Epitope prediction based on random peptide library screening has become a focus as a promising method in immunoinformatics research. Some novel software and web-based servers have been proposed in recent years and have succeeded in given test cases. However, since the number of available mimotopes with the relevant structure of template-target complex is limited, a systematic evaluation of these methods is still absent. In this study, a new benchmark dataset was defined. Using this benchmark dataset and a representative dataset, five examples of the most popular epitope prediction software products which are based on random peptide library screening have been evaluated. Using the benchmark dataset, in no method did performance exceed a 0.42 precision and 0.37 sensitivity, and the MCC scores suggest that the epitope prediction results of these software programs are greater than random prediction about 0.09-0.13; while using the representative dataset, most of the values of these performance measures are
Based on years of experience in phage display technology, Creative Biolabs now is able to provide services for the construction and screening of immune antibody library.. With years of research and development in the past decades, phage display has been a powerful technology to display millions or even billions of different peptides or proteins. It is now a common choice for the studies of protein-protein, protein-peptide and protein-DNA interactions. Among all the applications of phage display technology, one of the most successful ones is the isolation of monoclonal antibodies utilizing large capacity phage antibody libraries.. Thanks to the rapid development of this technology, it has become a reliable tool for the production of monoclonal antibody with high specificity and affinity. Compared with conventional hybridoma technology, the generation of immune antibody libraries is not limited by the requirement of fusion partners. This expands the possibility to develop monoclonal antibodies ...
Having been researching in the field of phage display technology for years, Creative Biolabs is able to offer a series of comprehensive phage display library screening services by its own biopanning strategies and enhanced equipments.. Phage display technology is one of the major approaches applied in various protein interaction studies, especially in the discovery of specific antibodies, scaffolds and ligands. As binders with the desired specificity generally exist at low frequencies in the constructed libraries, phage display library screening has become an effective technique for the enrichment and identification of binders with high affinity and specificity from interested libraries.. Libraries from customized library construction services, in-house premade antibody libraries, peptide libraries or scaffold libraries, libraries provided by clients and other commercialized libraries can all be screened in Creative Biolabs.. No matter its purified or unpurified targets, we can screen for ...
This paper reports the synthesis and screening of a combinatorial peptide library for new affinity ligands for glycosylated haemoglobin (HbA(1c)), which is an important indicator of diabetes control. The new ligands are suitable for large-scale synthesis and overcome the disadvantages of antibodies (unstable and expensive to produce etc.), while remaining as efficient as antibodies in binding to the analyte. The library consisted of 262 144 hexapeptides synthesised using the one-bead-one-compound technique. The hexapeptides attached onto beads were screened with glycosylated haemoglobin HbA(1c). The structures of the peptides exhibiting high affinity were characterised by Edman microsequencing. Computer modelling simulation of one of the lead sequences has shown that this class of ligand has a high affinity and specificity for glycosylated haemoglobin. (C) 1998 Elsevier Science S.A. All rights reserved.. ...
Since the advent of phage display technology, dating back to 1985, antibody libraries displayed on filamentous phage surfaces have been used to identify specific binders for many different purposes, including the recognition of tumors. Phage display represents a high-throughput technique for screening billions of random fusion antibodies against virtually any target on the surface or inside cancer cells, or even soluble markers found in patient serum. Many phage display derived binders targeting important tumor markers have been identified. Selection directed to tumoral cells surfaces lead to the identification of unknown tumoral markers. Also the improvement of methods that require smaller amounts of cells has opened the possibility to use this approach on patient samples. Robust techniques combining an antibody library displayed on the phage surface and protein microarray allowed the identification of auto antibodies recognized by patient sera. Many Ab molecules directly or indirectly targeting
0054]Other methods, such as preparation of random peptide libraries or epitope libraries are well known in the art and may be used to reproducibly produce antigens. E.g., J. K. Scott & G. P. Smith, Searching for Peptide Ligands with an Epitope Library, 249 Science 386 (1990); J. J. Devlin et al., Random Peptide Libraries: A Source of Specific Protein Binding Molecules, 249 Science 404-406 (1990); S. E. Cwirla et al., Peptides on Phage: A Vast Library of Peptides for Identifying Ligands, 87 Proc. Natl Acad. Sci. USA 6378-6382 (1990); K. S. Lam et al., A New Type of Synthetic Peptide Library for Identifying Ligand-binding Activity, 354 Nature 82-84 (1991); S. Cabilly, Combinatorial Peptide Library Protocols (Humana Press, 304 pp, 1997); U.S. Pat. No. 5,885,780. Such libraries may be constructed by ligating synthetic oligonucleotides into an appropriate fusion phage. Fusion phages are filamentous bacteriophage vectors in which foreign sequences are cloned into phage gene III and displayed as part ...
TY - JOUR. T1 - Peptide mimotopes of oncoproteins as therapeutic agents in breast cancer.. AU - Ashok, B. T.. AU - David, L.. AU - Chen, Y. G.. AU - Garikapaty, V. P.. AU - Chander, B.. AU - Kanduc, D.. AU - Mittelman, A.. AU - Tiwari, R. K.. PY - 2003/4. Y1 - 2003/4. N2 - Generation of an immune response to oncoproteins can lead to a cancer specific protective immunity. Several such oncoproteins are being examined as tumor targets with mixed results. We are evaluating the clinical utility of synthetic peptides that would mimic the antigen immunologically and elicit a tumor specific immune response. HER-2/neu, an oncoprotein whose expression in breast cancer is associated with poor prognosis, lower disease free-survival and a propensity for metastases was chosen as a model. Antibodies, Ab2, Ab4 and Ab5 directed towards the extracellular domain of HER-2/neu were reacted to peptides from two synthetic phage display peptide libraries, LX-8 (12-mer peptide library containing disulfide bridge) and ...
TY - JOUR. T1 - Identification of peptide mimotopes of gp96 using single-chain antibody library. AU - Shanmugam, Arulkumaran. AU - Suriano, Robert. AU - Goswami, Neha. AU - Chaudhuri, Devyani. AU - Ashok, Badithe T.. AU - Rajoria, Shilpi. AU - George, Andrea L.. AU - Mittelman, Abraham. AU - Tiwari, Raj K.. N1 - Funding Information: Acknowledgments We gratefully acknowledge the financial assistance of AVT and the National Cancer Institute RO1 grant 1RO1CA131946 (RKT).. PY - 2011/3. Y1 - 2011/3. N2 - Heat shock proteins such as gp96 are immunogenic and are widely used as vaccines in immunotherapy of cancers. The present study focuses on the use of peptide mimotopes as immunotherapeutic vaccines for prostate cancer. To this end, we developed a 15-mer gp96 peptide mimotope specifically reactive to MAT-LyLu gp96-peptide complex using combinatorial single-chain antibody and peptide phage display library. The immunogenicity of the synthesized gp96 mimotope was analyzed initially in normal BALB/c mice ...
