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 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 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.
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 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 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 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 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 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 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:
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: 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: A polyclonal antibody against SCP2. Recognizes SCP2 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC; Recommended dilution: WB:1:1000-1:5000, IHC:1:20-1:200
Description: A polyclonal antibody against SCP2. Recognizes SCP2 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC; Recommended dilution: IHC:1:20-1:200
Description: A polyclonal antibody against SCP2. Recognizes SCP2 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC; Recommended dilution: WB:1:500-1:2000, IHC:1:20-1:200
Description: A polyclonal antibody against SCP2. Recognizes SCP2 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, WB
Description: Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. Recombinant human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).
Description: 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 (Nikolaidis, N.M. et al. Am. Journal Respir. Cell Mol. Biol. (2003) 4: 458-464). Recombinant human TFF2 is a 12.0 kDa polypeptide of 107 amino acid residues, which includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds.
Description: Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant human BD-2 is a 4.3 kDa protein containing 41 amino acid residues.
Description: Relaxin-2 is a peptide hormone structurally related to insulin, which is expressed in the placenta, decidua, prostate, and in the ovary during pregnancy. Of the three known relaxin genes, Relaxin-2 is the only relaxin known to circulate in the blood. Relaxin-2 binds specifically to the LGR7 and LGR8 receptors, previously identified as an “orphan” G protein coupled receptors. Signaling by Relaxin-2 through its target receptors enhances the growth of pubic ligaments and ripening of the cervix during birth. Recombinant Relaxin-2 is a nonglycosylated 6.0 kDa disulfide linked heterodimeric protein consisting of a 24 amino acid A-chain and a 29 amino acid B-chain.
Description: IL-2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions which are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant murine IL-2 is a 17.2 kDa protein, containing 149 amino acid residues.
Description: PAI-2 is an inhibitory serpin expressed mainly in keratinocytes, activated monocytes, and placental trophoblasts. It exists predominantly as a 47 kDa nonglycosylated intracellular protein which can be induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated forms of PAI-2 are equally effective as inhibitors of urokinase-type plasminogen activator (uPA), the only established physiological target of this serpin. PAI-2 has a unique ability to form dormant polymers spontaneously and reversibly under physiological conditions. The physiological relevance of this property, which is neither a consequence of any mutation in the PAI-2 gene nor associated with any known disorder, is still unclear. However, it appears that the formation of intracellular dormant polymers may be important for the controlled release of the inhibitor from PAI-2 producing cells. Plasma levels of PAI-2 are usually low or undetectable, except during pregnancy and in some forms of monocytic leukemia. Secretion of PAI-2 from the placenta normally occurs during the third trimester of pregnancy and accounts for the dramatic increase in PAI-2 levels (up to 250 ng/ml), which are maintained at these levels until postpartum, and then rapidly decline. In addition to its vital role in protecting the placenta from degradation by uPA and/or uPA-activated proteases, PAI-2 has been shown to be essential for the prevention of metastatic spread of neck, lung and breast cancers. The beneficial effect of PAI-2 seen in these studies is presumed to stem from its ability to inhibit uPA-dependent cell dissemination. PAI-2 has also been reported to inhibit keratinocyte proliferation, and to participate in the innate immune response during viral infection. Recombinant human PAI-2 is a 415-residue nonglycosylated protein.
Description: FGF basic (FGF2) is a multipotential fibroblast growth factor that stimulates and supports proliferation, migration and differentiation. Mouse FGF basic (FGF-2) Recombinant Protein is purified FGF basic (FGF-2) produced in yeast.
Description: Interleukin-2 (IL-2) is a cytokine produced by T-helper cells in response to antigenic or mitogenic stimulation. It is required for T-cell proliferation and other activities crucial to the regulation of the immune response. Chicken IL-2 Recombinant Protein is purified interleukin-2 produced in yeast.
BMP-2 Bone Morphogenetic Protein-2 Human Recombinant Protein, Monomer
Description: Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 115 amino acids (283-396) and having a molecular mass of 13009 Dalton. ;The BMP-2 is purified by proprietary chromatographic techniques.
Description: ErbB-2 Human Recombinant is a 43.4 kDa protein containing 397 amino acid residues of the human Herstatin, and an extra Methionine at N-Terminal (underlined), produced in E.coli.
IL-2 Interleukin-2 Human Recombinant Protein, His Tag
Description: Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 133 amino acids fragment (21-153) having a molecular weight of 20kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. _x000D_ The IL-2 His is purified by proprietary chromatographic techniques._x000D_
Description: This gene encodes two proteins: sterol carrier protein X (SCPx) and sterol carrier protein 2 (SCP2), as a result of transcription initiation from 2 independently regulated promoters. The transcript initiated from the proximal promoter encodes the longer SCPx protein, and the transcript initiated from the distal promoter encodes the shorter SCP2 protein, with the 2 proteins sharing a common C-terminus. Evidence suggests that the SCPx protein is a peroxisome-associated thiolase that is involved in the oxidation of branched chain fatty acids, while the SCP2 protein is thought to be an intracellular lipid transfer protein. This gene is highly expressed in organs involved in lipid metabolism, and may play a role in Zellweger syndrome, in which cells are deficient in peroxisomes and have impaired bile acid synthesis. Alternative splicing of this gene produces multiple transcript variants, some encoding different isoforms.
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: A sandwich quantitative ELISA assay kit for detection of Bovine Alpha-Fetoprotein (aFP) in samples from serum, plasma or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Bovine Alpha-Fetoprotein (aFP) in samples from serum, plasma or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Canine Alpha-Fetoprotein (aFP) in samples from serum, plasma or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Canine Alpha-Fetoprotein (aFP) in samples from serum, plasma or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Equine Alpha-Fetoprotein (aFP) in samples from serum, plasma, tissue homogenates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Equine Alpha-Fetoprotein (aFP) in samples from serum, plasma, tissue homogenates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Human Alpha-Fetoprotein (aFP) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Human Alpha-Fetoprotein (aFP) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Porcine Alpha-Fetoprotein (aFP) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Porcine Alpha-Fetoprotein (aFP) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Rat Alpha-Fetoprotein (aFP) in samples from serum, plasma, tissue homogenates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Rat Alpha-Fetoprotein (aFP) in samples from serum, plasma, tissue homogenates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Monkey Alpha-Fetoprotein (aFP) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.
Description: A sandwich quantitative ELISA assay kit for detection of Monkey Alpha-Fetoprotein (aFP) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.
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.
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: 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: AFP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 597 amino acids (19-609a.a.) and having a molecular mass of 67.3kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa)._x000D_ _x000D_ AFP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Description: Quantitativesandwich ELISA kit for measuring Mouse Alpha-fetoprotein, AFP in samples from serum, plasma, cell culture supernates, tissue homogenates, cell lysates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.
Description: Quantitativesandwich ELISA kit for measuring Mouse Alpha-fetoprotein, AFP in samples from serum, plasma, cell culture supernates, tissue homogenates, cell lysates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.
