Human Natriuretic peptides B acts as a cardiac hormone; it is associated with many biological actions, such as diuresis, natriuresis, vasorelaxation, which inhibits the secretion of rennin and aldosterone. It acts as a paracrine antifibrotic factor in the heart. Natriuretic peptides B can help restore the body balance of salt and water, improves the heart function. Natriuretic peptides B binds and stimulates the cGMP production of the NPR1 receptor and binds the clearance receptor NPR3.

Brain-type Natriuretic Peptide (BNP) is a nonglycosylated peptide that is produced predominantly by ventricular myocytes and belongs to the natriuretic peptide family. Proteolytic cleavage of the 12 kDa BNP precursor gives rise to N-terminal Pro BNP (NT-proBNP) and mature BNP. N-terminal proB-type natriuretic peptide (NT-proBNP), a useful marker of heart failure (HF), is considered to be secreted mainly from the ventricle, increased serum NT-proBNP levels are also encountered in conditions such as atrial fibrillation (AF) and atrial septal defect in patients without HF.

NPFF Protein, Human, Recombinant (GST) is expressed in E. coli.

FGF basic is one of 22 mitogenic proteins of the FGF family, which show 35-60% amino acid conservation. Unlike other FGFs, FGF acidic and basic lack signal peptides and are secreted by an alternate pathway. The 17 kDa mouse sequence has 98% aa identity with rat, and 95% identity with human, bovine, and sheep FGF basic. Binding of FGF to heparin or cell surface HSPG is necessary for binding, dimerization and activation of tyrosine kinase FGF receptors. FGF basic binds other proteins, polysaccharides and lipids with lower affinity. Expression of FGF basic is nearly ubiquitous but disruption of the mouse FGF basic gene gives a relatively mild phenotype, suggesting compensation by other FGF family members. FGF basic modulates such normal processes as angiogenesis, wound healing and tissue repair, embryonic development and differentiation, neuronal function and neural degeneration. Transgenic overexpression of FGF basic results in excessive proliferation and angiogenesis is reminiscent of a variety of pathological conditions.

Carboxypeptidase A2 (CPA) is a secreted pancreatic procarboxy-peptidase that cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition.

Lysosomal Pro-X Carboxypeptidase (PRCP) belongs to the peptidase S28 family. PRCP is detected in many tissues, with highest levels observed in placenta, lung, and liver. It is also present in the heart, brain, pancreas, and kidney. PRCP exists as a homodimer. PRCP cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. PRCP has been shown to be an activator of the cell matrix-associated prekallikrein.

Trefoil factors (TFF) are secretory products of mucin producing cells. They play a key role in the maintenance of the surface integrity of oral mucosa and enhance healing of the gastrointestinal mucosa by a process called restitution. TFF comprises the gastric peptides (TFF1), spasmolytic peptide (TFF2), and the intestinal trefoil factor (TFF3). They have an important and necessary role in epithelial restitution within the gastrointestinal tract. Members of the trefoil family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfide bonds. They are stable secretory proteins expressed in gastrointestinal mucosa. Trefoil Factor 3(TFF3) is involved in the maintenance and repair of the intestinal mucosa. TFF3 promotes the mobility of epithelial cells in healing processes (motogen).

Interleukin‑17C (IL‑17C) is a 15‑20 kDa glycosylated cytokine that plays an important role in mucosal immunity and chronic inflammation. The six IL‑17 cytokines (IL‑17A‑F) are encoded by separate genes but adopt a conserved cystine knot fold. IL‑17C is Cytokine that plays a crucial role in innate immunity of the epithelium, including to intestinal bacterial pathogens, in an autocrine manner. Stimulates the production of antibacterial peptides and proinflammatory molecules for host defense by signaling through the NF-kappa-B and MAPK pathways. Acts synergically with IL22 in inducing the expression of antibacterial peptides, including S100A8, S100A9, REG3A and REG3G.