Rx Biosciences offers construction and screening of custom bacterial display libraries of small peptides. The library is useful in ligand discovery, antibody-antigen binding affinity study and identification of targets. Libraries of polypeptides displayed on the surface of bacteria are screened using flow cytometry or routinely used selection procedures (biopanning). The library is created by combining a highly diverse collection of synthetically-constructed randomized peptide sequences using a unique proprietary technique. The library has been specifically optimized to eliminate unwanted stop codons and aggregation-prone sequences. As in a phage display, the peptides the bacterial display peptides are expressed at the surface (plasma membrane) as a conjugated protein. The expression of the peptides is inducible.. We accept customer supplied vectors also and the customer owns the exclusive rights.. ...
628 Nasopharyngeal carcinoma (NPC) is one of the most common cancers among Chinese living in South China, Taiwan and Singapore. For treatment of NPC, although radiotherapy, surgical removal, and chemotherapy have been applied for decades and the 5 year survival rate in the advanced cases are still below 75 %. Much effort using other methods such as high dose chemotherapy plus bone marrow stem cell injection and other targeting therapy are needed to control this cancer. In the present experiment, we used random peptide phage display libraries to identify and isolate a specific novel peptide from NPC cell line for targeting drug delivery. After subtraction with control epithelial cells for 3 times, the remained phage libraries were biopanning on NPC-TW04 cells for 5 rounds. It was found that 44 selected phage clones could specifically bind to NPC cell surface. When ELISA was used to verify those clones, 16 phage clones showed higher affinity to NPC cells and were subjected to DNA sequencing. The ...
Two phage-displayed random peptide libraries were screened for ligands with potential inhibitory activity against pancreatic phospolipase A2 or ammodytoxin C (neurotoxin found in the venom glands of Vipera ammodytes ammodytes). The interaction of selected peptides with pancreatic phospholipase A2 and ammodytoxin C was confirmed with surface plasmon resonance and phage ELISA assays. Interestingly, peptides showed equal affinity to both proteins, regardless which of the two proteins was used as a target in the selection procedure. Despite pronounced affinity, none of the synthetic peptides inhibited enzyme targets in vitro at the concentrations below 167 [micro]M ...
TY - JOUR. T1 - Automated panning and screening procedure on microplates for antibody generation from phage display libraries. AU - Turunen, Laura. AU - Takkinen, Kristiina. AU - Söderlund, Hans. AU - Pulli, Timo. PY - 2009. Y1 - 2009. N2 - Antibody phage display technology is well established and widely used for selecting specific antibodies against desired targets. Using conventional manual methods, it is laborious to perform multiple selections with different antigens simultaneously. Furthermore, manual screening of the positive clones requires much effort. The authors describe optimized and automated procedures of these processes using a magnetic bead processor for the selection and a robotic station for the screening step. Both steps are performed in a 96-well microplate format. In addition, adopting the antibody phage display technology to automated platform polyethylene glycol precipitation of the enriched phage pool was unnecessary. For screening, an enzyme-linked immunosorbent assay ...
Our libraries developed from precision DNA fragments have enabled us to generate a peptide phage display system with unmatched complexity.
We plan to do some fishing into a random peptide library and would like to know the experience of those that have used constrained peptides vs unconstrained peptides. Are peptides that are removed from their constrained vectors likely to still function in an unconstrained context? ie is the greater likelyhood of getting a hit on the constrained library offset by the potential lack of function when the peptides are subsequently used unconstrained? -- Scott Vande Pol Case Western Reserve University Department of Pathology Cleveland Oh. 44106 sbv at pop.cwru.edu ...
A peptide library is a tool for protein-related study. A peptide library contains a great number of peptides that have a systematic combination of amino acids. Usually, peptide library is synthesized on solid phase, mostly on resin, which can be made as flat surface or beads. The peptide library provides a powerful tool for drug design, protein-protein interactions, and other biochemical as well as pharmaceutical applications. You can create a mix of desired amino acids at each point in a sequence. In this way, you could create a library of 20 different polypeptides with only one amino acid residue at random and the rest being the same. The usefulness of this form of peptide synthesis is limited as you cant go beyond 70 acids in length. This would give you 2070 possible combinations and thats only if you dont include the plethora of available amino acids with pre-installed post-translational modifications. Most drug development does not involve such a random assortment of proteins as you ...
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The interaction between a CD4+ TH cell and an antigen presenting cell (APC) is a finely tuned event in adaptive immunity. The affinity is dictated by the T cell receptor (TCR) and the characteristics of antigenic peptide epitopes presented on the major histocompatibility complex class II (pMHC class II) molecules on APCs. Due to the high degree of polymorphism in MHC molecules and the vast repertoire of epitopes that may be presented on each, it is an immense challenge to predict epitopes relevant to disease and homeostasis. It would therefore be of very high value to develop a technology that allows for precise experimental identification of T cell epitopes in the absence of any prior knowledge of the relevant antigen, as long as one has access to T cells. We have developed a novel and generic combinatorial display system for MHC class II, based on phage display. Using phage display, one can probe an epitope sequence space orders of magnitude larger than any cellular or chemical system. As a ...
article{c02feb63-0c75-498d-9b63-6043d6df0ab2, abstract = {Background: Phage Display technology is a well established technique for high throughput screening of affinity ligands. Here we describe a new compact chromato-panning procedure for selection of suitable binders from a phage peptide display library. Results: Both phages and E. coli cells pass non-hindered through the interconnected pores of macroporous gel, so called cryogel. After coupling a ligand to a monolithic cryogel column, the phage library was applied on the column and non-bound phages were washed out. The selection of strong phage-binders was achieved already after the first panning cycle due to the efficient separation of phage-binders from phage-non-binders in chromatographic mode rather than in batch mode as in traditional biopanning procedures. E. coli cells were applied on the column for infection with the specifically bound phages. Conclusion: Chromato-panning allows combining several steps of the panning procedure ...
