Spotlight on Select New Antimicrobial Innate Immune Peptides Discovered during 2015-2019
Background: Antibiotic resistance is a global issue and new antimicrobials are required.
Introduction: Antimicrobial peptides are important players of host innate immune systems that protect us from infection. Due to their ability to eliminate drug-resistant pathogens, AMPs are promising candidates for developing the next generation of antimicrobials.
Methods: The antimicrobial peptide database provides a useful tool for searching, predicting, and designing new AMPs. During 2015-2019, ~500 new natural peptides have been registered.
Results: This article highlights a select set of new AMP members with interesting properties. Teixobactin is a cell wall inhibiting peptide antibiotic, while darobactin inhibits a chaperone and translocator for outer membrane proteins. Remarkably, cOB1, a sex pheromone from commensal enterococci, restricts the growth of multidrug-resistant Enterococcus faecalis in the gut at a picomolar concentration.
A novel proline-rich AMP has been found in a plant Brassica napus. A shrimp peptide MjPen-II comprises three different sequence domains: serine-rich, proline-rich, and cysteine-rich regions. Surprisingly, an amphibian peptide urumin specifically inhibits H1 hemagglutinin-bearing influenza A virus.
Defensins are abundant and typically consist of three pairs of intramolecular disulfide bonds. However, rat rattusin dimerizes via forming five pairs of intermolecular disulfide bonds. While human LL-37 can be induced by vitamin D, vitamin A induces the expression of resistin-like molecule alpha (RELMα) in mice. The isolation and characterization of an alternative human cathelicidin peptide, TLN-58, substantiates the concept of one gene multiple peptides. The involvement of a fly AMP nemuri in sleep induction may promote the research on the relationship between sleep and infection control.
Conclusion: The functional roles of AMPs continue to grow and the general term “innate immune peptides” becomes useful. These discoveries widen our view on antimicrobial peptides and may open new opportunities for developing novel peptide therapeutics for different applications.
Description: A competitive ELISA for quantitative measurement of Porcine Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Porcine Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Porcine Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Canine Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Canine Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Canine Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rat Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rat Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rat Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Goat Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Goat Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Goat Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Mouse Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Mouse Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Mouse Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Human Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Human Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Human Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Monkey Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Monkey Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Monkey Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rabbit Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rabbit Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rabbit Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
SCP2D1 SCP2 sterol-binding domain containing 1 Human Recombinant Protein
Description: SCP2D1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (1-156 a.a) and having a molecular mass of 20.1kDa.SCP2D1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Description: A competitive ELISA for quantitative measurement of Guinea pig Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Guinea pig Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Guinea pig Sterol carrier protein 2 in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Polyclonal Sterol carrier protein 2 Antibody (internal region)
Description: A polyclonal antibody raised in Goat that recognizes and binds to Human Sterol carrier protein 2 (internal region). This antibody is tested and proven to work in the following applications:
Description: ACAT2 is a cytoplasmic enzyme which belongs to the thiolase family. ACAT2 takes part in lipid metabolism, lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. It is responsible for the synthesis of cholesteryl esters which are part of lipoproteins containing apoB. ACAT2 deficiency contributes to severe mental retardation and hypotonus.
Description: SLC3A2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 434 amino acids (206-630a.a.) and having a molecular mass of 47.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).;SLC3A2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Description: SLC51B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (57-128 a.a) and having a molecular mass of 10.7kDa.
Recombinant E.coli Outer-membrane lipoprotein carrier protein Protein, His, E.coli-10ug
Description: SLC4A4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (1-424 a.a.) and having a molecular mass of 51.5 kDa.;SLC4A4 is fused to 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Recombinant Human Kidney mitochondrial carrier protein 1, His-SUMO, E.coli-100ug
Peptide Gaussian accelerated molecular dynamics (Pep-GaMD): Enhanced sampling and free energy and kinetics calculations of peptide binding
Peptides mediate up to 40% of known protein-protein interactions in higher eukaryotes and play an important role in cellular signaling. However, it is challenging to simulate both binding and unbinding of peptides and calculate peptide binding free energies through conventional molecular dynamics, due to long biological timescales and extremely high flexibility of the peptides.
Based on the Gaussian accelerated molecular dynamics (GaMD) enhanced sampling technique, we have developed a new computational method “Pep-GaMD,” which selectively boosts essential potential energy of the peptide in order to effectively model its high flexibility. In addition, another boost potential is applied to the remaining potential energy of the entire system in a dual-boost algorithm.
