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Yes, standard credit cards (e.g. VISA, Mastercard) are accepted.

The minimum quantity to be ordered should be at least is 1 mg.

There is no maximum upper limit at Innopep for research. As a bulk order, custom packaging is available.

We offer discounts for large orders of a product (bulk).

Orders are shipped standard overnight or second-day via FedEx. UPS and Freight Forwarder services are available upon request at the time of order.

Dry ice is not required for the shipment of peptides. Usually, the lyophilizates packed in sealed vials are sufficiently stable to tolerate 1-2 days at ambient temperature. Upon receipt, the product should be stored at the recommended storage temperature.

Included with your shipment are:
- Commercial invoice if applicable.
- Packing list.
Analytical Datasheets (Certificates of Analysis) of the products, which can be downloaded from our homepage after having received the order, are included only on request.
All vials contain labels listing the designation and amount of product, storage temperature, safety information, and lot number.

Peptides, especially arginine- and lysine-rich peptides, can be very hygroscopic. Thus they have to be protected from humidity and handled rapidly.
Peptides should not be subjected to strong light, extreme pH-values, and oxidants.

Peptides usually are provided as lyophilizates, which tend to be hygroscopic. Adsorption of humidity will reduce the peptide content and adhered water may decrease stability. Before opening, the vial should be allowed to reach ambient temperature. Lyophilizates often “stick” due to electrostatic charging. The peptide has to be weighed out quickly and then the vial resealed.
Except for handling very short peptides or large amounts, reconstituting the peptide and aliquoting the resulting solution is preferable to weighing out.

The solubility of a peptide in a solvent or buffer is determined mainly by its polarity, which results from the amino acid composition, and its conformation.
Solubility in aqueous buffer can be expected for peptides containing a large proportion of charged amino acids. As the peptides are usually produced as trifluoroacetate salts, the basic amino acids (Arg, Lys, His) and the N-terminal amino group will be protonated. The aqueous solubility of peptides containing Asp and/or Glu can be improved by adding diluted ammonia, which will generate the ammonium salts.
DMSO (dimethyl sulfoxide) is a highly suitable solvent for dissolving non-polar peptides (peptides containing a large proportion of Ile, Leu, Val, Met, Phe, Pro, Trps), it will also disrupt aggregates. Addition of DMSO (or DMF, acetonitrile, or other highly polar water-miscible solvents) may help to reconstitute a peptide, which is scarcely soluble in water. DMSO should not be used in combination with strong acids as trifluoroacetic acid. Most peptides will dissolve in acetic acid. Cys- and Met-containing peptides require special attention to prevent oxidation of the sulfur.
Polar, uncharged amino acids as Asn, Gln, Gly, Ser, Thr facilitate reconstitution in water.
Reconstitution of peptides, especially long peptides or inner salts, may take time. Gentle warming or short repetitive sonication to accelerate dissolution is usually tolerated.

Unfortunately, the solubility of a peptide in aqueous buffer cannot be predicted just by studying the structure. However, a few clues can be deduced from the sequence: a relatively short peptide containing Lys and Arg residues will be soluble in aqueous buffers, as most basic functionalities will be protonated as trifluoroacetate salts. By contrast, “acidic” peptides containing a large proportion of Asp and Glu tend to be insoluble in aqueous buff, but they are readily dissolved by diluted ammonia, and by basic buffers.
Degassed buffers have to be used for reconstituting Cys- and Met-containing peptides. Contrary to sulfoxide formation, the oxidation of the thiol moiety is pH-dependent. Peptides containing free cysteines should be dissolved in acidic buffers.

Peptides containing a single free cysteine will be oxidized at pH>7 yielding dimers. This oxidation can be reverted. Peptides containing two or more thiol moieties yield a mixture of products upon oxidation. pH 7.5-8 is the pH optimum for disulfide bond formation. Hence, peptides containing free cysteines are best dissolved in degassed solvents, e.g. buffers pH<7, diluted acetic acid, 0.1% trifluoroacetic acid in aqueous acetonitrile. DMSO should be avoided, especially with peptide trifluoroacetates.

Basic buffers should be avoided.

For long-term storage the peptide should be kept in solid form in the deep freezer at -20 °C. For short-time storage a refrigerator (+4 °C) will suffice. Peptides should be protected from intense sunlight. Peptides containing fluorophores should be kept in the dark.

The shelf stability of peptides is sequence-dependent. Lyophilizates contain water, which may be involved in degradation reactions during storage. Peptides containing Asn, Gln, Cys, Met, Trp tend to be less stable. The stability may range from few months to years, if the peptide is kept in a tightly closed vessel at -20°C.

The stability of the aliquots may range from weeks to months. Dissolved peptides are less stable than the lyophilizates. The solutions should be aliquoted before freezing to avoid thawing-refreezing. Solution stability depends on the type of solvent and the pH (pH 5-7 is considered as optimum). Peptides containing Asn, Gln, Cys, Met, Trp, Tyr tend to be less stable. Stock solutions of peptide substrates should be prepared in dry organic solvents to avoid premature hydrolysis.

Typical degradation reactions include:
Oxidation of Met yielding the sulfoxide; Oxidation of Trp and Tyr; Oxidation of Cys to cysteic acid; Deamidation of Asn, Gln, and the C-terminal amide; Aspartimide formation; Cleavage of Asn-Pro; Pyroglutamine formation of N-terminal Gln; Dimerization of Trp and Tyr; Racemization

There could be many reasons for loss of activity, though oxidation of Met yielding the sulfoxide is a common one. The rate of sulfoxide formation is sequence-dependent. The problem can be circumvented by replacing Met with its stable isostere Nle.
Sulfotyrosine-containing peptides may lose their activity due to desulfation, Glu-containing peptides can be decarboxylated.