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Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Prolactin’s primary function is to promote and maintain lactation and also in breast cancer development, regulation of reproductive function and immunoregulation.

Methionine sulfoxide reductase B3 (MSRB3) is a member of the methionine sulfoxide reductases (MSR) family proteins. MSRB3 catalyzes the reduction of methionine sulfoxide to methionine. The MSRB3 enzyme acts as a monomer and requires zinc as a cofactor. MSRs are thought to defend against reactive oxygen species-induced oxidative damage in various organs, including the most environmentally exposed organ, the human skin. MSRB3 has a vital role in cold tolerance by eliminating MetO and ROS which accumulate at the ER during cold acclimation.

4-Hydroxyphenylpyruvate Dioxygenase Isoform-1 is an Fe-containing enzyme, which catalyzes the second reaction in the catabolism of tyrosine the conversion of 4-hydroxyphenylpyruvate to homogentisate. Present as a homodimer, HPD uses zinc as a cofactor to catalyze the third step in the conversion of L-phenylalanine to fumarate and acetoacetic acid. Flaws in the gene encoding HPD result in tyrosinemia type 3 and hawkinsinuria, two inborn defects of metabolism which are related to a number of symptoms, like mental retardation and seizures and hair and urine abnormalities.

METTL1 is recognized as tRNA (guanine-N(7)-)-methyltransferase that is a part of the methyltransferase superfamily. METTL1 displays high sequence similarity to yeast ORF YDL201w and can be inactivated by phosphorylation. METTL1 protein has a conserved S-adenosylmethionine-binding motif and ccatalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.

Proteasome 26S Subunit, Non-ATPase 13 (PSMD13) is a part of the proteasome subunit S11 family and contains one PCI domain. PSMD13 plays a role as a regulatory subunit of the 26S proteasome which takes part in the ATP-dependent degradation of ubiquitinated proteins.

PRMT1 Methylates (mono & asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain (may methylate HNRNPA1 and histones). Methylates SUPT5H.
The PRMT1 protein functions as a histone methyltransferase specific for H4.
PRMT1 is an essential factor in oncogenesis and is a potential novel therapeutic target in cancer.
PRMT1-mediated methylation serves as a positive modulator of IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells.
CAF1 is a new regulator of PRMT1-dependent arginine methylation.
PRMT1 arginine-methylates MRE11 therefore it regulates the activity of MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response.
PRMT1 plays a post-translationally part in regulating the transcriptional activity.
PRMT1 is found predominantly in the cytoplasma though a fraction of PRMT1 is located in the nucleus.

Ubiquitin-conjugating enzyme E2 J2 (UBE2J2) is a member of the ubiquitin-conjugating enzyme family. UBE2J2 catalyzes the covalent attachment of ubiquitin to other proteins. UBE2J2 is located in the membrane of the endoplasmic reticulum. UBE2J2 participates in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD).

ALDH1A1 is part of the aldehyde dehydrogenases family.
Aldehyde dehydrogenase is the 2nd protein of the main oxidative pathway of alcohol metabolism. Cytosolic and mitochondrial are 2 main liver isoforms of ALDH that are differentiateed by their electrophoretic mobility, kinetic property, & subcellular localization. The majority of Caucasians have two main isozymes, whereas just about 50% of Orientals have only the cytosolic form, excluding the mitochondrial form. ALDH1A1 is also a member of the group of corneal crystallins that assist the transparency of the cornea.
(Retinal + NAD+ + H2O = retinoate + NADH).

BPGM is found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. PGM deficiency increases the oxygen affinity of cells. BPGM is a multifunctional enzyme that catalyzes 2,3-DPG synthesis through its synthetase activity, and 2,3-DPG degradation using its phosphatase activity. BPGM has phosphoglycerate phosphomutase activity. Mutations in BPGM cause hemolytic anemia. BPGM catalyzes the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

DDT is an enzyme that catayzes the tautomerization of D-dopachrome to give 5,6-dihydroxyindole (DHI). DDT is part of the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. DDT shares a homologous amino acid sequence (33% identical) with MIF and has similar tautomerase activity. DDT functions a proinflammatory cytokine.

