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Human Oxytocin stimulates uterine smooth muscle contractions indirectly and stimulates the mammary glands to increase lactation without increasing the production of milk.

CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.

Nafarelin acetate is a synthetic analog of the naturally occurring gonadotropin-releasing hormone (GnRH). Nafarelin stimulates the release of the pituitary gonadotropins, LH and FSH, resulting in a temporary increase of ovarian steroidogenesis.

Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.

NPPC is proteolytically managed to create a secreted hormone of the natriuretic peptide family. NPPC is vasoactive and natriuretic and controls the evolution and differentiation of cartilaginous growth plate chondrocytes.

CNDP Dipeptidase 2 (CNDP2), is a cytosolic, non-specific dipeptidase which is a part of the peptidase M20A protein family. CNDP2 is a secreted peptidase homologous to M20 peptidases. CNDP2 expresses through all adult and fetal tissue, though, an isoform missing exons 3 and 4 expresses in all fetal tissue in adult liver. Over expression of CPGL-B in hepatocellular carcinoma cells results in significant inhibition of HC cell viability, colony formation, cell invasiveness and tumor configuration.

Prolyl Endopeptidase , also known as PREP is a cytosolic prolyl endopeptidase which cleaves peptide bonds on the C-terminal side of prolyl residues within peptides which are up to about 30 a.a long. In addition, Prolyl endopeptidases have been shown to be implicated in the maturation and degradation of peptide hormones and neuropeptides.

Hepatitis B is one of a few known non-retroviralviruses which employ reverse transcriptionas a part of its replication process. (HIV, a completely unrelated virus, also uses reverse transcription, but it is a retrovirus.) HBV invades the cell by binding to surface receptor and become internalized. The viral core particles then migrate to the hepatocyte nucleus and the partially double-stranded, relaxed circular genomes (RC-DNA) are repaired to form a covalently closed circular DNA (cccDNA), which is the template for viral genomic and sub-genomic RNAs by cellular RNA polymerase II. Of these, the pregenomic RNA(pgRNA is selectively packaged into progeny capsids and is then reverse-transcribed into new RC-DNA. The core can either bud into the endoplasmic reticulum to be enveloped or exported from the cell or recycled back into the genome for conversion to cccDNA.

SERPINB2 is an inhibitory serpin produced primarily in keratinocytes, stimulated monocytes, and placental trophoblasts. SERPINB2 is found primarily as a 47 kDa non-glycosylated intracellular protein that is induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated SERPINB2 are similarly effective as inhibitors of uPA, the only proven physiological target of SERPINB2.

Hepatitis B is one of a few known non-retroviralviruses which employ reverse transcriptionas a part of its replication process. (HIV, a completely unrelated virus, also uses reverse transcription, but it is a retrovirus.) HBV invades the cell by binding to surface receptor and become internalized. The viral core particles then migrate to the hepatocyte nucleus and the partially double-stranded, relaxed circular genomes (RC-DNA) are repaired to form a covalently closed circular DNA (cccDNA), which is the template for viral genomic and sub-genomic RNAs by cellular RNA polymerase II. Of these, the pregenomic RNA (pgRNA is selectively packaged into progeny capsids and is then reverse-transcribed into new RC-DNA. The core can either bud into the endoplasmic reticulum to be enveloped or exported from the cell or recycled back into the genome for conversion to cccDNA.

Arginine vasopressin (AVP), also known as argipressin or antidiuretic hormone (ADH), is a human hormonethat is released when the body is low on water; it causes the kidneysto conserve water, but not salt, by concentrating the urineand reducing urine volume. It also raises blood pressure by inducing moderate vasoconstriction. It has various effects in the brain.
A very similar substance, lysine vasopressin (LVP) or lypressin, has the same function in pigsand is often used in human therapy.
Vasopressin is a peptide hormone. It is derived from a preprohormoneprecursor that is synthesized in the hypothalamus, from which it is liberated during transport to the posterior pituitary. Most of it is stored in the posterior partof the pituitary glandto be released into the blood stream; some of it is also released directly into the brain.
AVP allows water reabsorption by the introduction of additional water channels in cortical and inner medullary collecting ducts.

Glutamyl endopeptidase (GLU-C) is an enzyme which cleaves peptide bonds on the carboxyl-terminal side of glutamic acid and, less frequently, aspartic acid (for example: Glu-|-Xaa, Asp-|-Xaa). GLU-C is a pathogenic factor involved in the adherence and colonization of human tissue. GLU-C preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. GLU-C is required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. GLU-C is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. Furthermore, GLU-C protects bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. GLU-C may also be involved in the stability of secreted lipases.

A fusion tag called FLAG consists of eight amino acids (AspTyrLysAspAspAspAspLys) including an enterokinase-cleavage site. FLAG is specifically designed for immunoaffinity chromatography. It allows elution under non-denaturing conditions. Several antibodies against this peptide have been developed. One antibody denoted as M1 binds the peptide in the presence of bivalent metal cations preferably Ca(+). Elution is effected by chelating agents. Another strategy is competitive elution with excess of free Flag Peptide. The FLAG peptide purifies and detects recombinant fusion proteins. FLAG peptide is useful in Western blotting, immunocytochemistry, immunoprecipitation, flow cytometry, protein purification, and in the study of protein-protein interactions, cell ultrastructure, and protein localization. Flag peptide is a hydrophilic tag which significantly improves the detection and purification of recombinant fusion proteins.

The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.