With the success of the human genome project, the focus of life science research has shifted to the functional and structural analyses of proteins, such as the fields of proteomics and structural genomics. These analyses of proteins, including newly identified proteins, are expected to contribute to the identification of therapeutically applicable proteins for various diseases. Thus, pharmacoproteomic-based drug discovery and the development of protein therapies has currently attracted a great deal of attention (1, 2, 3) . However, it is clinically difficult to use most bioactive proteins, such as tumor necrosis factor-α (TNF-α), as antitumor agents because of their very low stability and pleiotropic action in vivo (4 , 5) .. TNF-α was reported to exert a strong cytotoxicity to various kinds of tumor cells but not to normal cells in vitro and to cause hemorrhagic necrosis of certain transplanted solid tumors (6) . Thus, TNF-α has been considered a promising new drug for cancer therapy. On ...
The product of the HER2/Neu oncogene is a receptor tyrosine kinase that is amplified in 25-30% of human primary breast tumors. In this project? we have isolated the HER2/Neu kinase from Sf9 cells infected with a baculovirus expression vector. We probed the substrate specificity of the HER2/Neu kinase using two peptide libraries: (1) a soluble peptide library containing three degenerate positions N-terminal to tyrosine; and (2) a bead-supported combinatorial library possessing sis degenerate positions at P - 1, P - 2, P - 3, P + 1, P + 2, and P + 3. We identified four novel substrate sequences for HER2/Neu from the two peptide libraries. We synthesized these peptides as individual sequences and measured steady-state kinetic properties for phosphorylation by HER2/Neu. One of the peptides, AAEEIYAARRG, is the best synthetic peptide substrate reported to date for HER2/Neu. All of the sequences bear a resemblance to sites of autophosphorylation on HER2/Neu and related epidermal growth factor (EGF) ...
Directed evolution is a powerful method for engineering of specific affinity proteins such as antibodies and alternative scaffold proteins. For selections from combinatorial protein libraries, robust and high-throughput selection platforms are needed. An attractive technology for this purpose is cell surface display, offering many advantages, such as the quantitative isolation of high-affinity library members using flow-cytometric cell sorting. This thesis describes the development, evaluation and use of bacterial display technologies for the engineering of affinity proteins. Affinity proteins used in therapeutic and diagnostic applications commonly aim to specifically bind to disease-related drug targets. Angiogenesis, the formation of new blood vessels from pre-existing vasculature, is a critical process in various types of cancer and vascular eye disorders. Vascular Growth Factor Receptor 2 (VEGFR2) is one of the main regulators of angiogenesis. The first two studies presented in this thesis ...
Directed evolution is a powerful method for engineering of specific affinity proteins such as antibodies and alternative scaffold proteins. For selections from combinatorial protein libraries, robust and high-throughput selection platforms are needed. An attractive technology for this purpose is cell surface display, offering many advantages, such as the quantitative isolation of high-affinity library members using flow-cytometric cell sorting. This thesis describes the development, evaluation and use of bacterial display technologies for the engineering of affinity proteins.. Affinity proteins used in therapeutic and diagnostic applications commonly aim to specifically bind to disease-related drug targets. Angiogenesis, the formation of new blood vessels from pre-existing vasculature, is a critical process in various types of cancer and vascular eye disorders. Vascular Growth Factor Receptor 2 (VEGFR2) is one of the main regulators of angiogenesis. The first two studies presented in this thesis ...
Cell panning of phage-displayed antibody library is a powerful tool for the development of therapeutic and imaging agents since disease-related cell surface proteins in native complex conformation can be directly targeted. Here, we employed a strategy taking advantage of an integrated vector system which allows rapid conversion of scFv-displaying phage into scFv-Fc format for efficient cell-based scFv library selection on a tetraspanin protein, CD9. A mouse scFv library constructed by using a phagemid vector, pDR-D1 was subjected to cell panning against stable CD9 transfectant, and the scFv repertoire from the enriched phage pool was directly transferred to a mammalian cassette vector, pDR-OriP-Fc1. The resulting constructs enabled transient expression of enough amounts of scFv-Fcs in HEK293E cells, and flow cytometric screening of binders for CD9 transfectant could be performed simply by using the culture supernatants. All three clones selected from the screening showed correct CD9-specificity. They
LifeTein Peptide Library: SARS-CoV-2 Receptor Binding Domain, 4 Fragments [LT-V013] - Overlapping Peptide Library: The SARS-CoV-2 Receptor Binding Domain is divided in to 4 fragments of 20 amino acids per peptide. The resulting overlapping peptide libraries can then be used for processes including continuous and linear epitope mapping, antibody screening and characterization. Reference 1: A highly conserved cryptic epitope in the receptor-binding
Heparan sulfate (HS) binds and modulates the transport and activity of a large repertoire of regulatory proteins. The HS phage display antibodies are powerful tools for the analysis of native HS structure in situ; however, their epitopes are not well defined. Analysis of the binding specificities of a set of HS antibodies by competitive binding assays with well defined chemically modified heparins demonstrates that O-sulfates are essential for binding; however, increasing sulfation does not necessarily correlate with increased antibody reactivity. IC50 values for competition with double modified heparins were not predictable from IC50 values with corresponding singly modified heparins. Binding assays and immunohistochemistry revealed that individual antibodies recognize distinct epitopes and that these are not single linear sequences but families of structurally similar motifs in which subtle variations in sulfation and conformation modify the affinity of interaction. Modeling of the antibodies ...
Principal Investigator:ITOH Kunihiko, Project Period (FY):1996 - 1997, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:応用薬理学・医療系薬学
Reconstitution of a neocytokine from the first 30 aa of IL-2 is very novel in the field of peptide agonists. Recently characterized peptides, with agonist activities related to cytokines of the hemopoietin family, have consisted up to this point of small mimetics of erythropoietin (EPO (28)) or thrombopoietin (29) selected by random phage display peptide libraries and a small nonpeptidyl mimic of G-CSF (30). These compounds act as full agonists in various biological assays, and their signaling pathways appear to be identical to those induced by the natural ligand, yet their amino acid sequences are not found in the primary sequence of the natural protein. The crystal structure of the 20-aa mimetic peptide of EPO and of the extracellular domain of the EPO receptor (EPOR) reveals a dimerization of the peptide that is bound to the homodimeric EPOR. In this study, it was shown that the peptide p1-30 contains a part of the native aa sequence of IL-2, forms a tetrameric structure that mimics a ...