Matrix extracellular phosphoglycoprotein (MEPE) is expressed in bone and teeth where it has multiple functions. The C-terminus of MEPE contains a mineral-binding, acidic serine- and aspartate-rich motif (ASARM) that is also present in other noncollagenous proteins of mineralized tissues.MEPE-derived ASARM peptides function in phosphate homeostasis and direct inhibition of bone mineralization in a phosphorylation-dependent manner.

Releases the N-terminal proline from various substrates. Cleaves specifically Pro-betaNA and small peptides containing proline at the amino terminal. No activity against hydroxyproline-betaNA. Proline iminopeptidase Protein, Elizabethkingia meningoseptica, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 41.6 kDa and the accession number is O05420.

Metalloprotease capable of the hydrolysis of insoluble hydrophobic substrates. Hydrolyzes azocoll and gelatin and, at a lower rate, soluble and insoluble collagens. Does not cleave short synthetic peptides. Preferentially hydrolyzes the 24-Phe-|-Phe-25 bond in the insulin B-chain, followed by the 5-His-|-Leu-6 bond. Inactivates endothelin-1, primarily by cleavage of the 5-Ser-|-Leu-6 and 16-His-|-Leu-17 bonds. Hydrolyzes the alpha chain of C3 to generate a C3b-like protein. Inhibits complement-mediated hemolysis and opsinization of bacteria. Hydrolyzes the insect antimicrobial peptide cecropin. Decreases the length of E.faecalis chains via the activation of autolysin. Degrades polymerized fibrin.

High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors. Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Receptor for TAFA4, mediates its effects on chemoattracting macrophages, promoting phagocytosis and increasing ROS release. FPR1 Protein, Human, Recombinant (GST & His & Myc) is expressed in E. coli expression system with N-10xHis-GST and C-Myc tag. The predicted molecular weight is 34.9 kDa and the accession number is P21462.

Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum.

Deiminates the guanidino group of C-terminal arginine residues on a variety of peptides, including the vasoregulatory peptide-hormone bradykinin, to yield ammonia and a citrulline residue. May promote the growth of the pathogen in the periodontal pocket by producing ammonia, ammonia having a protective effect during acidic cleaning cycles in the mouth. PAD Protein, Porphyromonas gingivalis, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 60.9 kDa and the accession number is Q9RQJ2.

Peptide Ready HLA-G&B2M Monomer is absent from peptide, namely peptide-receptive MHC. It can be loaded with antigenic peptides matching HLA-G. Peptide ready MHC molecules comprising human HLA alleles and B2M, which can be readily tetramerized and loaded with peptides of choice in a high-throughput manner.

Peptide Ready HLA-A*02:01&B2M Tetramer is absent from peptide, namely peptide-receptive MHC. It can be loaded with antigenic peptides matching HLA-A*02:01. Peptide ready MHC molecules comprising human HLA alleles and B2M, which can be readily tetramerized and loaded with peptides of choice in a high-throughput manner.

TMED10 disrupts the complex formation between TGF-beta type I (also termed ALK5) and type II receptors (TbetaRII). Misexpression studies revealed that TMED10 attenuated TGF-beta-mediated signaling. A 20-amino acid-long region from Thr(91) to Glu(110) within the extracellular region of TMED10 was found to be crucial for TMED10 interaction with both ALK5 and TbetaRII. Synthetic peptides corresponding to this region inhibit both TGF-beta-induced Smad2 phosphorylation and Smad-dependent transcriptional reporter activity. In a xenograft cancer model, where previously TGF-beta was shown to elicit tumor-promoting effects, gain-of-function and loss-of-function studies for TMED10 revealed a decrease and increase in the tumor size, respectively. That TMED10 expression levels are the key determinant for efficiency of TGF-beta receptor complex formation and signaling.