Pep-GaMD has been demonstrated on binding of three model peptides to the SH3 domains. Independent 1 µs dual-boost Pep-GaMD simulations have captured repetitive peptide dissociation and binding events, which enable us to calculate peptide binding thermodynamics and kinetics.
The calculated binding free energies and kinetic rate constants agreed very well with available experimental data. Furthermore, the all-atom Pep-GaMD simulations have provided important insights into the mechanism of peptide binding to proteins that involves long-range electrostatic interactions and mainly conformational selection. In summary, Pep-GaMD provides a highly efficient, easy-to-use approach for unconstrained enhanced sampling and calculations of peptide binding free energies and kinetics.
Automatic construction of molecular similarity networks for visual graph mining in chemical space of bioactive peptides: an unsupervised learning approach
The increasing interest in bioactive peptides with therapeutic potentials has been reflected in a large variety of biological databases published over the last years.
However, the knowledge discovery process from these heterogeneous data sources is a nontrivial task, becoming the essence of our research endeavor.
Therefore, we devise a unified data model based on molecular similarity networks for representing a chemical reference space of bioactive peptides, having an implicit knowledge that is currently not explicitly accessed in existing biological databases.
Indeed, our main contribution is a novel workflow for the automatic construction of such similarity networks, enabling visual graph mining techniques to uncover new insights from the “ocean” of known bioactive peptides.
The workflow presented here relies on the following sequential steps: (i) calculation of molecular descriptors by applying statistical and aggregation operators on amino acid property vectors; (ii) a two-stage unsupervised feature selection method to identify an optimized subset of descriptors using the concepts of entropy and mutual information; (iii) generation of sparse networks where nodes represent bioactive peptides, and edges between two nodes denote their pairwise similarity/distance relationships in the defined descriptor space; and (iv) exploratory analysis using visual inspection in combination with clustering and network science techniques.
For practical purposes, the proposed workflow has been implemented in our visual analytics software tool, to assist researchers in extracting useful information from an integrated collection of 45120 bioactive peptides, which is one of the largest and most diverse data in its field.
Finally, we illustrate the applicability of the proposed workflow for discovering central nodes in molecular similarity networks that may represent a biologically relevant chemical space known to date.
131I-metaiodobenzylguanidine and peptide receptor radionuclide therapy in pheochromocytoma and paraganglioma
Purpose of review: Pheochromocytomas and paragangliomas are rare tumors arising, respectively, from the adrenal medulla and extra-adrenal sympathetic or parasympathetic paraganglia. The main therapeutic objectives in case of metastatic disease are the reduction of tumor burden and the control of symptoms resulting from excessive catecholamine secretion.
Treatment choices constitute not only a wait and see attitude, locoregional approaches, chemotherapy regiments but also radiopharmaceutical agents, and they should be discussed in a specialized multidisciplinary board. This review will briefly discuss the radiopharmaceutical modalities in patients with pheochromocytomas and paragangliomas (I-MIBG and PRRT).
Recent findings: I-MIBG (Azedra) has received FDA approval for patients with iobenguane-scan-positive, unresectable, locally advanced or metastatic pheochromocytomas and paragangliomas who require systemic anticancer therapy, whereas peptide receptor radionuclide therapy using radiolabelled somatostatin analogues is currently performed in compassionate use, with very promising results.
No prospective head-to-head comparison between the modalities has been conducted to date.
Summary: Promising results have been reported for both radiopharmaceutical agents, mostly in the setting of retrospective series. No prospective head-to-head comparison between the modalities is yet available.