Phage display is a method to discover peptide ligands while minimizing and optimizing the structure and function of proteins (Hallahan, 2003). The phage is used as a scaffold to display recombinant libraries of peptides and provides a means to recover and amplify the peptides that bind to putative receptor molecules in vivo. In vivo selection simultaneously provides positive and subtractive screens because organs and tissues such as tumors are spatially separated. Phage DNA can then be sequenced to determine the amino acid sequence of peptides on the capsid that have been recovered from tumors. The T7 phage display system exploits the T7 capsid protein as a scaffold to display peptides on the capsid protein unique to the 10B protein on the surface of the phage. Gene 10 encoding the capsid protein is cloned with a series of multiple cloning sites at the C-terminus of the 10B protein. The natural translational frame shift site within the capsid gene has been removed so that only a single form of ...
The aim of this work was to verify the possibility of applying affinity chromatography in bacteriophage purification, from the perspective of therapeutic purposes. Elution profiles of phages modified with specific affinity motifs (Figures 3,4,5 and 6) show substantially higher phage concentration in elution fractions compared to final washing samples. This indicates binding of modified phages to the affinity resins and effective elution with standard competitive agents. Thus, affinity tags can be successfully incorporated into the T4 phage capsid by the in vivo phage display technique and they strongly elevate bacteriophage affinity to a specific resin. Non-specific binding was also observed: unmodified phages or those modified with the non-specific tag were eluted with the titre 104-105 pfu/ml. Nevertheless, the unspecific binding is 102-105 times weaker than the specific one and importantly it does not interfere with the aim of preparation of purified anti-bacterial active bacteriophages for ...
We are leaders in the field of human antibody engineering and have been involved in many of the seminal discoveries in the field. We are experts in phage, yeast and lentivirus display platforms and panning procedures, human antibody library constructions, Fc engineering, humanization procedures and targeted siRNA delivery to name a few. We have constructed human antibody libraries with tens of billion members and have successfully isolated therapeutic human antibodies against over two dozen targets. We have also developed and utilize antibody expression systems in bacteria, mammalian, yeast and insect cells. Students and post-doctoral fellows join the Marasco lab to become skilled artisans in the field under Dr. Marascos mentorship. An overview of some of our antibody engineering tools can be found here. ...
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Abstract. Currently, novel drug design focused on the searching pharmacological compounds acting via influence on GPCRs heteromers. The strategy allows obtaining highly selective effects since these heteromers appear only on specific cells and tissues. Therefore, human monoclonal scFv antibodies able to recognizing GPCRs heteromers may constitute a valuable tool in modern therapies. Antibody phage display technique together with high throughput screening play a key role in the development of clinically useful immunomolecules. Therefore in the present work we focused on the comparison of various strategies used for biopanning process during phage display procedure, dedicated to isolation scFv antibodies specifically recognizing GPCRs heteromers. Experiments were conducted in two different cell lines (CHO-K1 and HEK 293) and six various selection procedures were described. Elimination of nonspecific bindings constitutes a key point during the process. Results obtained duing selection conducted in ...
Adamalysin-like metalloproteinases with thrombospondin (TS) motifs (ADAMTS)-5 is the multi-domain metalloproteinase that most potently degrades aggrecan proteoglycan in the cartilage and its activity is implicated in the development of osteoarthritis (OA). To generate specific exosite inhibitors for it, we screened a phage display antibody library in the presence of the zinc-chelating active site-directed inhibitor GM6001 (Ilomastat) and isolated four highly selective inhibitory antibodies. Two antibodies were mapped to react with exosites in the catalytic/disintegrin domains (Cat/Dis) of the enzyme, one in the TS domain and one in the spacer domain (Sp). The antibody reacting with the Sp blocked the enzyme action only when aggrecan or the Escherichia coli-expressed aggrecan core protein were substrates, but not against a peptide substrate. The study with this antibody revealed the importance of the Sp for effective aggrecanolytic activity of ADAMTS-5 and that this domain does not interact with sulfated
In vivo screening of phage-displayed peptide libraries has revealed extensive molecular differences in the blood vessels of individual normal tissues. Pathological lesions also put their signature on the vasculature; in tumours, both blood and lymphatic vessels differ from normal vessels. The changes that characterize tumour blood vessels include selective expression of certain integrins. Peptides isolated by in vivo phage display for homing to tumours have been shown to be useful in directing therapeutic agents to experimental tumours. The targeting can enhance the efficacy of the therapy while reducing side effects. Phage screening has also revealed lung-specific vascular markers that promote tumour metastasis to the lungs by mediating specific adherence of tumour cells to the lung vasculature. These phage-screening studies have revealed a previously unsuspected degree of vascular specialization and provide potentially useful guidance devices for targeted therapies.. ...
The display of repertoires of antibody fragments on the surface of filamentous phage offers a new way to produce immunoreagents with defined specificities. Phage derived antibody fragments offer a number of advantages over mouse monoclonal antibodies, such as better clearance from the blood, the possibility to select from human combinatorial libraries and the relative ease by which such fragments can be manipulated. The phage display technique thus facilitates the selection of antibody fragments of therapeutic value or research interest. Antibodies to M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface ...
The display of repertoires of antibody fragments on the surface of filamentous phage offers a new way to produce immunoreagents with defined specificities. Phage derived antibody fragments offer a number of advantages over mouse monoclonal antibodies, such as better clearance from the blood, the possibility to select from human combinatorial libraries and the relative ease by which such fragments can be manipulated. The phage display technique thus facilitates the selection of antibody fragments of therapeutic value or research interest. Antibodies to M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface ...
In a previous study, a scFv phage display library against white spot syndrome virus (WSSV) was constructed and yielded a clone designated A I with conformational specificity against native but not denatured viral antigen. Although the clone A1 has been used successfully as a diagnostic antibody, its precise target antigen has not been elucidated. A different strategy was adopted involving the construction of a second T7 phage display library utilizing mRNA isolated from shrimp infected with WSSV. Following RT-PCR and T7 phage library construction, phages displaying the candidate epitope were selected with A I scFv. Since successive enrichment steps were not associated with an increased titer of the phages, enrichment after successive tests was confirmed by PCR resulting in the prefer-red selection of a specific DNA sequence encoding a novel nucleocapsid protein WSSV388. Immune electron microscopy revealed that WSSV388 is located on the nucleocapsid. This result demonstrated that unknown antigen ...
