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Quote Request for Peptide Synthesis

Information Box (* For multiple peptides, please email us directly at )
Alanine Ala (A) Leucine Leu (L)
Arginine Arg (R) Lysine Lys (K)
Asparagine Asn (N) Methionine Met (M)
Aspartic Acid Asp (D) Phenylalanine Phe (F)
Cysteine Cys (C) Proline Pro (P)
Glutamic Acid Glu (E) Serine Ser (S)
Glutamine Gln (Q) Threonine Thr (T)
Glycine Gly (G) Tryptophan Trp (W)
Histidine His (H) Tyrosine Tyr (Y)
Isoleucine Ile (I) Valine Val (V)

Peptide Synthesis Price & Advantages
High quality at the most competitive price: From $2.0 per amino acid residue (aa).
High success rate: >99%.
Fast delivery time: 2 weeks for unpurified peptides and 3 weeks for purified peptides.
Synthesis: Peptides up to 121 amino acids can be synthesized.
Quantity: From 1mg to kilogram scales.
Purities: From Crude to >98% purity.
Report: MS and HPLC results are provided for all purified peptides to ensure purity and confirmation of the identity.

As a pioneer in the peptide industry, Peptide 2.0 Inc has the expertise you can rely on to produce from simple peptides to most complex and challenging molecules. With the state-of-the-art facility and an outstanding management team, Peptide 2.0 is able to provide custom peptide service with the best quality and the best value to our customers at unprecedented price from $2.00 per amino acid.
Peptide 2.0 Inc produces thousands of peptides each year for research and pre-clinical applications. Options include the synthesis of peptides from 2 to 121 amino acids in length with any number of labels and modifications including phosphorylation, acetylation, biotin, and cyclization. Heavy isotype peptides for quantitative protein measurement are available in multiple scales and formats to meet the necessary stringency of specific experiment.
Delivery time in general is in 2-4 weeks.
Modifications Includes:
  • Acetylation, acylation (e.g. lipopeptides), biotinylation and formylation
  • Amidation
  • Thioethers, hydroxyethylene isosteres, retro-inverso peptides
  • Cyclizations: single or multiple disulfide bridges, head to tail and side chain (lactam bridge, thioether)
  • Phosphorylation, sulfation and glycosylation
  • Incorporation of chromophores
  • Fluorescent dyes/fluorogenic groups
  • Fluorophore/quencher pairs
  • Conjugation to a carrier protein
  • Incorporation of D-enantiomers and unusual amino acids
  • Labeling with stable isotopes and radiolabeling
  • Introduction of C-terminal alcohol moieties
  • Introduction of C-terminal ester and thioester groups
  • Depsipeptides
  • Stabilizing modifications including PEGylation, N-methylated amino acids and reduced peptide bonds
  • Ligations
  • Hydrocarbon-stapled peptides
  • Conjugation of cytotoxic molecules
  • Incorporation of chelating moieties (DOTA, DPTA)
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