V5 Tag Peptide - GKPIPNPLLGLDST

V5 tag peptide is an affinity tag derived from a short epitope present in the P protein (RNA polymerase α-subunit) and non-structural V protein of the paramyxovirus Simian Virus 5 (SV5). The 14-amino-acid V5 tag sequence (GKPIPNPLLGLDST) is commonly fused to recombinant proteins to enable highly specific detection, purification, and visualization using anti V5 tag antibodies. V5 epitope tag is recognized for its reliability in protein analysis assays such as Western blotting, immunoprecipitation, and ELISA.

V5 tag peptide (CAS Nr: 922704-46-9) is synthetized by JPT Peptide Technologies, a leader in custom peptide synthesis for cancer and immunological research. It is fully characterized and optimized for researchers to achieve reproducible results in advanced molecular biology applications.

We also offer biotinylated V5 tag peptide variants for enhanced detection and capture applications. The V5 peptides provided by us are for research use only, do not use in humans!

V5 Tag Peptide - GKPIPNPLLGLDST - Specifications

• Peptide sequence: H-GKPIPNPLLGLDST-OH
• Amount: 5 mg
• Purity: Trial Grade: each peptide purified to > 90% (HPLC/MS)
• Counterion: TFA
• Delivery Format: Freeze-dried in plastic vial
• MW (average): 1421.66
• Application(s): T-cell immunity
• Condition(s)/Topic(s): Cancer
• Standard Delivery Time: 2-5 days
• CAS: 922704-46-9

Interested in other peptide affinity tags or related peptides? Explore our peptide catalog.

Research areas and applications

V5 epitope tag is widely used in molecular and cellular biology to facilitate the detection, purification, and characterization of recombinant proteins. It is broadly applied in cancer research, immunology, recombinant protein studies, and cell engineering, where precise tracking of tagged proteins is required.

Key research areas and applications include:

• Protein Expression and Localization: V5 tag peptide is widely used to track the expression, localization (subcellular or cell surface), and trafficking of fusion proteins in cells using imaging techniques such as immunofluorescence (IF/ICC) and flow cytometry.
• Protein Detection and Purification: The tag enables efficient detection and affinity purification of recombinant proteins using anti V5 tag antibody based applications such as Western blotting, ELISA-based assays, immunoprecipitation (IP), co-immunoprecipitation (Co-IP), and affinity chromatography.
• Protein-Protein Interaction Studies: It is widely used to study protein complexes and identify interacting partners involved in dynamic cellular processes through techniques such as co-immunoprecipitation.
• Membrane Protein Studies: Due to its small size, the V5 epitope tag peptide is well suited for analyzing the topology, expression, and trafficking of membrane-bound proteins and receptors, including detection of extracellular epitopes.
• Vaccine and Therapeutic Research: The peptide is being researched for its application in developing subunit vaccines (e.g., HIV-1 and tuberculosis) by enabling tracking, detection, and purification of recombinant vaccine antigens.
• Cell Engineering Applications: It can be used to monitor, purify, and characterize engineered proteins and receptors, including constructs used in cell engineering approaches such as CAR-T development.

Advantages of V5 Tag Peptide (CAS Nr: 922704-46-9)

• Minimal Structural Interference: At only 14 amino acids, the V5 peptide is small and generally does not interfere with protein folding, structure, or biological function.
• Low Background Signal: Because the V5 epitope originates from the paramyxovirus Simian Virus 5 (SV5) and is absent from mammalian cells, V5-tagged proteins can typically be detected with minimal background in mammalian expression systems.
• High Specificity and Sensitivity: High-affinity anti V5 antibodies enable sensitive and specific detection of V5-tagged proteins in techniques such as Western blotting, immunofluorescence (IF/ICC), flow cytometry, and immunoprecipitation.
• Protease Resistance: Compared with some other epitope tags (e.g., FLAG or Myc), the V5 epitope tag peptide shows relatively high resistance to proteolytic cleavage, including trypsin treatment.
• Flexible Tag Placement: The V5 tag peptide sequence can be fused to either the N- or C-terminus of recombinant proteins, allowing flexible experimental design.
• Nanobody Compatibility: V5-tagged proteins can be purified using nanobody-based affinity resins (e.g., V5-Trap), which often provide high binding efficiency and lower background in immunoprecipitation compared with conventional antibody-based approaches.
• Mild Elution Conditions: Bound proteins can be eluted using free V5 peptide, allowing recovery without harsh chemical treatments that may disrupt protein structure or protein-protein interactions.

JPT’s affinity tag peptides

One of the major setbacks in the production of recombinant proteins is the purification of the target protein from other components expressed by the organism. Therefore, recombinant proteins are usually expressed with a short peptide tag that allows for a specified subsequent affinity purification.

JPT Peptide Technologies has substantial, long-standing expertise in providing peptides in all formats, scales and modifications to the global scientific community. All our catalog peptides are provided with HPLC-MS analyses to confirm the identity and demonstrate the high quality of our peptides.

• All peptides are made in Germany
• Bulk orders or custom peptide synthesis upon request
• Provision of freeze-dried aliquots for enhanced stability
• Proven track record
• Custom peptide synthesis

Interested in V5 tag peptides?

Interested in V5 tag peptides or need assistance selecting the right product for your research? Our reliable customer support team can support you with product information, custom peptide synthesis, or modified and conjugated peptide designs. We also provide guidance on selecting the right anti V5 tag antibody for your application.

Please contact us or reach out to our scientific support team for personalized assistance. We look forward to supporting your research.