558117PRTArtificial Sequenceisolated from phage display libraries 1Ser Ser His Lys His Pro Val Thr Pro Arg Phe Phe Val Val Glu Ser 1 5 10 15Arg222PRTArtificial Sequenceisolated from phage display libraries 2Ser Ser Cys Asn Cys Tyr Val Thr Pro Asn Leu Leu Lys His Lys Cys 1 5 10 15Tyr Lys Ile Cys Ser Arg 20322PRTArtificial Sequenceisolated from phage display libraries 3Ser Ser Cys Ser His Asn His His Lys Leu Thr Ala Lys His Gln Val 1 5 10 15Ala His Lys Cys Ser Arg 20422PRTArtificial Sequenceisolated from phage display libraries 4Ser Ser Cys Asp Gln Asn Asp Ile Phe Tyr Thr Ser Lys Lys Ser His 1 5 10 15Lys Ser His Cys Ser Arg 20522PRTArtificial Sequenceisolated from phage display libraries 5Ser Ser Ser Ser Asp Val Tyr Leu Val Ser His Lys His His Leu Thr 1 5 10 15Arg His Asn Ser Ser Arg 20622PRTArtificial Sequenceisolated from phage display libraries 6Ser Ser Ser Asp Lys Cys His Lys His Trp Tyr Cys Tyr Glu Ser Lys 1 5 10 15Tyr Gly Gly Ser Ser Arg 20714PRTArtificial Sequenceisolated from phage display ...
We have recently identified peptide mimetics of the Cryptococcus neoformans capsular polysaccharide by screening phage display peptide libraries. 2H1, one of a large family of mAbs against the glucuronoxylomannan fraction (GXM), is highly protective and binds several peptide motifs. This study analyzes the immunologic properties of P601E (SYSWMYE), a peptide from the low affinity motif (W/YXWM/LYE) that has an extended cross-reactivity among anti-GXM mAbs and whose binding correlates with the protective potential of mAbs in experimental infection. P601E is a mimetic, since it competes for GXM binding to 2H1, but not a mimotope, since it does not elicit an anti-GXM response. Sequence analysis of 14 anti-P601E mAbs indicates that anti-P601E mAbs elicited in BALB/c mice have an order of homology with 2H1 of V kappa | J kappa || V(H) | J(H) | D. Further screening of a peptide library with anti-P601E mAbs isolated peptides having a motif almost identical to the peptide motif selected by 2H1. When these
The one-bead-one-compound (OBOC) combinatorial peptide library is a powerful tool to identify ligand and receptor interactions. Here, we applied the OBOC library technology to identify mimotopes specific to the immunoglobulin E (IgE) epitopes of the major shellfish allergen tropomyosin. OBOC peptide libraries with 8-12 amino acid residues were screened with serum samples from patients with shellfish allergy for IgE mimotopes of tropomyosin. Twenty-five mimotopes were identified from the screening and their binding reactivity to tropomyosin-specific IgE was confirmed by peptide ELISA. These mimotopes could be divided into seven clusters based on sequence homology, and epitope mapping by EpiSearch of the clustered mimotopes was performed to characterize and confirm the validity of mimotopes. Five out of six of the predicted epitopes were found to overlap with previously identified epitopes of tropomyosin. To further confirm the mimicry potential of mimotopes, BALB/c mice were immunized with ...
Methods Rat antiserum, raised against a 60-70 kDa band of partially purified GnSAF, was immobilised on anti-rat IgG Dynabeads. In addition, a human antibody, derived from a phage display antibody library and expressed by CHO-K1 cells, was immobilised on protein L agarose beads. Both antibodies were then used for 15 consecutive immunopurification steps with excess human granulosa-luteal cell-conditioned medium (GCM). In both cases 2 M NaI was used to elute the bound GCM proteins. The eluted fractions were bioassayed for GnSAF and inhibin bioactivities and the proteins separated by 1-D and 2-D gel electrophoresis. Spots and bands of interest were excised from the gels and identified by mass spectroscopic peptide mass mapping ...
Porcine parvovirus (PPV) is the major causative agent in a syndrome of reproductive failure in swine. Much has been learned about the structure and function of PPV in recent years, but nothing is known about the epitopes of the structural protein VP1, which is an important antigen of PPV. In this study, the monoclonal antibody C4 against VP1 of PPV was prepared and was used to biopan a 12-mer phage peptide library three times. The selected phage clones were identified by ELISA and then sequencing. The amino acid sequences detected by phage display were analyzed, and a mimic immuno-dominant epitope was identified. The epitope of VP1 is located in the N-terminal and contains the role amino acid sequence R-K-R. Immunization of mice indicated that the phage-displayed peptide induces antibodies against PPV. This study shows that peptide mimotopes have potential as alternatives to the complex antigens currently used for diagnosis of PPV infection or for development of vaccines.
Dr. Marilena Hall received her B.S. in Chemistry in 1992 from McGill University in Montreal, Canada. She then earned her Ph.D. at the California Institute of Technology (NSERC Fellowship) where she worked in the laboratory of Dr. Jacqueline K. Barton. Her thesis involved the design of a synthetic deoxyribonuclease using a chimera of a DNA-binding rhodium complex and a short Zn2+ -coordinating peptide.. From 1998-2000, Dr. Hall carried out post-doctoral research at New England Biolabs in Beverly, MA creating an artificial bifunctional intein capable of both protein splicing and homing endonuclease activity. During her post-doc, she was also an adjunct professor at Massasoit Community College, teaching general chemistry from 1999-2000. Professor Hall joined the Stonehill Department of Chemistry in the Fall of 2000.. Professor Halls research program employs peptide phage display libraries to identify short peptides that can mimic the coordination of Zn2+ in zinc-containing metalloenzymes.. Several ...
The blood-brain barrier (BBB) is a biological barrier that protects the brain from neurotoxic agents and regulates the influx and efflux of molecules required for its correct function. This stringent regulation hampers the passage of brain parenchyma-targeting drugs across the BBB. BBB shuttles have been proposed as a way to overcome this hurdle because these peptides can not only cross the BBB but also carry molecules which would otherwise be unable to cross the barrier unaided. Here we developed a new high-throughput screening methodology to identify new peptide BBB shuttles in a broadly unexplored chemical space. By introducing d-amino acids, this approach screens only protease-resistant peptides. This methodology combines combinatorial chemistry for peptide library synthesis, in vitro models mimicking the BBB for library evaluation and state-of-the-art mass spectrometry techniques to identify those peptides able to cross the in vitro assays. BBB shuttle synthesis was performed by the ...