INS (Insulin) is a Protein Coding gene. This gene encodes insulin, a peptide hormone that plays a vital role in the regulation of carbohydrate and lipid metabolism. After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. The binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Diseases associated with INS include Hyperproinsulinemia and Maturity-Onset Diabetes Of The Young, Type 10. A multitude of mutant alleles with phenotypic effects has been identified, including insulin-dependent diabetes mellitus, permanent neonatal diabetes mellitus, maturity-onset diabetes of the young type 10, and hyperproinsulinemia.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

NTS (Neurotensin) is a Protein Coding gene. This gene encodes a common precursor for two peptides, neuromedin N and neurotensin. NTS is a neuropeptide distributed in the central nervous and digestive systems. It belongs to the neurotensin family. NTS is an endogenous tridecapeptide of the central nervous system and the gastrointestinal tract of different mammalian species including the human. The human gene encoding neurotensin has previously been assigned to chromosome 12 but no regional localization was available. NTS is widely expressed in the central and peripheral nervous system, which is mainly mediated by neurotensin receptor1 (NTSR1) to activate the related downstream signaling pathways. Diseases associated with NTS include Dumping Syndrome and Duodenogastric Reflux.

Leukocyte-derived arginine aminopeptidase (LRAP), also known as endoplasmic reticulum-aminopeptidase 2 (ERAP2), is the second identified aminopeptidase localized in the in the lumenal side of endoplasmic reticulum (ER) processing antigenic peptides presented to major histocompatibility complex (MHC) class I molecules. It is a 96-amino acid protein with significant homology to placental leucine aminopeptidase and adipocyte-derived leucine aminopeptidase. LRAP preferentially hydrolyzes the basic residues Arg and Lys, and contains the HEXXH(X)18E zinc-binding motif, which is the characteristic of the M1 family of zinc metallopeptidases which also includes PILS/ARTS1/ERAP1 and LNPEP/PLAP. Induced by interferon-gamma, LRAP is able to trim various MHC class I antigenic peptide precursors.

Relaxin-1, also known as Prorelaxin H1 and RLN1, is a secreted protein that belongs to the insulin family. It is a peptide hormone that was first described in 1926 by Frederick Hisaw. Since its discovery as a reproductive hormone 8 years ago, relaxin has been implicated in a number of pregnancy-related functions involving extracellular matrix (ECM) turnover and collagen degradation. It is now becoming evident that relaxin's ability to reduce matrix synthesis and increase ECM degradation has important implications in several nonreproductive organs, including the heart, lung, kidney, liver and skin. The relaxin-like peptide family belongs in the insulin superfamily and consists of 7 peptides of high structural but low sequence similarity; relaxin-1 (RNL1), relaxin-2 (RNL2) and relaxin-3 ( RNL3), and the insulin-like (INSL) peptides, INSL3, INSL4, INSL5 and INSL6. The functions of relaxin-3, INSL4, INSL5, INSL6 remain uncharacterised. Relaxin-1 / RLN1 is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. Relaxin-1 / RLN1 may be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix. Relaxin and estrogen appear to play protective roles against airway fibrosis, airway SM thickening, and cardiac hypertrophy. Relaxin may also provide a means to regulate excessive collagen deposition during kidney development and in diseased states characterized by renal fibrosis.

Transglutaminases (TGase) are a family of calcium-dependent acyl-transfer enzymes ubiquitously expressed in mammalian cells and responsible for catalyzing covalent cross-links between proteins or peptides. Transglutaminase 3 (TGM3) is a member of a family of Ca2+-dependent enzymes that catalyze covalent cross-linking reactions between proteins or peptides. TGM3 isoform is widely expressed and is important for epithelial barrier formation. It is a zymogen, requiring proteolysis for activity. Calcium-activated TGM3 can bind, hydrolyze, and is inhibited by GTP, despite lacking structural homology with other GTP binding proteins. TGM3 displays a diffuse cytoplasmic distribution in vitro consistent with its proposed role in the early phase of cornified cell envelope assembly in the cytoplasm. TGM3-driven specific isopeptide bonds between intermediate filaments and KAPs participate to the progressive scaffolding of the hair shaft. Additionally, TGM3 may be a novel prognostic biomarker for esophageal squamous cell carcinoma (ESCC).

