1mg

Neuron-Specific Enolase (NSE) is recognized as a biomarker for small cell lung cancer. It is secreted from neuroendocrine cells as well as neurogenic tumors. Its levels in NSE-secreting neoplasms correlate with tumor mass and tumor metabolic activity.

Neurotrophin-4 (NT-4), also known as NT-5, is a neurotrophic factor structurally related to β-NGF, BDNF, and NT-3. Human NT-4 shares 48 – 52% aa sequence identity with human β-NGF, BDNF, and NT-3. Neurotrophins have six conserved cysteine residues that are involved in the formation of three disulfide bonds. NT-4 is expressed highest levels in prostate, lower levels in thymus, placenta, and skeletal muscle. NT-4 binds and induces receptor dimerization and activation of TrkB. NT-4 can signal through TrkB receptors and promotes the survival of peripheral sensory sympathetic neurons.

BNP and NT-proBNP are separated from precursor molecule proBNP via proteolytic processing. The BNP and NT-proBNP level in blood are proportional to the severity of cardiac dysfunction. They can be used for diagnosis of congestive heart failure (CHF).

Oncostatin M (OSM) is a multifunctional cytokine, and belongs to Interleukin-6 (IL-6) subfamily, which also includes IL-11, leukemia inhibitory factor (LIF), ciliary neurotropic factor, cardiotrophin-1, and novel neurotropin-1. In vivo, OSM is secreted from activated T cells, monocytes, neutrophils, and endothelial cells. OSM is related to LIF, and shares a receptor with LIF in human. Human OSM can bind to gp130 and recruit OSM Receptor β or LIF Receptor β to form a ternary complex. OSM stimulates the growth of different types of cells, including megakaryocytes, fibroblasts, vascular endothelial cells, and T cells. OSM inhibits the proliferation of several cancer cell lines, such as solid tissue tumor cells, lung cancer cells, melanoma cells, and breast cancer cells.

Oncostatin M (OSM) is a multifunctional cytokine, and belongs to Interleukin-6 (IL-6) subfamily, including IL-11, leukemia inhibitory factor (LIF), ciliary neurotropic factor, cardiotrophin-1, and novel neurotropin-1. In vivo, OSM is secreted from activated T cells, monocytes, neutrophils, and endothelial cells. OSM is related to LIF, and share a receptor with LIF in human. Human OSM can bind to gp130 and recruit OSM Receptor β or LIF Receptor β to form a ternary complex. OSM stimulates the growth of different types of cells, including megakaryocytes, fibroblasts, vascular endothelial cells, and T cells. On the other hand, OSM inhibits the proliferation of several cancer cell lines, such as solid tissue tumor cells, lung cancer cells, melanoma cells, and breast cancer cells.

Oncostatin M (OSM) is a multifunctional cytokine, and belongs to Interleukin-6 (IL-6) subfamily, which also includes IL-11, leukemia inhibitory factor (LIF), ciliary neurotropic factor, cardiotrophin-1, and novel neurotropin-1. In vivo, OSM is secreted from activated T cells, monocytes, neutrophils, and endothelial cells. OSM is related to LIF, and shares a receptor with LIF in human. Human OSM can bind to gp130 and recruit OSM Receptor β or LIF Receptor β to form a ternary complex. OSM stimulates the growth of different types of cells, including megakaryocytes, fibroblasts, vascular endothelial cells, and T cells. OSM inhibits the proliferation of several cancer cell lines, such as solid tissue tumor cells, lung cancer cells, melanoma cells, and breast cancer cells.

Oncostatin M (OSM) is a multifunctional cytokine, and belongs to Interleukin-6 (IL-6) subfamily, which also includes IL-11, leukemia inhibitory factor (LIF), ciliary neurotropic factor, cardiotrophin-1, and novel neurotropin-1. In vivo, OSM is secreted from activated T cells, monocytes, neutrophils, and endothelial cells. OSM is related to LIF, and shares a receptor with LIF in human. Human OSM can bind to gp130 and recruit OSM Receptor β or LIF Receptor β to form a ternary complex. OSM stimulates the growth of different types of cells, including megakaryocytes, fibroblasts, vascular endothelial cells, and T cells. OSM inhibits the proliferation of several cancer cell lines, such as solid tissue tumor cells, lung cancer cells, melanoma cells, and breast cancer cells.