Betaine-homocysteine methyltransferase (BHMT) is a cytosolic enzyme that catalyzes the conversion of betaine and homocysteine to dimethylglycine and methionine, respectively. BHMT displays differential expression in a model of liver cirrhosis.

Guanosine monophosphate reductase (GMPR) catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. GMPR acts in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in upholding the intracellular balance of A and G nucleotides. In addition, the GMPR protein functions in the re-utilization of free intracellular bases and purine nucleosides.

CKB is a cytoplasmic enzyme that takes part in energy homeostasis. CKB enzyme reversibly catalyzes the transfer of phosphate among ATP and various phosphogens such as creatine phosphate. CKB functions as a homodimer in the brain as well as in different tissues, and as a heterodimer with a similar muscle isozyme in heart. Creatine kinases supply the energy of phosphate hydrolysis essential to drive the normal role of many cellular systems including muscle, tumor and cancer cells.

The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

Carboxylesterase 1D, also known as CES1D is part of a big family of carboxylesterases which are responsible for the hydrolysis of ester in addition to amide bonds. CES1D is the principle lipase of white adipose tissue fat cake extracts. Partially purified white adipose tissue Ces1d had lipase activity in addition to lesser but detectable neutral cholesteryl ester hydrolase activity. CES1D demonstrates low catalytic efficiency for hydrolysis of CPT-11, a prodrugs for camptothecin used in cancer therapeutics.

FEN1 removes 5'' overhanging flaps in DNA repair and processes the 5'' ends of Okazaki fragments in lagging strand DNA synthesis. The interaction between FEN1 and AP endonuclease 1 during long-patch base excision repair provides coordinated loading of the proteins onto the substrate, therefore passing the substrate from one enzyme to another. FEN1 is part of the XPG/RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. DNA secondary structure can inhibit flap processing at certain trinucleotide repeats in a length-dependent manner by concealing the 5'' end of the flap that is necessary for both binding and cleavage by the protein encoded by this gene. Therefore, secondary structure can deter the protective function of this protein, leading to site-specific trinucleotide expansions.

Glycogen phosphorylase (PYGL) converts from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of the PYGL enzyme is further regulated by numerous allosteric effectors and hormonal controls. The liver isozyme supplies the glycemic demands of the body in general whereas the brain and muscle isozymes supply just those tissues.

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.

Cathepsins B, C, H, L, S, V, X/Z/P and 1 are cysteine proteases of the papain family. Cathepsin C is also known as DPPI (dipeptidyl-peptidase I). Cathepsin A is a serine carboxypeptidase and Cathepsin D and E are aspartic proteases. As lysosomal proteases, cathepsins play an important role in protein degradation. Because of their redistribution or increased levels in human and animal tumors, cathepsins may have a role in invasion and metastasis. Cathepsins are synthesized as inactive proenzymes and processed to become mature and active enzymes. Endogenous protein inhibitors, such as cystatins and some serpins, inhibit active enzymes.

UDP Glycosyltransferase 8 (UGT8) is a member of the UDP-glycosyltransferase family. UGT8 catalyzes the transfer of galactose to ceramide, a crucial enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system.

6PGD is the 2nd dehydrogenase in the pentose phosphate shift. Pentose is crucial for the biosynthesis of nucleic acid. The pentose phosphate cycle is a prominent source of NADPH. 6PGD deficiency is mostly asymptomatic, and the inheritance of this deasis is autosomal dominant. PGD deficiency elevate the erythrocyte pyruvate kinase levels of activity & decreases glutathione synthetase, which causes hemolysis.

UBE2D2 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2D2 takes part in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. UBE2D2 catalyzes ubiquitination of IkB-alpha in a SCFB-TRCP and phosphorylation dependent method.

UBE2K belongs to the ubiquitin-conjugating enzymes family which take part in many cellular processes such as selective protein degradation, DNA repair, cell cycle control, and sporulation. In this mechanism, the ATP-coupled activation and subsequent ligation of ubiquitin are catalyzed by separate enzymes functionally linked by ubiquitin carrier protein UBC1. In addition, UBE2K is involved in Alzheimer's disease, Huntington's disease and antigen processing through its interaction with amyloid-?, huntingtin, and MHC-heavy chain proteins.