GPR37 (cathepsin Z) is an orphan receptor that belongs to the G-protein coupled receptor 1 family. G protein-coupled receptors are a large protein family comprised of transmembrane receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses. They only exist in eukaryotes, including yeast, choanoflagellates, and animals. These receptors are bonded and activated by light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters. These ligands vary in size from small molecules to peptides to large proteins. G protein-coupled receptors are involved in many diseases and are also the target of approximately 40% of all modern medicinal drugs. GPR37 is expressed in the brain and spinal cord, and at lower levels in the testis, placenta, and liver, but no detectable expression is observed in any other tissue. GPR37 may have a unique functional role in the central nervous system.

Adrenomedullin consists of 52 amino acids and is a member of the adrenomedullin family. It s a a hypotensive peptide and has 1 intramolecular disulfide bond. It seems that adrenomedullin has a slight homology with the calcitonin gene-related peptide. Adrenomedullin has a highly expression in pheochromocytoma and adrenal medulla. It also can be detected in lung, ventricle and kidney tissues. Adrenomedullin and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, adrenomedullin is diuretic and natriuretic, and both adrenomedullin and PAMP inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels. It is believed that adrenomedullin functions through combinations of the calcitonin receptor like receptor and receptor activity-modifying proteins complexes, as well as CGRP receptors.

Glutaminyl cyclase, also known as QPCT, can promote the N-terminal cyclization reaction of N-terminal pyroglutamate(pGlu). The pGlu formation from its glutaminyl precursor is required in the maturation of numerous bioactive peptides, while the aberrant formation of pGlu may be related to several pathological processes, such as osteoporosis and amyloidotic diseases. Glutaminyl cyclase's structure reveals an alpha/beta scaffold akin to that of two-zinc exopeptidases but with several insertions and deletions, particularly in the active-site region. Glutaminyl cyclase's amino acid sequence of this enzyme is 86% identical to that of bovine glutaminyl cyclase. It is responsible for the presence of pyroglutamyl residues in many neuroendocrine peptides.

Plasma kallikrein, also known as Fletcher factor or kallikrein B1 (KLKB1), is a serine endopeptidase, like its homologs tissue kallikrein and kallikrein-related peptidases (KLKs). Its physiological role is to catalyze the release of kinins and other vasoactive peptides. KLKB1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 70.3 kDa and the accession number is P26262.

Pro-Neuropeptide Y (NPY) is a member of the NPY family. NPY is a secreted protein and is one of the most abundant peptides in the nervous system. It also can be found in some chromaffin cells of the adrenal medulla. NPY can be cleaved into Neuropeptide Y and C-flanking peptide of NPY chain, which regulates energy usage, and it is involved in learning, memory processing, and epilepsy. NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. In addition, NPY increases the proportion of energy stored as fat and blocks nociceptive signals to the brain.

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.

Endothelins are endothelium-derived vasoconstrictor peptides. Probable ligand for G-protein coupled receptors EDNRA and EDNRB which activates PTK2B, BCAR1, BCAR3 and, GTPases RAP1 and RHOA cascade in glomerular mesangial cells.

May contribute to the degradation of peptide hormones and be involved in the inactivation of neuronal peptides.

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Leucyl aminopeptidase Protein, Mycoplasma pneumoniae, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 64.8 kDa and the accession number is P75206.

Endothelins are endothelium-derived vasoconstrictor peptides. Probable ligand for G-protein coupled receptors EDNRA and EDNRB which activates PTK2B, BCAR1, BCAR3 and, GTPases RAP1 and RHOA cascade in glomerular mesangial cells. Endothelin-1/EDN1 Protein, Rat, Recombinant (His & KSI) is expressed in E. coli expression system with N-6xHis-KSI tag. The predicted molecular weight is 17.8 kDa and the accession number is P22388.