OX40 (TNFRSF4, CD134) is a member of the tumor necrosis factor (TNF) receptor superfamily that regulates T cell activity and immune responses. The OX40 protein contains four cysteine rich domains, a transmembrane domain, and a cytoplasmic tail containing a QEE motif. OX40 is primarily expressed on activated CD4+ and CD8+ T-cells, while the OX40 ligand (OX40L, TNFSF4, CD252) is predominantly expressed on activated antigen presenting cells. The engagement of OX40 with OX40L leads to the recruitment of TNF receptor-associated factors (TRAFs) and results in the formation of a TCR-independent signaling complex. One component of this complex, PKCθ, activates the NF-κB pathway. OX40 signaling through Akt can also enhance TCR signaling directly. Research studies indicate that the OX40L-OX40 pathway is associated with inflammation and autoimmune diseases. Additional research studies show that OX40 agonists augment anti-tumor immunity in several cancer types.

OX40 is a T cell co-stimulatory molecule of the TNF receptor superfamily that coordinates with other co-stimulators (CD28, CD40, CD30, CD27 and 4-1BB) to manage the activation of the immune response. Tumor necrosis factor ligand superfamily member 4 (TNFSF4) is also known as glycoprotein Gp34, OX40 ligand (OX40L), TAX transcriptionally-activated glycoprotein 1 and CD252, which belongs to the tumor necrosis factor family. TNFSF4 is the ligand for CD134 and is expressed on cells such as DC2s (a subtype of dendritic cells) enabling amplification of Th2 cell differentiation. OX40 is constitutively expressed on Tregs and enhances the sensitivity of Tregs to IL-2, thus promoting Treg proliferation. OX40 has also shown to decrease the cells’ immunosuppressive activity on effector T cells. OX40-OX40 Ligand signaling is involved in allergic airway inflammation, graft-versus-host disease and autoimmune disease.

Microtubule associated protein tau is a neuronal microtubule-associated protein found predominantly in brain. Abnormal phosphorylation of tau is involved in the pathogenesis of Alzheimer’s disease (AD). The tau protein phosphorylated at threonine 181 (p-tau181) is a promising diagnostic biomarker for AD.

Pregnancy-associated plasma protein A (PAPP-A) is a high molecular weight protein. htPAPP-A is a protein complex which comprises of two PAPP-A subunits and two proform of eosinophil major basic protein. It exists in the blood of pregnant woman. dPAPP-A is a htPAPP-A dimmer which is composed of two PAPP-A subunits. htPAPP-A serves as a useful marker for the diagnosis of Down syndrome (DS).

Pregnancy-associated plasma protein A (PAPP-A) is a high molecular weight protein. htPAPP-A is a protein complex which comprises of two PAPP-A subunits and two proform of eosinophil major basic protein. It exists in the blood of pregnant woman. dPAPP-A is a htPAPP-A dimmer which is composed of two PAPP-A subunits. htPAPP-A serves as a useful marker for the diagnosis of Down syndrome (DS).

PCT, a 116 amino acid (aa) protein, is comprised of three sections including a 57 aa N-terminal PCT, a 32 aa calcitonin and a 21 aa katacalcin. Calcitonin is a hormone, derived from PCT cleavage. PCT is a good diagnosis marker for bacterial infection. Other diseases such as sepsis, inflammation, surgery, heat shock, burn injuries and cardiogenic shock can also cause an increase of PCT level in blood.

PCT, a 116 amino acid (aa) protein, is comprised of three sections including a 57 aa N-terminal PCT, a 32 aa calcitonin and a 21 aa katacalcin. Calcitonin is a hormone, derived from PCT cleavage. PCT is a good diagnosis marker for bacterial infection. Other diseases such as sepsis, inflammation, surgery, heat shock, burn injuries and cardiogenic shock can also cause an increase of PCT level in blood.

PCT, a 116 amino acid (aa) protein, is comprised of three sections including a 57 aa N-terminal PCT, a 32 aa calcitonin and a 21 aa katacalcin. Calcitonin is a hormone, derived from PCT cleavage. PCT is a good diagnosis marker for bacterial infection. Other diseases such as sepsis, inflammation, surgery, heat shock, burn injuries and cardiogenic shock can also cause an increase of PCT level in blood.

