Custom Peptide Synthesis

Please input the peptide sequence, purity, and amount in the PepBox first, then add to the shopping cart or generate a quote.

In general, there are three (3) methods of placing the order:

1. Send us a Purchase Order (PO) under the NET45 term.
2. Completing the payment with the information on the second page of the quote.
3. Confirm the order directly through a university or company email under the NET45 term.

The turnaround time may vary depending on the peptide length and the complexity of synthesis. The general calculation is peptide length/10 + 1 week. For example, for a 15-amino acid peptide, the lead time is 15/10+1=2.5 weeks.

NovoPro can ship to most countries in the world through DHL or FedEx. The universal shipping cost is 49 USD.

NovoPro accepts credit/debit cards (Visa, MasterCard, American Express), Stripe, PayPal, and wire transfers.

In most cases, peptides will be lyophilized and shipped in small microcentrifuge tubes (2 ml). For each peptide, we will provide a Certificate of Analysis (COA), Mass Spectrum (MS) data, and High Performance Liquid Chromatography (HPLC) data.

The purity of NovoPro's catalog peptides is usually about 95%, with some reaching up to 99% purity. It represents that 95% of the NET PEPTIDE content (not total peptide content, see question 10) of the dry powder is the target peptide. The impurity is usually composed of the incomplete sequences of the target peptide. Deleted sequences are generated during peptide synthesis, when, due to the slight inefficiencies of the coupling reaction, some amino acid(s) are missed. The peptide purity was determined through High Performance Liquid Chromatography (HPLC).

Depending on the specific application(s). NovoPro can synthesize peptides to >98% purity. The following table is a general guideline for peptide purity requirements:

High Performance Liquid Chromatography (HPLC) is used for purification.

It is essential to understand the difference between net peptide content and total peptide content. The dry peptide powder usually contains not only the peptide, but also some other substances such as water, absorbed solvents, counter ions, and salts. The total peptide content refers to the weight of this mixture.

Net peptide weight indicates the actual weight of the peptide component of your sample. Net peptide content is usually 50-80% of the total peptide weight (also called gross peptide weight) and is generally determined by amino acid analysis or UV spectrophotometry. Net peptide content should not be confused with purity. Purity defines the percentage of the target peptide sequence in the total peptide components.

Theoretical NPC (calculated by assuming that counterions are the only non-peptide components) can be estimated by dividing the molecular weight of the peptide by a sum of this molecular weight and several trifluoroacetate (TFA) counterions that are required to neutralize the peptide, multiplied by the molecular weight of the TFA counterion (MW=114). For example, a synthetic peptide of MW=1000 with a free N-terminal amino group and one Arg has a theoretical net peptide content of 1000/(1000 + 2 x 114) = 1000/1228 =0.81 or 81%. In practice, counterions are not the only possible contaminants in the peptide sample. It can also contain water, absorbed solvents, and traces of other substances. As a result, the actual net peptide content is usually determined by quantitative amino acid analysis.

Lyophilized peptides can be stored long-term at -20°C, or preferably -80°C. For short-term storage, a 4°C condition is sufficient for less than 4 weeks.

• Apply the suggested solution as “Dissolution condition” in the peptide's COA.
• Sonication will increase solubility.
• 10% acetic acid in the solvent will help dissolve basic peptides.
• 10% ammonium bicarbonate will help dissolve acidic peptides.
• For peptides with extremely low solubility in aqueous solutions, organic solvents (such as DMSO, isopropanol, methanol, and acetonitrile) should be used first. Once the peptides are completely dissolved, water may be gradually added until the desired concentration is obtained.

Most peptides, except those without basic amino acids (such as Arg, Lys, His), or those with blocked N-termini, exist in the form of their salts. Synthetic peptides that are HPLC-purified are usually obtained as trifluoroacetate (TFA) salts. Their basic amino acid residues and N-termini are protonated and have trifluoroacetate (CF3COO -) counterions.

For peptides with fewer than 50 amino acids, we use stepwise Solid-phase peptide synthesis (SPPS) chemical methods. For peptides with more than 50 amino acids, we use fragment condensation, native ligation, or our proprietary recombinant methods.

Each peptide has its specific characteristics, and not all outcomes can be anticipated. If something goes wrong during the synthesis and we cannot deliver your peptide on time, it is possible to adjust peptide sequences or cancel the order, which is 100% free of charge.

NovoPro can synthesize peptides of length up to 200 aa. Peptides of 50-70 aa can be obtained by direct chemical synthesis. Longer peptides can be generated by chemically linking several synthetic peptide components.

Quality assurance documentation provided with every NovoPro peptide includes Mass Spectral (MS) and High Performance Liquid Chromatography (HPLC) analyses determining composition and purity. Amino acid analysis is available upon request. We also provide storage and handling guidelines.

Peptides are synthesized from the C-terminus to the N-terminus of the sequence.

Peptide libraries are efficient tools for GPCR ligand screening, protein-protein interaction studies, functional proteomics, nucleic acid binding, enzyme substrate and inhibitor screening, antigen and epitope screening, peptide/protein cross-talk studies, the discovery of signal molecules, and other processes significant to modern drug discovery.

Currently, we do not provide cGMP-grade peptides.

We recommend placing the phosphorylated residue no more than 10 residues away from the N-terminus, as the coupling efficiency of residues following a phosphorylated residue is significantly reduced.

We recommend adding a spacer between the peptide and the dye molecule. This will reduce the chance of the dye affecting peptide folding and binding to receptors. However, if the purpose of the dye labeling is to quantify fluorescence transfer between different structures, spacers should not be introduced.

Capping will help the peptide appear more like a native protein. The N-terminus can be capped with an acetyl group, and the C-terminus with an amide group.

PEGylation adds poly (ethylene glycol) polymer to target molecules through covalent attachments. PEGylation effectively enhances the peptides' therapeutic properties by masking them from the host's immune system, increasing their solubility (for hydrophobic drugs) and bioavailability. It can also prolong the peptides' circulatory time within the host through reduced renal clearance.