Mimotopes online peptide superstore provides custom peptide synthesis, peptide library synthesis and peptide reagents for immunology, drug discovery, bioassay development, epitope mapping, proteomics, target discovery and lead optimization.
Peptides , SARS-CoV2,COVID-19 Peptides , 96-well Overlapping Peptide Library; Specifications: Spike glycoprotein from SARS-CoV-2: NCBI the RefSeq (YP_009724390.1) of 1273 aa Peptide length: 15 aa, 9aa for the C-terminal peptide. Gross peptide weight: not quantified Synthesis scale: 5 mol Offset number: 7 aa Format: lyophilized in 96-well plate (P-DW-20-C Axygen ) Counter ion: TFA QC validation: MALDI-TOF QC on 10 % of peptidesCoronavirus Spike glycoproteins mediate the virus attachment to host cell surface receptors and facilitate the virus entry by assisting fusion between viral and host cell membranes. They are composed of two subunits, S1 and S2. The Spike protein of SARS-CoV-2 harbors furin cleavage sites, one being located at the boundary between S1 and S2.
Press Release issued Oct 16, 2017: Persistence Market Research (PMR), in its latest report, projects that the global antibody library technologies market revenue will increase at a CAGR of 4.4% between 2016 and 2024. Some of the latest antibody library design and selection methods enable easy identification of any MAB with any specificity, which is why pharmaceutical companies are increasingly making use of such technologies in their facilities.
Specifying 14-3-3: A fragment-based combinatorial peptide microarray generates affinity-based fingerprints of seven mammalian 14-3-3 isoforms. High-affinity motifs are identified against the highly homologous isoforms. Putative 14-3-3σ-specific peptides were also delineated by a dual-color ratiometric screening strategy (see picture). (Figure Presented) © 2008 Wiley-VCH Verlag GmbH & Co. KGaA ...
Monoclonal antibodies developed for therapeutic or diagnostic purposes need to demonstrate highly defined binding specificity profiles. Engineering of an antibody to enhance or reduce binding to related antigens is often needed to achieve the desired biologic activity without safety concern. Here, we describe a deep sequencing-aided engineering strategy to fine-tune the specificity of an angiopoietin-2 (Ang2)/vascular endothelial growth factor (VEGF) dual action Fab, 5A12.1 for the treatment of age-related macular degeneration. This antibody utilizes overlapping complementarity-determining region (CDR) sites for dual Ang2/VEGF interaction with KD in the sub-nanomolar range. However, it also exhibits significant (KD of 4 nM) binding to angiopoietin-1, which has high sequence identity with Ang2. We generated a large phage-displayed library of 5A12.1 Fab variants with all possible single mutations in the 6 CDRs. By tracking the change of prevalence of each mutation during various selection ...
TY - JOUR. T1 - Heat-shock proteins as dendritic cell-targeting vaccines - getting warmer. AU - McNulty, Shaun. AU - Colaco, Camilo. AU - Blandford, Lucy. AU - Bailey, Christopher. AU - Baschieri, Selene. AU - Todryk, Stephen. PY - 2013. Y1 - 2013. N2 - Heat-shock proteins (hsp) provide a natural link between innate and adaptive immune responses by combining the ideal properties of antigen carriage (chaperoning), targeting and activation of antigen-presenting cells (APC), including dendritic cells (DC). Targeting is achieved through binding of hsp to distinct cell surface receptors and is followed by antigen internalization, processing and presentation. An improved understanding of the interaction of hsp with DC has driven the development of numerous hsp-containing vaccines, designed to deliver antigens directly to DC. Studies in mice have shown that for cancers, such vaccines generate impressive immune responses and protection from tumour challenge. However, translation to human use, as for ...
Along with the immunizations been completed by ICA, Creative Biolabs was contracted by Virbac to discovery specific monoclonal antibodies through its Magic™ Antibody Discovery Platform. To meet the specific requirement of this project, Creative Biolabs adopted its advanced advanced phage display technology using extracted RNA sent from ICA to construct an immune antibody library for specific antibody isolation. This one-stop service covers phage display library construction, biopanning, single clone validation, DNA sequencing and quality control to discover specific antibodies against the interested antigen in the monoclonal format. A simple sketch of this process is shown below.. About Creative Biolabs. Creative Biolabs is a professional service provider in developing highly specific, high-affinity monoclonal antibodies from all popular antibody production species, including rabbit, chicken, llama, camel, alpaca, cow, dog, mouse, rat, sheep, monkey, human, and even shark. Creative Biolabs ...
Factor Xa subsite mapping by proteome-derived peptide libraries improved using WebPICS, a resource for proteomic identification of cleavage ...
Dr. Scott received her PhD for work on the germline immunoglobulin V genes. She attended medical school with the goal of becoming an academic biomedical researcher. Her postdoctoral research included projects to analyze the spectra of mutational hot-spots (W.G. Thilly), the development of the first phage-displayed peptide libraries and their use in analyzing antibody specificity (G.P. Smith) and in developing peptide mimics of a discontinuous protein epitope (E.D. Getzoff & J.A. Tainer). She began working at SFU in 1993 as an Assistant Professor in the Dept. of Chemistry and Member of the Institute of Molecular Biology & Biochemistry at SFU. (The Institute became a Department in SFUs Faculty of Science in 2001.) Dr. Scott was promoted to Associate Professor in 1998 and to Professor in 2002. In 2004, Dr. Scott began a joint appointment in the newly-formed Faculty of Health Sciences, as one of its founding faculty members. That year, she was awarded a Canada Research Chair in Molecular ...
CD28 is one of the key molecules for co-stimulatory signalling in T cells. Here, novel ligands (affibodies) showing selective binding to human CD28 (hCD28) have been selected by phage display technology from a protein library constructed through combinatorial mutagenesis of a 58-residue three-helix bundle domain derived from staphylococcal protein A. Analysis of selected affibodies showed a marked sequence homology and biosensor analyses showed that all investigated affibodies bound to hCD28 with micromolar affinities (K-D). No cross-reactivity towards the related protein human CTLA-4 could be observed. This lack of cross-reactivity to hCTLA-4 suggests that the recognition site on hCD28 for the affibodies resides outside the conserved MYPPPYY motif. The apparent binding affinity for hCD28 could be improved through fusion to an Fc fragment fusion partner, resulting in a divalent presentation of the affibody ligand. For the majority of selected anti-CD28 affibodies, in co-culture experiments ...