PCT, a 116 amino acid (aa) protein, is comprised of three sections including a 57 aa N-terminal PCT, a 32 aa calcitonin and a 21 aa katacalcin. Calcitonin is a hormone, derived from PCT cleavage. PCT is a good diagnosis marker for bacterial infection. Other diseases such as sepsis, inflammation, surgery, heat shock, burn injuries and cardiogenic shock can also cause an increase of PCT level in blood.

Programmed Cell Death Protein 1 (PD-1), is cell surface receptor expressing on T cells and pro-B cells. The binding of PD-1 to its two ligands, PD-L1 and PD-L2, could result in down-regulation of the immune system by inhibiting the T-cell activation process. Thus, PD-1 is an important immune checkpoint and a popular target for therapeutic antibodies against many cancers.

Programmed cell death protein 1, also known as PD-1 and CD279 (cluster of differentiation 279) or PDCD1, is a protein that in humans is encoded by the PDCD1 gene. PD-1 is a cell surface receptor that belongs to the immunoglobulin superfamily and is expressed on T cells and pro-B cells.PD-1 binds two ligands, PD-L1 and PD-L2. PD-1 and its ligands play an important role in down regulating the immune system by preventing the activation of T-cells, which in turn reduces autoimmunity and promotes self-tolerance. The inhibitory effect of PD-1 is accomplished through a dual mechanism of promoting apoptosis (programmed cell death) in antigen specific T-cells in lymph nodes while simultaneously reducing apoptosis in regulatory T cells (suppressor T cells)

Programmed cell death protein 1, also known as PD-1 and CD279 (cluster of differentiation 279) or PDCD1, is a protein that in humans is encoded by the PDCD1 gene. PD-1 is a cell surface receptor that belongs to the immunoglobulin superfamily and is expressed on T cells and pro-B cells.PD-1 binds two ligands, PD-L1 and PD-L2. PD-1 and its ligands play an important role in down regulating the immune system by preventing the activation of T-cells, which in turn reduces autoimmunity and promotes self-tolerance. The inhibitory effect of PD-1 is accomplished through a dual mechanism of promoting apoptosis (programmed cell death) in antigen specific T-cells in lymph nodes while simultaneously reducing apoptosis in regulatory T cells (suppressor T cells).

Programmed death (PD-1) is an immunoinhibitory receptor that belongs to the CD28 family and is expressed on T cells, B cells, monocytes, natural killer cells, and many tumor-infiltrating lymphocytes (TILs); PD-1 is a type I membrane protein of 268 amino acids and which structure includes an extracellular IgV domain followed by a transmembrane region and an intracellular tail. The intracellular tail contains two phosphorylation sites located in an immunoreceptor tyrosine-based inhibitory motif and an immunoreceptor tyrosine-based switch motif, which suggests that PD-1 negatively regulates TCR signals. This is consistent with binding of SHP-1 and SHP-2 phosphatases to the cytoplasmic tail of PD-1 upon ligand binding. It has 2 ligands that have been described PD-L1(B7H1) and PD-L2(B7-DC); PD-1 induction on activated T cells occurs in response to PD-L1 or L2 engagement and limits effector T-cell activity in peripheral organs and tissues during inflammation, thus preventing autoimmunity.Recombinant Human PD-1 produced in HEK293 cells is a polypeptide chain containing 149 amino acids with C-terminal 6×His. A fully biologically active molecule, rhPD-1 has a molecular mass of 30-40 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.

Programmed death-ligand 1 (PD-L1) also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7-H1), is a protein that in humans is encoded by the CD274 gene. PD-L1 is a 40 kDa type 1 transmembrane protein that has been speculated to play a major role in suppressing the immune system during particular events such as pregnancy, tissue allografts, autoimmune disease and other disease states such as hepatitis. Normally the immune system reacts to foreign antigens where there is some accumulation in the lymph nodes or spleen which triggers a proliferation of antigen-specific CD8+ T cell. The formation of PD-1 receptor / PD-L1 or B7.1 receptor /PD-L1 ligand complex transmits an inhibitory signal which reduces the proliferation of these CD8+ T cells at the lymph nodes and supplementary to that PD-1 is also able to control the accumulation of foreign antigen specific T cells in the lymph nodes through apoptosis which is further mediated by a lower regulation of the gene Bcl-2. PD-L1 binds to its receptor, PD-1, found on activated T cells, B cells, and myeloid cells, to modulate activation or inhibition. Recombinant Human PD-L1(B7-H1) Fc Chimera produced in CHO cells is a polypeptide chain containing 457 amino acids. A fully biologically active molecule, rh PD‑L1(B7-H1) has a molecular mass of 70-72 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.

