Peptide Products & Services
Custom Peptide Synthesis Services
Selleck Chemicals provides high quality peptide synthesis services with a success rate well above the industry standard (>98%). We also strive to provide these services at a competitive price. Since our inception in 2005, we have delivered more than 50,000 customized peptides to scientists from pharmaceutical and biotech companies, as well as universities and research institutions, and have received widespread acknowledgement for our services. As a result, we have the knowledge and expertise to offer optimal solutions to our customers.
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Modulation of AÎ² aggregation and cytotoxicity by FLN. (A) CD spectra of AÎ² monomer incubated for 7 days at 37Â°C in the absence (AÎ² aggregate) or presence of 10x FLN (FLN). (B) TEM images of 50 Î¼M of AÎ² incubated for seven days at 37Â°C in the absence of any dye (AÎ² only), or in the presence of 3x FLN. Scale bar is 100 nm. (C) Dot blot images of AÎ² aggregates formed without (AÎ² only) or with 3x and 10x FLN using OC and 4G8 antibodies. For each antibody, all samples were spotted onto one nitrocellulose membrane. Each membrane was immuno-stained with the OC or 4G8 antibody. For clearer presentation of the data, the sections of each membrane were cut and re-arranged. (D) Viability of neuroblastoma SH-SY5Y cells. Three controls (PBS buffer, AÎ² monomer, and FLN) and two AÎ² aggregates formed in the absence or presence of 3x FLN at 37Â°C for 5 days. Values represent means Â± standard deviation (nâ¥3). Values are normalized to the viability of cells administered with PBS buffer only. Two-sided Studentâs t-tests were applied to the MTT reduction data. (*; P = 0.013).
CD spectra of AÎ² monomer and preformed AÎ² aggregates. (A) CD spectra of AÎ² monomer, AÎ² aggregates formed in the absence or presence of 10x EOB or PHB for 5 days at 37Â°C. (B) CD spectra of AÎ² aggregates formed in the absence or presence of 10x EOY, ERB, or ROB for 5 days at 37Â°C.
Directed folding of peptides containing four cysteine residues to bicyclic structures. a, The two CXC motifs in peptide 9 strongly promote the formation of a fused bicyclic structure. b, The CXC motif in 10 directs the intramolecular pairing of cysteine residues to two products and does not promote the formation of peptide dimers. c, The four isolated cysteine residues in 11 oxidize to form three products in statistically expected ratios. Oligomerization of 9â11 is never observed. Disulfide pairing was established by tryptic digestion LC-MS (Supplementary Figs S6âS10). aa, amino acid.
Using an in vitro approach with purified and titrated matriptase and internally-quenched fluorescent octapeptide mimetics (IQFPs) of the consensus cleavage sequences of H1, H2, and H3 we show that, at physiological pH, matriptase was capable of cleaving both the H1 (IQSRGLFG) and H3 (KQTRGLFG) consensus cleavage sequences, whereas no cleavage was observed with the H2 (IESRGLFG) consensus sequence (Figure A). V max was 8.52 Â± 0.76 FU min-1 nmole-1 for H1 cleavage and 16.53 Â± 2.38 FU min-1 nmole-1 for H3 cleavage. Trypsin (not normally expressed in the lungs) was used as a control in this assay and our data showed that trypsin cleaved all three consensus sequences with similar efficiency (Vmax of 364.37 Â± 28.90 FU min-1 nmole-1 for H1, 312.17 Â± 52.32 FU min-1 nmole-1 for H2 and 277.13 Â± 4.11 FU min-1 nmole-1 for H3.
Cardiovascular effects of PACAP and PACAP(6â38) in the RVLM of normotensive and hypertensive rats. A and B: changes in mean arterial pressure (MAP; i), HR (ii), and percentage of sSNA (iii) before and after the administration of PACAP (A) or PACAP(6â38) (B). Arrows indicate times of drug infusion. âPBSâ indicates the period after the bilateral RVLM microinjection of PBS; âPACAPâ and âPACAP(6â38)â indicate the periods after the bilateral RVLM microinjection of PACAP or PACAP(6â38), respectively. C: comparison of maximum MAP (i), HR (ii), and percentage of sSNA responses (iii) after PACAP or PACAP(6â38). *P < 0.05; **P < 0.01; ***P < 0.001.
|High Quality at the most competitive Price:||From $1.9 per amino acid residue (aa).|
|High Success Rate:||>98%.|
|Fast Delivery Time:||2 weeks for unpurified peptides and 3 weeks for purified peptides.|
|Synthesis:||Peptides up to 100 amino acids can be synthesized.|
|Quantity:||From 5mg to kilogram scales.|
|Purities:||From Crude to >98% purity.|
|Report:||MS and HPLC results are provided for all customized peptides to ensure purity and confirmation of the identity.|
Peptide synthesis is conducted under Selleck's strict quality control processes. The typical delivery consists of lyophilized peptide of the required sequence, purity, and quantity and associated QC reports.
Customer Product Validation
"Selleckchem has performed custom peptide synthesis for us including synthesis of complex peptides. They deliver on time facilitating our research needs." ------ Angion.com
"We have ordered a fluorophore-modified peptide from Selleck with very competitive price. I am also very satisfied with the product and service. We will continue to order more produce from your company in future." ------ Chuanliu Wu, ETH Zürich, Institut f. Pharmazeut. Wissenschaften
"The one you made for us worked beautifully in our binding and dephosphorylation assays and the quick turnaround on price quotes (service)." ------ Stefan Strack, Ph.D. Associate Professor of Pharmacology, University of Iowa Carver College of Medicine