Rx Biosciences provides quality custom phage display library construction and screening services for biological research and drug discovery related projects. The gene of interest is randomly mutated to produce various combinations of the peptides or small antibodies [e.g. scFv and Fab] or proteins which get displayed on the surface of a filamentous phage [M13, fd, and f1 strains] as fusion proteins. Using a binding affinity-based process called panning; a small number of phages that display proteins specifically binding to a target of interest are recovered from the phage library that usually has a repertoire of many billions of unique displayed proteins. Finally, the proteins displayed by the selected phages are identified by phage amplification followed by DNA sequencing.. ...
Combinatorial protein engineering, taking advantage of large libraries of protein variants and powerful selection technology, is a useful strategy for developing affinity proteins for applications in biotechnology and medicine. In this thesis, two small affinity proteins have been subjected to combinatorial protein engineering to improve or redirect the binding. In two of the projects, a three-helix protein domain based on staphylococcal protein A has been used as scaffold to generate so called Affibody molecules capable of binding to key proteins related to two diseases common among elderly people.. In the first project, Affibody molecules were selected using phage display technology for binding to Ab-peptides, believed to play a crucial role in Alzheimers disease, in that they can oligomerize and contribute to the formation of neural plaques in the brain. The selected Affibody molecules were found to efficiently capture Ab from spiked human plasma when coupled to an affinity resin. The ...
Video articles in JoVE about sequence homology include Genetic Manipulation in Δku80 Strains for Functional Genomic Analysis of Toxoplasma gondii, Creating and Applying a Reference to Facilitate the Discussion and Classification of Proteins in a Diverse Group, Optimization and Comparative Analysis of Plant Organellar DNA Enrichment Methods Suitable for Next-generation Sequencing, Identification of Rare Bacterial Pathogens by 16S rRNA Gene Sequencing and MALDI-TOF MS, Targeted in Situ Mutagenesis of Histone Genes in Budding Yeast, Phage Phenomics: Physiological Approaches to Characterize Novel Viral Proteins, Assessment of DNA Contamination in RNA Samples Based on Ribosomal DNA, Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates, Forward Genetics Screens Using Macrophages to Identify Toxoplasma gondii Genes Important for Resistance to IFN-γ-Dependent Cell Autonomous Immunity, Purifying the Impure:
mAbs. Col-1, an immunoglobulin G (IgG)-2a mAb, was purchased from Zymed. The isotype control IgG2a was obtained from Sigma and used as a control antibody.. Phage library and biopanning. Three successive rounds of biopanning with the anti-CEA antibody Col-1 were done with two pIII-display peptide phage libraries: CL10 and LL9. CL10 expresses cysteine-flanked decapeptides circularized by disulfide bridges and LL9 comprises nine linear peptides. The libraries were applied separately or pooled for biopannings. They were kindly provided by Prof. Dr. Luca Mazzucchelli (University of Bern, Bern, Switzerland; ref. 18). Biopannings were done as outlined in ref. 19, with slight modifications. In short, ELISA plates (Nunc) were coated with 40 μg/mL Col-1 in bicarbonate buffer (pH 8.5). Wells were blocked with PBS/1% dry milk and incubated with an aliquot of the phage library (∼5 × 1010 phage particles) in PBS/1% dry milk/0.1% Tween 20 at 37°C and 4°C for 1 h each. Unbound phage particles were removed ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
The subject invention provides novel and advantageous methods for identifying amino acid sequences in random peptide libraries that can bind to Gag polypeptides. The subject invention also establishes a novel in vitro system that can be used to test competitive inhibitors of retrovrial capsid assembly. Also provided are peptides, and compositions containing these peptides, which are inhibitors of the retrovirus Gag protein(s) function. Chimeric Gag polypeptides are also provided.
The designing, synthesizing and screening of one-bead-one-compound (OBOC) combinatorial chemistry libraries against a single target ligand has been well developed. Recently, novel cholesterol/peptide hybrid combinatorial One-Bead-One-Compound (OBOC) combinatorial libraries have been developed and synthesized with self folding capabilities. The library design strategy was based on a similar pentamer and hexamer self-folding branched tricylic libraries previously developed. The cholic acid on the side chain of the carboxyl lysine is believed to interact with fixed hydrophobic amino acids at the amino-termini (position 5) of the twin branched L-amino acid arms and self-fold into a tricyclic molecule. The newly synthesized library has arginine (R) and Lysine (K) down-proportioned to 10 % for each position to decrease the probability of positive charge nonspecific binding. Thirty L-, D-, and unnatural amino acids were used in each position as building blocks. Hydrophobicity was fixed at position 5 ...
In this study of diverse antibody libraries, the authors demonstrate that by targeting different residues of the same antibody gene, it is possible to create sublibraries with distinct profiles in terms of the number and affinities of the library clones against different-sized antigens. Apparent affinities for anti-streptavidin clones were measured on the BLItz system using Streptavidin biosensors.
TY - JOUR. T1 - Identification of anti-CA125 antibody responses in ovarian cancer patients by a novel deep sequence-coupled biopanning platform. AU - Frietze, Kathryn M.. AU - Roden, Richard B.S.. AU - Lee, Ji Hyun. AU - Shi, Yang. AU - Peabody, David S.. AU - Chackerian, Bryce. N1 - Funding Information: K.M. Frietze was supported by a University of New Mexico Cancer Center Postdoctoral Matching Grant. This study was funded, in part, by NIH grant R01AI083305 to B. Chackerian. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.. PY - 2016/2. Y1 - 2016/2. N2 - High-grade epithelial ovarian cancer kills more women than any other gynecologic cancer and is rarely diagnosed at an early stage. We sought to identify tumor-associated antigens (TAA) as candidate diagnostic and/or immunotherapeutic targets by taking advantage of tumor ...
Evolutionary processes, and specifically selection-based mechanisms, have long served to inspire in vitro methods for generating proteins and nucleic acids that mediate functions of interest. Examples going back two decades include the development of phage display methods (Scott and Smith, 1990) and methods based on selection of RNA molecules (Ellington and Szostak, 1990; Tuerk and Gold, 1990) from libraries of enormous structural diversity (as many as1010 distinct molecular structures). A recent review (Dreier and Plückthun, 2011) provides a sense of what can be accomplished with one these methods, ribosome display, in terms of generating macromolecules, such as antibody fragments, with desired functional properties (e.g., high-affinity binding to a target molecule).. However, these methods typically involve repeated and somewhat tedious interventions by the investigators to progress from one round of molecular variant generation and selection to the next. The overall process can be quite ...
PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.
Plant Cell Environ., 38: 375-384, 2015. Full text Arabidopsis thaliana root cell wall proteomics: increasing the proteome coverage using a combinatorial peptide ligand library and description of unexpected Hyp in peroxidase amino acid sequences. ...
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Abstract: The design of compounds that form cytotoxic, non-mutagenic 3-methyladenine adducts in pancreatic ß-cells is being studied in this project for potential applications in the treatment of diseases such as diabetes and cancer. These compounds are composed of three components: 1) a cell-targeting moiety, glucosamine, which targets the insulin producing pancreatic ß-cells by way of the GLUT-2 transporters present on these cells 2) a site-specific DNA methylating agent, Me-Lex, which has been shown to selectively produce cytotoxic, non-mutagenic N3- methyladenine adducts 3) a linker component that connects the two other components together. The linker is a critical component because it has to be such that the cell-targeting and DNAmethylating properties of the two functional components are maintained. A synthetic route was explored, which enables the easy introduction of various linkers into the molecules. Fluorescent compounds were also designed to bind weakly to DNA at the same positions ...
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Although peptides are well recognised biological molecules in vivo, their selection from libraries is challenging because of relative low affinity whilst in linear conformation. We hypothesized that multiplexed peptides and DNA on the surface of beads would provide a platform for enhanced avidity and the selection of relevant peptides from a library (ORBIT bead display). Using human immunodeficiency virus (HIV-1) gp120 as a target, we identify peptides that inhibit HIV-1 replication in vitro through blocking of protein:protein interaction with the co-receptor CCR5. The bead display approach has many potential applications for probing biological systems and for drug lead development.
Antibody building blocks stuck together with bacterial superglue can protect against bunyaviruses, and herald a new approach to developing antibodies to fight emerging viruses.
The Lippincott Interactive Anesthesia Library on CD-ROM Version 3.0 : The Lippincott Interactive Anesthesia Library on CD-ROM Version 3.0 Pub Da
Reaxense Inc - a one-stop for comprehensive product range in medicinal chemistry, small molecule screening and drug discovery. We offer personalised custom synthesis, fragment libraries, focused and targeted libraries, custom synthesis and chemical sourcing.
TY - JOUR. T1 - Rapid simultaneous screening for DNA integrity and antigen specificity of clones selected by phage display. AU - Fischer, P.. AU - Leu, S. J.C.. AU - Yang, Y. Y.. AU - Chen, P. P.. N1 - Copyright: Copyright 2004 Elsevier B.V., All rights reserved.. PY - 1994. Y1 - 1994. UR - http://www.scopus.com/inward/record.url?scp=0028180282&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0028180282&partnerID=8YFLogxK. M3 - Article. C2 - 7520712. AN - SCOPUS:0028180282. VL - 16. SP - 828+830. JO - BioTechniques. JF - BioTechniques. SN - 0736-6205. IS - 5. ER - ...
Do you need peptides synthesized? Peptide antigens for antibody production? Or even specialized peptide libraries? -- The UNC High Throughput Peptide Synthesis and Array Facility can help!
|p||strong|Introduction|/strong||br /|Recombinant antibody technologies have been widely used to produce various single-chain Fv or Fab antibody fragments of different specificity. The randomized combination of cloned variable heavy and light chain imm
Phage display is a convenient method to select proteins of interest based on binding affinity. Through subsequent rounds of panning and ELISA assays, protein library members with the desired binding activity are retained on the immobilized target, while the non-binding members are washed off. The bacteriophage serves as a physical link between the gene of interest and the protein product, since the latter is expressed on the coat of the phage thanks to its fusion with the gIII residue. We have recently used this technology to discover an antibody fragment (scFv), called H5, capable of selectively binding to the integrin binding domain of fibronectin (FN) under a strained configuration, typically due to forces exerted on the extracellular matrix (ECM) by cells.. FN is a highly elastic protein that forms fibers and contributes to the ECM. The elasticity of the protein is derived from the so-called type III repeats within the protein. The 9th and 10th type III repeats possess the PHSRN synergy ...
Learn information about Fab antibody fragment, covering definition, molecular weight, structure, expression, production, purification and services.
The key to preventing epidemic is the ability to diagnose the infected early to preempt further propagation. For this, Bio-Synthesis, Inc. provides primers and probes (as well as synthetic RNA control) for COVID-19 diagnosis via RT-PCR assay. For medicinal chemistry, it specializes in peptide synthesis, characterization, modification, purification to generate various peptide-based building blocks as well as pharmaceutical intermediates-in addition to peptide libraries, peptide arrays, peptidomimetics. Antibody purification, characterization/quantification, modification and labeling are also offered. It specializes in oligonucleotide modification and provides an extensive array of chemically modified nucleoside analogues (over ~200) including bridged nucleic acid (BNA). A number of options are available to label oligonucleotides (DNA or RNA) with fluorophores either terminally or internally as well as conjugate to peptides. It recently acquired a license from BNA Inc. of Osaka, Japan, for the ...
ProbesOnline for April 2010. In this issue you will find new product information for Applied Biosystems® Attune™ Acoustic Focusing Cytometer, Click-iT® Nascent RNA Capture Kit, LC3B Antibody Kit for Autophagy, BacMam 2.0 GFP Transduction Control
Protection against disease-causing pathogens, known as immunity, involves numerous cells organs, tissues and their products. To able to understand the biology of immune cells (hematopoietic cells) and their role in an immune system, we have used several different methods, including transcriptome analyses, bioinformatics, production of recombinant proteins and analyses of some of them, focusing on the granule proteases by substrate phage display.. Hematopoietic cells express surface receptors interacting with the constant region of immunoglobulins (Igs) known as Fc receptors (FcRs). These receptors play major roles in the immune system, including enhancing phagocytosis, activating antibody dependent cellular cytotoxicity and cell activation. A detailed bioinformatics analysis of FcRs reveals that the poly-Ig receptors (PIGR), FcR-like molecules and common signalling γ chain all appeared very early with the appearance of the bony fishes, and thereby represent the first major evolutionary step in ...