HLA-E is a nonclassical member of the major histocompatibility complex class I gene locus. HLA-E protein shares a high level of homology with MHC Ia classical proteins: it has similar tertiary structure, associates with β2-microglobulin, and is able to present peptides to cytotoxic lymphocytes. The main function of HLA-E under normal conditions is to present peptides derived from the leader sequences of classical HLA class I proteins, thus serving for monitoring of expression of these molecules performed by cytotoxic lymphocytes.

MAGE-A4 and MAGE-A8 are type I membes of the melanoma associated antigen (MAGE) family. The MAGE family is a large, highly conserved group of proteins that share a common MAGE homology domain. Both MAGE-A4 and MAGE-A8 antigen-presenting peptides can be presented by HLA-A*02:01.

Peptide Ready HLA-G&B2M Monomer is absent from peptide, namely peptide-receptive MHC. It can be loaded with antigenic peptides matching HLA-G. Peptide ready MHC molecules comprising human HLA alleles and B2M, which can be readily tetramerized and loaded with peptides of choice in a high-throughput manner.

Peptide Ready HLA-A*11:01&B2M Monomer is absent from peptide, namely peptide-receptive MHC. It can be loaded with antigenic peptides matching HLA-A*11:01. Peptide ready MHC molecules comprising human HLA alleles and B2M, which can be readily tetramerized and loaded with peptides of choice in a high-throughput manner.

Qa-1b binds a peptide (AMAPRTLLL), referred to as Qdm (for Qa-1 determinant modifier), derived from the signal sequence of murine class Ia molecules. This peptide binds with high affinity and accounts for almost all of the peptides associated with this molecule. Human histocompatibility leukocyte antigen (HLA)-E, a homologue of Qa-1b, binds similar peptides derived from human class Ia molecules and interacts with CD94/NKG2 receptors on natural killer cells.

Peptide Ready HLA-A*02:01&B2M Monomer is absent from peptide, namely peptide-receptive MHC. It can be loaded with antigenic peptides matching HLA-A*02:01. Peptide ready MHC molecules comprising human HLA alleles and B2M, which can be readily tetramerized and loaded with peptides of choice in a high-throughput manner.

HLA-E*01:03&B2M&Peptide ready Monomer is absent from peptide, namely peptide-receptive MHC. It can be loaded with antigenic peptides matching HLA-E*01:03. Peptide ready MHC molecules comprising human HLA alleles and B2M, which can be readily tetramerized and loaded with peptides of choice in a high-throughput manner.

HLA-E is a nonclassical member of the major histocompatibility complex class I gene locus. HLA-E protein shares a high level of homology with MHC Ia classical proteins: it has similar tertiary structure, associates with β2-microglobulin, and is able to present peptides to cytotoxic lymphocytes. The main function of HLA-E under normal conditions is to present peptides derived from the leader sequences of classical HLA class I proteins, thus serving for monitoring of expression of these molecules performed by cytotoxic lymphocytes.

THOP1, also known as Thimet oligopeptidase 1, Thimet oligopeptidase, EC 3.4.24.15, or EP24.15, is a zinc(II) endopeptidase implicated in the processing of numerous physiological peptides. As an intracellular enzyme, highly expressed in the brain, kidneys and neuroendocrine tissue, THOP1 has been proposed to metabolize peptides within cells, thereby affecting antigen presentation and G protein-coupled receptor signal transduction. Its substrates is gonadotrophin-releasing hormone (GnRH), an important hypothalamic hormone that regulates the synthesis and release of oestradiol and facilitates female sexual behaviour. THOP1 against toxic effects of Abeta in the early stages of Alzheimer disease (AD) pathology, and suggest that the observed increase in THOP1 expression might be part of a compensatory defense mechanism of the brain against an increased Abeta load.

