Overview
The Biotin-Dynorphin A (1-17) Peptide Fragment is an essential tool for researchers exploring the intricate roles of dynorphins in various physiological processes. Dynorphins are a class of opioid peptides generated from the precursor protein prodynorphin. This specific peptide fragment spans amino acids 1 through 17, allowing you to study its unique interactions and effects on the Κ-opioid receptor (KOR), a critical target in pain modulation and addiction research.
Key Features
- High purity peptide suitable for research applications
- Comprised of the first 17 amino acids of Dynorphin A
- Facilitates studies on drug addiction and appetite regulation
- Available in a convenient 1 mg package
- Supports a variety of labeling and detection methods
Specifications
| Property | Details |
|---|---|
| Peptide Name | Biotin-Dynorphin A (1-17) |
| Quantity | 1 mg |
| Amino Acid Sequence | 1-17 aa |
FAQ
What are the primary applications of Biotin-Dynorphin A (1-17)?
This peptide fragment is used primarily in research investigating opioid receptor interactions, drug addiction, and appetite control. It can help scientists understand how these peptides modulate pain and other physiological responses.
How should I store this peptide?
For optimal stability, store the Biotin-Dynorphin A (1-17) peptide in a cool, dry place, preferably at -20°C. Avoid repeated freeze-thaw cycles to maintain its integrity.
Can I use this peptide for labeling experiments?
Yes, this peptide can be utilized in labeling experiments. For additional options, check out our diverse selection of peptides and consider our labeling kits for various detection techniques.
This high-quality Biotin-Dynorphin A (1-17) Peptide Fragment is a valuable addition to your research toolkit. Whether you are studying the pathways of drug addiction or the physiological roles of opioid peptides, this product will enhance your experiments. Don’t miss the chance to purchase this and other related products, like the PKG Substrate or Autocamtide-2to further your research.




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