Description: This gene encodes alpha-fetoprotein, a major plasma protein produced by the yolk sac and the liver during fetal life. Alpha-fetoprotein expression in adults is often associated with hepatoma or teratoma. However, hereditary persistance of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the alpha-fetoprotein and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. Alpha-fetoprotein is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of alpha-fetoprotein in amniotic fluid is used to measure renal loss of protein to screen for spina bifida and anencephaly. [RefSeq]
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. The yolk sac and the liver produce AFP during fetal life. AFP expression in adults is often associated with hepatoma or teratoma. However, hereditary persistence of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the AFP and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. AFP is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of AFP in amniotic fluid is used to measure renal loss of protein to screen for spinal bifida and anencephaly.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. The yolk sac and the liver produce AFP during fetal life. AFP expression in adults is often associated with hepatoma or teratoma. However, hereditary persistence of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the AFP and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. AFP is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of AFP in amniotic fluid is used to measure renal loss of protein to screen for spinal bifida and anencephaly.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. The yolk sac and the liver produce AFP during fetal life. AFP expression in adults is often associated with hepatoma or teratoma. However, hereditary persistence of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the AFP and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. AFP is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of AFP in amniotic fluid is used to measure renal loss of protein to screen for spinal bifida and anencephaly.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. The yolk sac and the liver produce AFP during fetal life. AFP expression in adults is often associated with hepatoma or teratoma. However, hereditary persistence of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the AFP and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. AFP is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of AFP in amniotic fluid is used to measure renal loss of protein to screen for spinal bifida and anencephaly.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP) (ISOBM TD-2 workshop). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP) (ISOBM TD-2 workshop). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP) (ISOBM TD-2 workshop). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP) (ISOBM TD-2 workshop). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: This antibody recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as Alpha fetoprotein (AFP). The AFP antibody is highly specific and shows no cross-reaction with other oncofetal antigens or serum albumin. Alpha fetoprotein is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. AFP antibody has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: This antibody recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as Alpha fetoprotein (AFP). The AFP antibody is highly specific and shows no cross-reaction with other oncofetal antigens or serum albumin. Alpha fetoprotein is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. AFP antibody has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: This antibody recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as Alpha fetoprotein (AFP). The AFP antibody is highly specific and shows no cross-reaction with other oncofetal antigens or serum albumin. Alpha fetoprotein is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. AFP antibody has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: This antibody recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as Alpha fetoprotein (AFP). The AFP antibody is highly specific and shows no cross-reaction with other oncofetal antigens or serum albumin. Alpha fetoprotein is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. AFP antibody has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Human Alpha fetoprotein (AFP) purified protein control for Western blot
Description: Alpha-fetoprotein is a major plasma protein produced by the yolk sac and the liver during fetal life. This protein is thought to be the fetal counterpart of serum albumin, and the alpha-fetoprotein and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4.
Description: Alpha-fetoprotein (AFP) is a major plasma protein produced by the yolk sac and the liver during fetal life. Alpha-fetoprotein expression in adults is often associated with hepatoma or teratoma. However, hereditary persistance of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the alpha-fetoprotein and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. Alpha-fetoprotein is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of alpha-fetoprotein in amniotic fluid is used to measure renal loss of protein to screen for spina bifida and anencephaly.
Description: AFP, also called Alpha-fetoprotein, is a protein that in humans is encoded by the AFP gene. It is mapped to 4q13.3. The level of AFP in amniotic fluid is used to measure renal loss of protein to screen for spina bifida and anencephaly. In rodents AFP binds estradiol to prevent the transport of this hormone across the placenta to the fetus. The main function of this is to prevent the virilization of female fetuses. Moreover, it has an important role as a diagnostic marker, especially in certain tumors and liver diseases of childhood. AFP is also used to test the potential usefulness of plasma alpha fetoprotein determination as a diagnostic marker in biliary atresia, hepatitis, and yolk sac derived tumours.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: It recognizes an oncofetal glycoprotein with a single chain of 70kDa, which is identified as alpha fetoprotein (AFP). This mAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. AFP is normally synthesized in the liver, intestinal tract, and yolk sac of the fetus. Antibody to AFP has been shown to be useful in detecting hepatocellular carcinomas (HCC) and germ cell neoplasms, especially yolk sac tumors.
Description: A Monoclonal antibody against Human AFP / Alpha Fetoprotein. The antibodies are raised in Mouse. This antibody is applicable in WB and IHC-P, E
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human AFP / Alpha Fetoprotein . This antibody is tested and proven to work in the following applications:
Description: A monoclonal antibody for detection of AFP alpha 1 Fetoprotein from Human. This AFP alpha 1 Fetoprotein antibody is for WB, IHC-P, IF. It is affinity-purified from mouse ascites by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in mouse by using as an immunogen synthetic peptide
Description: A monoclonal antibody for detection of AFP alpha 1 Fetoprotein from Human. This AFP alpha 1 Fetoprotein antibody is for WB, IHC-P, IF. It is affinity-purified from mouse ascites by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in mouse by using as an immunogen synthetic peptide