Programmed death-ligand 1 (PD-L1) also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7-H1), is a protein that in humans is encoded by the CD274 gene. PD-L1 is a 40 kDa type 1 transmembrane protein that has been speculated to play a major role in suppressing the immune system during particular events such as pregnancy, tissue allografts, autoimmune disease and other disease states such as hepatitis. Normally the immune system reacts to foreign antigens where there is some accumulation in the lymph nodes or spleen which triggers a proliferation of antigen-specific CD8+ T cell. The formation of PD-1 receptor / PD-L1 or B7.1 receptor /PD-L1 ligand complex transmits an inhibitory signal which reduces the proliferation of these CD8+ T cells at the lymph nodes and supplementary to that PD-1 is also able to control the accumulation of foreign antigen specific T cells in the lymph nodes through apoptosis which is further mediated by a lower regulation of the gene Bcl-2. PD-L1 binds to its receptor, PD-1, found on activated T cells, B cells, and myeloid cells, to modulate activation or inhibition.

Programmed death-ligand 1 (PD-L1) also known as cluster of differentiation 274 (CD274) or B7 homolog 1 (B7-H1), is a protein that in humans is encoded by the CD274 gene. PD-L1 is a 40 kDa type 1 transmembrane protein that has been speculated to play a major role in suppressing the immune system during particular events such as pregnancy, tissue allografts, autoimmune disease and other disease states such as hepatitis. Normally the immune system reacts to foreign antigens where there is some accumulation in the lymph nodes or spleen which triggers a proliferation of antigen-specific CD8+ T cell. The formation of PD-1 receptor / PD-L1 or B7.1 receptor /PD-L1 ligand complex transmits an inhibitory signal which reduces the proliferation of these CD8+ T cells at the lymph nodes and supplementary to that PD-1 is also able to control the accumulation of foreign antigen specific T cells in the lymph nodes through apoptosis which is further mediated by a lower regulation of the gene Bcl-2. PD-L1 binds to its receptor, PD-1, found on activated T cells, B cells, and myeloid cells, to modulate activation or inhibition. Recombinant Human PD-L1(B7-H1) Fc Chimera produced in CHO cells is a polypeptide chain containing 457 amino acids. A fully biologically active molecule, rh PD‑L1(B7-H1) has a molecular mass of 70-72 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.

PD-L1 and PD-L2 are ligands for PD-1, a costimulatory molecule that plays an inhibitory role in regulating T cell activation in the periphery. PD-L2 also known as PD-L2, B7-DC serves as a negative and a positive regulator of T cell function. The expression and function of PD-L2 are similar to PD-L1. Both PD-L2−PD-1 and PD-L1−PD-1 signals inhibit T cell proliferation by blocking cell cycle progression but not by increasing cell death. PD-L2−PD-1 interactions are able to inhibit TCR-mediated proliferation and cytokine production in the absence of CD28 costimulation. Threshold for T cell activation may be a balance between activating signals, such as those delivered by the engagement of CD28 by B7-1 and B7-2, and inhibitory signals, mediated by engagement of PD-1 by PD-L1 and PD-L2. The structural conservation of B7-like and CD28-like receptors may reflect the distance between T cells and APCs in the immunological synapse. The PD-L−PD-1 pathway may play a key role in the induction and/or maintenance of peripheral tolerance and autoimmune disease. Because PD-L1 and PD-L2 can inhibit effector T cell proliferation and cytokine production, the PD-L−PD-1 pathway may be an attractive therapeutic target. Blocking the PD-1 pathway may enhance anti-tumor immunity, whereas stimulating this pathway may be useful for down-regulating ongoing immune responses in transplant rejection and autoimmune and allergic diseases.

Platelet-Derived Growth Factor-AA (PDGF-AA) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In chemical terms, platelet-derived growth factor is a dimeric glycoprotein composed of two A (-AA) or two B (-BB) chains or a combination of the two (-AB). The dimeric isoforms PDGF­AA, AB and BB are differentially expressed in various cell types, and their effects are mediated through two distinct receptors termed α and β. Differences exist in isoform binding to each receptor. Ingeneral, PDGF isoforms are potent mitogens for connective tissue cells including dermal fibroblasts, glial cells, arterial smooth muscle cells and some epithelial andendothelial cells. In addition to its activity as a mitogen, PDGF is chemotactic for fibroblasts, smooth muscle cells, neutrophils and mononuclear cells. PDGF-AA plays a significant role in blood vessel formation (angiogenesis).

