Expertise in Protein Technologies

Get ARVYS Expertise

• We integrate our expertise in protein technologies for each project to ensure project's success.
• We can monitor activity and stability of proteins during purification procedures thus minimizing presence of aggregated or denatured target protein in your preparations.
• Our instrumentation and experience allow us to develop a variety of biochemical and biophysical assays and use them for protein, peptide, and small molecule characterization.
• We reduce your cost by maximizing the activity and stability of your protein product.
• We deliver endotoxin-free active proteins for your in vivo studies.

Why Do You Need Expert Help to Purify and Characterize Proteins?

Your protein which appears as a single protein band on SDS-PAGE could be heterogeneous due to:

• Aggregated, modified or partially degraded forms of the target protein
• Other proteins with the same rate of migration on SDS-PAGE
• Products from faster growing cells which may come from incomplete clonal selection or clone modification
• Presence of highly active impurities which are not easily visualized, such as endotoxin

Heterogeneity in preparations results in the following problems:

• Presence of even small amounts of denatured or misfolded proteins may trigger further protein denaturation leading to instability during manipulations and storage
• Small impurities may contribute disproportionately to the product concentration measurements resulting in erroneous data interpretation.
• In in vivo studies, denatured protein, contaminants and endotoxin may induce unwanted biological responses
• In screening experiments, denatured protein may bind inhibitors and significantly affect K_i and IC₅₀ values

Your protein preparation may be fully or partially inactive due to:

• Failure to form a native conformation during production or renaturation procedures
• Denaturation, degradation or modification
• Alteration by protein tagging or labeling
• Shielding of an active site by contaminating ligands

Loss or alteration of functional activity results in the following problems:

• Ligand binding parameters are changed
• Larger amounts of protein have to be used
• Result consistency may be affected
• Increased contribution from background activity reduces assay window
• Biological responses are too low to be measured
• Your protein preparation may generate inconsistent and unreliable data.

Below is a selected list of peer-reviewed publications citing ARVYS Proteins as a contributor.

Inclusion above does not imply endorsement by the authors, journals, or institutions listed.