| Size | Price | Stock | Qty |
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| 1mg |
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| 5mg |
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| 10mg |
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| Other Sizes |
| Targets |
The V5 tag itself has no biological target; it serves as an affinity handle. It is recognized by the commercially available anti‑V5 antibody (e.g., clone SV5‑Pk1). The antibody binds to the peptide with high affinity (typically Kd in the low nanomolar range), allowing immunoprecipitation, Western blotting, immunofluorescence, and fluorescence‑activated cell sorting (FACS) of tagged proteins.
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| ln Vitro |
The free V5 peptide (50‑500 ng/mL) can competitively elute V5‑tagged proteins from anti‑V5 antibody affinity columns, displacing the bound protein without the need for harsh elution conditions (e.g., low pH or high salt). This allows the recovery of the eluted protein in its native, active form. In vitro, the free peptide has no intrinsic effect on cell viability or metabolism.
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| ln Vivo |
In animals, the V5 peptide itself is not used as a therapeutic. Instead, transgenic mice or other model organisms expressing a V5‑tagged protein of interest can be studied using anti‑V5 antibodies to track protein expression in tissues by immunohistochemistry or Western blotting of tissue lysates. The peptide alone is rapidly cleared by the kidneys and does not accumulate in tissues.
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| Enzyme Assay |
The V5 epitope tag peptide is typically immobilized on a solid support (e.g., CNBr‑activated Sepharose or magnetic beads) via its primary amine group. The immobilized peptide is used to affinity‑purify anti‑V5 antibodies from serum or hybridoma supernatant. Alternatively, the free peptide is used in an ELISA‑format competition assay: increasing concentrations of free V5 peptide (0.1‑100 ug/mL) are added to wells coated with the V5 peptide, followed by a fixed concentration of anti‑V5 antibody. The reduction in antibody binding is measured with an HRP‑labeled secondary antibody.
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| Cell Assay |
The cellular activity of the V5 tag peptide is only relevant after conjugation to a protein of interest. For localization studies, a plasmid encoding the V5‑tagged protein is transfected into cells (e.g., HEK‑293, HeLa, or CHO cells) using a lipid‑based reagent. After 24‑48 hours, cells are fixed with 4% paraformaldehyde, permeabilized with 0.1% Triton X‑100, and stained with a mouse anti‑V5 primary antibody (1:1000 dilution) followed by an Alexa Fluor‑488 conjugated anti‑mouse secondary antibody. The cells are then imaged by fluorescence microscopy.
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| Animal Protocol |
The peptide alone is not used in animals. However, a xenograft model can be established by injecting tumor cells expressing a V5‑tagged protein. After tumor growth, the mice are sacrificed, and the tumors are excised, lysed, and analyzed by Western blotting using anti‑V5 antibody to confirm expression of the tagged protein. This is a common control experiment to verify that the introduced gene product is expressed in vivo.
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| ADME/Pharmacokinetics |
The V5 peptide is water‑soluble due to its amino acid composition (multiple polar residues) and the TFA counterion. In the bloodstream, the free peptide is rapidly degraded by proteases (half‑life <5 minutes) and is eliminated primarily by renal filtration. The peptide does not cross the blood‑brain barrier. The TFA salt does not alter the peptide's pharmacokinetic profile.
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| Toxicity/Toxicokinetics |
The V5 tag peptide is non‑toxic at the low concentrations used in research. The TFA counterion, if present at very high concentrations (e.g., >1 mg/mL) and administered intravenously, could cause hypotension due to calcium chelation, but such amounts are never used in practice. The peptide does not cause genotoxicity, immunogenicity, or organ toxicity in standard research assays.
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| References | |
| Additional Infomation |
The V5 epitope tag is one of several commonly used epitope tags (others include HA, Myc, FLAG, and His‑tag). It was first described in the 1990s and has become a standard tool in molecular biology. The V5 epitope is recognized by well‑characterized monoclonal antibodies, and the peptide is available as a TFA salt to enhance solubility and stability in aqueous buffers. It is not approved for human therapeutic use.
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| Molecular Formula |
C64H108N16O20.C2HF3O2
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|---|---|
| Sequence |
Gly-Lys-Pro-Ile-Pro-Asn-Pro-Leu-Leu-Gly-Leu-Asp-Ser-ThrGKPIPNPLLGLDST
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| SequenceShortening |
GKPIPNPLLGLDST
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| Appearance |
White to off-white solid
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| HS Tariff Code |
2934.99.9001
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| Storage |
Powder -20°C 3 years 4°C 2 years In solvent -80°C 6 months -20°C 1 month Note: Please store this product in a sealed and protected environment, avoid exposure to moisture. |
| Shipping Condition |
Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)
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| Solubility (In Vitro) |
H2O :~100 mg/mL (~65.12 mM)
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|---|---|
| Solubility (In Vivo) |
Solubility in Formulation 1: 25 mg/mL (16.28 mM) in PBS (add these co-solvents sequentially from left to right, and one by one), Clear solution.
(Please use freshly prepared in vivo formulations for optimal results.) |
Calculation results
Working concentration： mg/mL；
Method for preparing DMSO stock solution： mg drug pre-dissolved in μL DMSO (stock solution concentration mg/mL). Please contact us first if the concentration exceeds the DMSO solubility of the batch of drug.
Method for preparing in vivo formulation:：Take μL DMSO stock solution, next add μL PEG300, mix and clarify, next addμL Tween 80, mix and clarify, next add μL ddH2O，mix and clarify.
(1) Please be sure that the solution is clear before the addition of next solvent. Dissolution methods like vortex, ultrasound or warming and heat may be used to aid dissolving.
(2) Be sure to add the solvent(s) in order.
Products are for research use only; We do not sell to patients
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