Platelet-derived growth factor (PDGF) presenting in serum but absent from plasma was first discovered in an animal study by Lynch and co-workers in the late 1980s. It is a disulfide-linked dimer consisting of two peptides-chain A and chain B. PDGF has three subforms: PDGF-AA, PDGF-BB, and PDGF-AB. It is involved in many biological processes, including hyperplasia, embryonic neuron development, chemotaxis, and respiratory tubule epithelial cell development. The function of PDGF is mediated by two receptors (PDGFR-α and PDGFR-β).

Platelet-derived growth factor (PDGF) presenting in serum but absent from plasma was first discovered in animal study by Lynch and co-workers in the late 1980s. It is a disulfide-linked dimer consisting of two peptides-chain A and chain B. PDGF has three subforms: PDGF-AA, PDGF-BB, PDGF-AB. It is involved in a number of biological processes, including hyperplasia, embryonic neuron development, chemotaxis, and respiratory tubule epithelial cell development. The function of PDGF is mediated by two receptors (PDGFR-α and PDGFR-β).

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

Platelet-Derived Growth Factor Subunit B (PDGFB) belongs to the PDGF/VEGF growth factor family. Platelet-derived growth factor is a potent mitogen for cells of mesenchymal origin. PDGFB can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. As growth factor, it plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. It is required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. PDGFB also plays an important role in wound healing.

Platelet-Derived Growth Factor-BB (PDGF-BB) is one of five dimers (PDGF-AA, AB, BB, CC, and DD) formed by 4 different PDGF subunits. In vivo, PDGF-BB is mainly produced in heart and placenta, and predominantly expressed by osteoblasts, fibroblasts, smooth muscle cells, and glial cells. An inactive precursor of PDGF-BB is produced in the endoplasmic reticulum and then activated by a proprotein convertase after secretion. PDGF-BB functions in a paracrine manner and promotes organogenesis, human skeletal development, and wound healing. PDGF-BB also promotes angiogenesis, particularly in the presence of Fibroblast Growth Factor basic. Therefore, PDGF-BB and its related pathways are potential pharmacological targets.

PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is a 50 kDa glycoprotein produced and secreted in many tissues throughout the body. A major component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. In addition, PEDF is able to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuroprotective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recent identification of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities implicate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF also has the potential to be useful in the treatment of various angiogenesis-related diseases including a number of cancers.

Pepsinogen are aspartic proteinases, which are classified into two groups: pepsinogen I (PGI) and pepsinogen II (PGII). PGI and PGII are mainly secreted by gastric chief cells. PGI and PGII are of useful aid in diagnosing severe atrophic gastritis and stomach cancer.

Pepsinogen are aspartic proteinases, which are classified into two groups: pepsinogen I (PGI) and pepsinogen II (PGII). PGI and PGII are mainly secreted by gastric chief cells. PGI and PGII are of useful aid in diagnosing severe atrophic gastritis and stomach cancer.

Pepsinogen are aspartic proteinases, which are classified into two groups: pepsinogen I (PGI) and pepsinogen II (PGII). PGI and PGII are mainly secreted by gastric chief cells. PGI and PGII are of useful aid in diagnosing severe atrophic gastritis and stomach cancer.

Pepsinogen are aspartic proteinases, which are classified into two groups: pepsinogen I (PGI) and pepsinogen II (PGII). PGI and PGII are mainly secreted by gastric chief cells. PGI and PGII are of useful aid in diagnosing severe atrophic gastritis and stomach cancer.

Pepsinogen are aspartic proteinases, which are classified into two groups: pepsinogen I (PGI) and pepsinogen II (PGII). PGI and PGII are mainly secreted by gastric chief cells. PGI and PGII are of useful aid in diagnosing severe atrophic gastritis and stomach cancer.

Pepsinogen are aspartic proteinases, which are classified into two groups: pepsinogen I (PGI) and pepsinogen II (PGII). PGI and PGII are mainly secreted by gastric chief cells. PGI and PGII are of useful aid in diagnosing severe atrophic gastritis and stomach cancer.

