Robinson type. SRS is categorized by moderate intellectual deficit, hypotonia, an unsteady gait, osteoporosis, kyphoscoliosis and facial asymmetry, its transmission is X-linked recessive.

Aspartoacylase 3 (ACY3) belongs to the Aspartoacylase subfamily. ACY3 has a vital role in deacetylating mercapturic acids in kidney proximal tubules. Aspartoacylase 3 localizes to the cytoplasm of S2 and S3 proximal tubules and also to the apical domain of S1 proximal tubules. In addition, ACY3 protein is expressed at low levels in the stomach, testis, heart, brain, lung and liver, and can function as an HCV (Hepatitis C virus) core binding protein.

ACADS is a tetrameric mitochondrial flavoprotein, which is part of the acyl-CoA dehydrogenase family. ACADS catalyzes the first step of the mitochondrial fatty acid beta-oxidation pathway. Mutations in ACADS have been associated with Short Chain Acyl-CoA Dehydrogenase Deficiency.

Fucosyltransferase 3 (FUT3) catalyzes alpha-1, 3 and alpha-1, 4 glycosidic linkages which take part in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. FUT3 takes part in blood group Lewis determination; Lewis-positive (Le+) individuals have an active enzyme while Lewis-negative (Le-) individuals have an inactive enzyme. FUT3 also operates on the corresponding 1, 4-galactosyl derivative, creating1, 3-L-fucosyl links.

Tyrosyl-tRNA synthetase (YARS) is a member of the class I tRNA synthetase family. YARS is a vital enzyme which catalyzes the aminoacylation of tRNATrp with tryptophan, a critical function of the cell’s protein synthesis machinery. Expression of YARS is highly stimulated in human cells by the addition of IFN-gamma.

UROD is the fifth enzyme in the human heme biosynthetic pathway and is in charge for the transfer of uroporphyrinogen to coproporphyrinogen through the deletion of four carboxymethyl side chains. UROD Mutations and deficiency result in 3 autosomal disorders in humans: familial porphyria cutanea tarda (f-PCT), sporadic porphyria cutanea tarda (s-PCT) and hepatoerythropoietic porphyria (HEP).

QDPR belongs to the short-chain dehydrogenases/reductase (SDR) family of enzymes. Operating as a homodimer, QDPR has an imperative role in the recycling of tetrahydrobiopterin (BH4), a vital cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine). More precisely, QDPR catalyzes the regeneration of BH4 from quinonoid dihydrobiopterin (qBH2), the product generated from the hydroxylation reactions. Mutations in the QDPR gene may lead to phenylketonuria II.

Alcohol dehydrogenase 6 (ADH6) belongs to the alcohol dehydrogenase family. Alcohol dehydrogenase family members metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH6 is expressed in the stomach as well as in the liver, and it contains a glucocorticoid response element upstream of its 5’ UTR, which is a steroid hormone receptor binding site.

Alanyl-tRNA synthetase is a member of the aminoacyl-tRNA synthetase family, key enzymes of protein biosynthesis which charge tRNA molecules with the respective amino acids. This 108 kDa protein is an autoantigen recognized by PL-12 antibodies which occur in a subset of patients with polymyositis and dermatomyositis. Preliminary data suggest that epitope spreading occurs in the autoimmune PL-12 response such that even antibodies to an isolated alanyl-tRNA molecule can develop.

MGLL is a membrane-associated member of the serine hydrolase superfamily. MGLL is expressed in abundance in skeletal muscle and adipose tissue. MGLL functions jointly with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.

GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

IVD is a mitochondrial matrix enzyme that is part of the cyl-CoA dehydrogenase family which catalyzes the third step in leucine catabolism. The genetic deficiency of IVD leads to a buildup of isovaleric acid, which is toxic to the central nervous system and results in isovaleric acidemia. IVD is a homotetrameric flavoenzyme which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA.

GSTZ1 is part of the glutathione S-transferase super-family which encodes multifunctional enzymes vital in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. GSTZ1 is a bifunctional protein which has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 has low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. GSTZ1 catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.

Abhydrolase domain-containing protein 10 (ABHD10) is a member of the AB hydrolase superfamily.

Deoxyribose-phosphate aldolase (DERA) is a member of the deoC/fbaB aldolase protein family involved in the carbohydrate degradation pathway. DERA catalyzes the conversion of 2-deoxy-D-ribose 5-phosphate to D-glyceraldehyde 3-phosphate and an acetyldehyde.

The AsnRS enzyme is a member of the ligases family, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. An asparagine-tRNA ligase is an enzyme which catalyzes the chemical reaction: ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn. The three substrates of the AsnRS enzyme are ATP, L-asparagine, and tRNA(Asn), whereas its three products are AMP, diphosphate, and L-asparaginyl-tRNA(Asn).

Phenylalanyl-tRNA synthetase 2 mitochondrial (FARS2) is a member of the class II aminoacyl- tRNA synthetase family. FARS2 is a mitochondrial matrix protein. FARS2 when acting as a monomer, catalyzes the ATP-dependent conversion of L-phenylalanine and tRNA (Phe) to L-phenlalanyltRNA (Phe), an event which is vital for proper translation and protein expression.

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.

Tyrosylprotein Sulfotransferase 2 (TPST2) is a member of the protein sulfotransferase family. TPST2 is a widely expressed protein, which catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The TPST2 protein is a type II integral membrane protein located in the Golgi body.

Tartrate-resistant acid phosphatase type 5 (ACP5) is involved in osteopontin and bone sialoprotein dephosphorylation. ACP5 is an iron containing glycoprotein which catalyzes the conversion of orthophosphoric monoester to alcohol and orthophosphate. ACP5 expression seems to increase in some pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias. ACP5 is the most basic of the acid phosphatases and is the only form not inhibited by L(+)-tartrate.