PepSpots™ Peptide Arrays on Cellulose
The membrane-bound peptides on PepSpots™ Peptide Arrays are synthesized directly on cellulose membranes by SPOT synthesis technology (SPOT peptide synthesis technique). SPOT synthesis is a fast and economic technique for custom peptide synthesis of hundreds of membrane peptides in parellel. SPOT peptide synthesis was developed to give rapid and low-cost access to large numbers of custom peptides.
They are used both as membrane bound peptide arrays (PepSpots™) for efficient and inexpensive antibody epitope mapping or protein-protein interaction studies and as soluble peptide libraries (Micro-Scale Peptides and PepTrack™ Peptide Libraries). PepSpots™ peptide arrays are reliable and combine an easy experimental procedure (like ELISA), inexpensive equipment needs and a highly flexible array and library formatting.
More than 100 scientific papers describing the application of this PepSpots™ peptide array technology and the hundreds of successful epitope mapping and epitope characterization projects performed at JPT over the last decade distinguish PepSpot™ peptide arrays as the method of choice for fast and reliable antibody epitope mapping and characterization.
For high troughput screening with thousands of peptides and projects with unpurified samples (e.g. serum, lysate, blood) we recommend the use of PepStar™ Peptide Microarrays. See the table below for a comparison of both technologies. Our customer support will be glad to help in case of question (email@example.com).
Comparison of PepSpots™ Peptides on Cellulose and PepStar™ Peptide Microarrays
|Peptides attached via||C-terminus||N-terminus|
|Reorder possible from same synthesis||No||Yes, up to several hundred|
|Immobilization of protein controls possible||No||Yes, up to 8 controls|
|Total incubation volume of diluted sample||Depending on number of peptides (several ml)||200 - 300 µl|
|Applicable to patient samples||Limited||Yes|
|Each peptide is displayed||1x||3x|
|Array surface||Cellulose membrane||Glass slide|
Applications for PepSpots™ Peptides on Cellulose
- Antibody epitope mapping
- Functional characterization of mapped epitopes (e.g substitutional or truncation analyses):
Which amino acids are critical for binding?
Which amino acids are so called "key-residues”?
- Characterization of protein-protein contact sites, such as:
- Protein modules involved in signal transduction processes
- Recognition sequences for heat shock proteins
Benefits of PepSpots™ Peptides on Cellulose
- Rapid, low-cost and accurate synthesis using robotics (SPOT Technology)
- Hydrophilic surface of cellulose membranes
- Minimization of unspecific hydrophobic interactions with target molecule
- Easy detection using standard ELISA protocols
Testimonials for PepSpots™ Peptides on Cellulose
"Our teams at the Vrije Universiteit Brussel deal with a wide variety of projects in different areas of applied biological sciences. For many of them we are in need of peptide related tools and services ranging from peptide libraries and highly purified peptides to peptide arrays. In our search for an integrated and reliable provider we came across JPT. Meanwhile, we are collaborating with JPT for many years and are very satisfied with the relationship which led to several well received publications. Especially, their unique array technology helped us to enhance our knowledge on different protein protein interactions such as Chaperone-substrate recognition."
Prof. Joost W.H. Schymkowitz & Prof. Frederic Rousseau, VIB Switch Laboratory, Vrije Universiteit Brussel, Belgium
Selected References for PepSpots™ Peptides on Cellulose
Optimization of the All-D Peptide D3 for Aβ Oligomer Elimination
Klein et al., PLoS One (2016) - PMID: 27105346
Solid-material-based Coupling Efficiency Analyzed with Time-of-Flight Secondary Ion Mass Spectrometry
Muenster et al, Applied Surface Science (2015)- PMID: n.a.
Development of a Rapid and Simple Immunochromatographic Assay to Identify Vibrio Parahaemolyticus
Sakata et al., J Microbiol Methods. (2015) - PMID: 26093260
Itch WW Domains Inhibit its E3 Ubiquitin Ligase Activity by Blocking E2-E3 Transthiolation
Riling et al., J Biol Chem. (2015) - PMID: 26245901
Cardiac Myosin-binding Protein C: a Potential Early Biomarker of Myocardial Injury
Baker et al., Basic Res Cardiol. (2015) - PMID: 25837837
Identification of Amyloid Beta Mid-domain Fragments in Human Cerebrospinal Fluid
Rogeberg et al., Biochimie (2015) - PMID: 25866191
Differential and Concordant Roles for PARP1 and Poly (ADP-ribose) in Regulating WRN and RECQL5 Activities
Khadka et al., Mol Cell Biol. (2015) - PMID: 26391948
Structural Differences of Amyloid-β fibrils Revealed by Antibodies From Phage Display
Droste et al., BMC Biotechnol. (2015) - PMID: 26084577
Meeting Antigen Sequence Diversity with JPT's ULTRA Peptide Library Concept
- New software tools for peptide sequence design and mass calculations
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