Pepsinogens, aspartic proteinases, are classified into two groups, pepsinogen I (PGI) and pepsinogen II (PGII). PGI and PGII are mainly secreted by gastric chief cells. They are useful in diagnosing severe atrophic gastritis and stomach cancer.

Pepsinogens, aspartic proteinases, are classified into two groups, pepsinogen I (PGI) and pepsinogen II (PGII). PGI and PGII are mainly secreted by gastric chief cells. They are useful in diagnosing severe atrophic gastritis and stomach cancer.

Pepsinogens, aspartic proteinases, are classified into two groups, pepsinogen I (PGI) and pepsinogen II (PGII). PGI and PGII are mainly secreted by gastric chief cells. They are useful in diagnosing severe atrophic gastritis and stomach cancer.

Protein Induced by Vitamin K Absence or Antagonist-II (PIVKA-II), also known as Des-γ-carboxy-prothrombin (DCP), is an abnormal form of prothrombin. Normally, the prothrombin’s 10 glutamic acid residues (Glu) in the γ-carboxyglutamic acid (Gla) domain at positions 6, 7, 14, 16, 19, 20,25, 26, 29 and 32 are γ-carboxylated to Gla by vitamin-K dependent γ- glutamyl carboxylase in the liver and then secreted into plasma. In patients with hepatocellular carcinoma (HCC), γ-carboxylation of prothrombin is impaired so that PIVKA-II is formed instead of prothrombin. PIVKA-II is considered as is an efficient biomarker specific for HCC.

Protein Induced by Vitamin K Absence or Antagonist-II (PIVKA-II), also known as Des-γ-carboxy-prothrombin (DCP), is an abnormal form of prothrombin. Normally, the prothrombin’s 10 glutamic acid residues (Glu) in the γ-carboxyglutamic acid (Gla) domain at positions 6, 7, 14, 16, 19, 20,25, 26, 29 and 32 are γ-carboxylated to Gla by vitamin-K dependent γ- glutamyl carboxylase in the liver and then secreted into plasma. In patients with hepatocellular carcinoma (HCC), γ-carboxylation of prothrombin is impaired so that PIVKA-II is formed instead of prothrombin. PIVKA-II is considered as is an efficient biomarker specific for HCC.

Protein Induced by Vitamin K Absence or Antagonist-II (PIVKA-II), also known as Des-γ-carboxy-prothrombin (DCP), is an abnormal form of prothrombin. Normally, the prothrombin’s 10 glutamic acid residues (Glu) in the γ-carboxyglutamic acid (Gla) domain at positions 6, 7, 14, 16, 19, 20,25, 26, 29 and 32 are γ-carboxylated to Gla by vitamin-K dependent γ- glutamyl carboxylase in the liver and then secreted into plasma. In patients with hepatocellular carcinoma (HCC), γ-carboxylation of prothrombin is impaired so that PIVKA-II is formed instead of prothrombin. PIVKA-II is considered as is an efficient biomarker specific for HCC.

PCT
is a 116 amino acid (aa) protein. It is comprised of three sections of a 57 aa
N-terminal PCT, a 32 aa calcitonin and a 21 aa katacalcin. Calcitonin is a
hormone, derived from PCT cleavage. PCT is a good diagnosis marker for
bacterial infection. Other diseases such as sepsis, inflammation, surgery, heat
shock, burn injuries and cardiogenic shock can also cause an increase of PCT
level in blood.

The
progesterone is a steroid hormone which is secreted by the female reproductive
systems. Its concentration is associated with the development and regression of
the corpus luteum. The progesterone is used in evaluation of ovulation status and
assessment of the luteal phase

Progastrin-releasing peptide (ProGRP) is a stable
precursor of the gastrin releasing peptid. It is composed of GRP (residues
1–27), a cleavage site (residues 28–30), and a constant region (residues 31–98).
ProGRP is a tumor marker for the diagnosis and monitoring of small cell lung
cancer (SCLC).

Progastrin-releasing peptide (ProGRP) is a stable
precursor of the gastrin releasing peptid. It is composed of GRP (residues
1–27), a cleavage site (residues 28–30), and a constant region (residues 31–98).
ProGRP is a tumor marker for the diagnosis and monitoring of small cell lung
cancer (SCLC).

Prostaglandin E2