GALNT2, also known as GalNAc-T2, is a member of the GalNAc-transferases family. Members of this family transfer an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. GALNT2 may play a role in lipid metabolism. It catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b.

NAGA (Alpha-N-Acetylgalactosaminidase) is a Protein Coding gene. NAGA encodes the lysosomal enzyme alpha-N-acetylgalactosaminidase, which cleaves alpha-N-acetylgalactosaminyl moieties from glycoconjugates. It belongs to the glycosyl hydrolase 27 family. The antinociceptive effect of NAGA may involve the participation of endogenous opioid peptides and endogenous catecholamines. Normal alpha-NAGA is synthesized as a 52 kDa precursor which matures to a 49 kDa species through phosphorylation and carbohydrate trimming. Mutations in gene encoding alpha-NAGA cause a wide range of diseases, characterized by mild to severe clinical features. NAGA is widely expressed in the placenta, appendix, and other tissues. Diseases associated with NAGA include Kanzaki Disease and Schindler Disease, Type I.

Carboxypeptidase Q (Cpq) is a member of the peptidase M28 family. PGCP is involved in a number of fundamental biological processes such as the hydrolysis of circulating peptides, catalyzing the hydrolysis of dipeptides with unsubstituted terminals into amino acids. Carboxypeptidase may play an important role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor. The monomeric form is inactive while the homodimer is active.

Plasma kallikrein, also known as Fletcher factor or kallikrein B1 (KLKB1), is a serine endopeptidase, like its homologs tissue kallikrein and kallikrein-related peptidases (KLKs). Its physiological role is to catalyze the release of kinins and other vasoactive peptides. KLKB1 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 70.19 kDa and the accession number is A0A2K5VTJ9.

Insulin-Degrading Enzyme (IDE) is a secreted enzyme that belongs to the peptidase M16 family. IDE is a large zinc-binding protease and cleaves multiple short polypeptides that vary considerably in sequence. IDE plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling. IDE degrades amyloid formed by APP and IAPP. IDE may participate in the degradation and clearance of naturally secreted amyloid β-protein by neurons and microglia. IDE, which migrates at 110 kDa during gel electrophoresis under denaturing conditions, has since been shown to have additional substrates, including the signaling peptides glucagon, TGF α and β-endorphin.

Protachykinin-1(TAC1) is a secreted protein and belongs to the tachykinin family. TAC1 is encoded by the TAC1 gene. This gene encodes four products of the tachykinin peptide hormone family, substance P and neurokinin A, as well as the related peptides, neuropeptide K and neuropeptide gamma. These hormones are thought to function as neurotransmitters which interact with nerve receptors and smooth muscle cells. They are known to induce behavioral responses and function as vasodilators and secretagogues.

Recombinant Murine TFF-2 is an 11.9 kDa polypeptide of 106 amino acid residues, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds. The Trefoil Factor peptides (TFF1, TFF2 and TFF3) are expressed in the gastrointestinal tract, and appear to play an important role in intestinal mucosal defense and repair. TFF2 has been shown to inhibit gastrointestinal motility and gastric acid secretion. Recent data suggests a potential role for TFF2 in acute and chronic asthma. It inhibits gastrointestinal motility and gastric acid secretion. As a structural component of gastric mucus, it possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains.

Carboxypeptidase A4 (CPA4) is a member of the peptidase M14 family. CPA4 is metalloprotease that could be involved in the histone hyperacetylation pathway. CPA4 binds one zinc ion per subunit and could catalyze to release of a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val.They have distinct expression patterns and different specificities for example, preferentially cleaving aromatic (carboxypeptidase As) or basic (carboxypeptidase Bs) residues. Several, such as carboxypeptidase Xs, have lost their catalytic activity. Carboxypeptidases play important roles in digestion of food, processing of bioactive peptides and blood coagulation.

Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.