Selank Peptide | Selank 10mg
Selank Peptide is a high-purity synthetic neuropeptide engineered specifically for in vitro and in vivo laboratory research. As a synthetic analogue of the naturally occurring immunomodulatory peptide tuftsin, Selank has become a prominent subject in biochemical and life science research investigating peptide signaling pathways. This product is provided in a stable, lyophilized (freeze-dried) format to ensure molecular integrity during transport and long-term storage. It is strictly designated for laboratory research use and chemical analysis only.
Selank Peptide Specifications
| Property | Value |
| Name | Selank |
| CAS Number | 129954-34-3 |
| Peptide Sequence | TKPRPGP |
| Molecular Formula | C33H57N11O9 |
| Molecular Weight | 751.9 g/mol |
| PubChem CID | 11765600 |
| Synonyms | Selank, 129954-34-3, Selanc, Thr-Lys-Pro-Arg-Pro-Gly-Pro, TS9JR8EP1G |
| Vial Size | Selank 5mg, Selank 10mg |
| Purity (HPLC) | ≥99.0% |
Selank Key Features
- Research-Use Only: Expressly synthesized and distributed for laboratory experimentation, biochemical analysis, and in vitro or in vivo animal model testing.
- Lyophilized Peptide Format: Supplied as a highly stable freeze-dried cake or powder to preserve molecular structure and minimize degradation during shipping.
- High Chemical Purity: Manufactured utilizing advanced solid-phase peptide synthesis (SPPS) and purified via high-performance liquid chromatography (HPLC) to meet stringent laboratory standards.
- Strict Storage Requirements: Requires temperature-controlled conditions, specifically long-term storage at -20°C, to maintain optimal stability.
- Advanced Molecular Architecture: Features a modified heptapeptide structure designed to study regulatory peptide dynamics and degradation-resistant signaling analogues.
- Controlled Laboratory Handling: Formulated for precise volumetric reconstitution using sterile bacteriostatic water or laboratory-grade normal saline.
Product Overview
What is Selank?
Selank is a synthetic heptapeptide analogue structurally pertaining to the endogenous tetrapeptide tuftsin (Thr-Lys-Pro-Arg). Tuftsin is a normally happening peptide understood for its role in immunomodulatory signaling within mammalian systems. By altering the core tuftsin sequence via the enhancement of 3 amino acids to its C-terminus (Pro-Gly-Pro), molecular biologists effectively developed an extra stable compound efficient in withstanding fast enzymatic cleavage.
The resulting series, Thr-Lys-Pro-Arg-Pro-Gly-Pro, exhibits long term biochemical task in experimental settings contrasted to its moms and dad particle. This structural adjustment makes Selank Peptide a highly valued device for investigators studying peptide kinetics, receptor binding affinities, and regulative enzyme interactions.
Discovery Background and Scientific Background
The development of Selank dates back to the late 20th century at the Institute of Molecular Genes of the Russian Academy of Sciences. Scientist looked for to manufacture a steady analogue of tuftsin that can serve as a feasible structure for exploring neuropeptide characteristics and regulatory paths within organic systems. By engineering the glyproline (Pro-Gly-Pro) piece onto the terminal end of the particle, the clinical group effectively lessened the impact of aminopeptidases and carboxypeptidases– enzymes that usually break down peptides within fractions of a second.
This architectural advancement opened new doors forever science study. Over the subsequent decades, the substance has been thoroughly researched within academic and institutional labs to determine just how particular peptide series interact with endogenous biochemical systems.
Laboratory Research Context
In contemporary life science study and synthetic peptide research study, Selank functions as a primary recommendation material for exploring neuropeptide transmission and chemical degradation waterfalls. Since the compound integrates immunomodulatory-derived structures with regulatory peptide expansions, it supplies a distinct model for analyzing multi-system cellular communication.
Research designs making use of Selank Peptide emphasis mostly on its communications with various peptidase enzymes, its binding fondness to mobile membrane layers, and its security account in varied organic media. These investigations add substantially to the broader understanding of peptide synthesis optimization and molecular layout in pharmacology.
Selank in Scientific Research
Laboratory Investigations
Laboratory evaluation of Selank Peptide focuses heavily on its structural resilience and interaction dynamics. Synthetic peptide research frequently utilizes high-performance analytical tools, such as mass spectrometry and nuclear magnetic resonance (NMR) spectroscopy, to observe the peptide’s behavior under altered environmental conditions. Researchers manipulate variables such as pH, temperature, and enzyme presence to establish baseline stability profiles for the heptapeptide chain.

Neuropeptide-Related Research
As an experimental neuropeptide analogue, Selank is extensively used in research studies evaluating exactly how small-chain amino acid compounds go across mobile obstacles and affect regional signaling settings. Researchers investigate the peptide’s potential interactions with endopeptidases– the specialized enzymes responsible for inactivating regulative peptides. By observing the rate at which Selank breaks down into its constituent amino acid pieces, researchers gather valuable information relating to the safety nature of proline-rich peptide sequences.
Experimental Approach Considerations
When designing study methods involving Selank, investigators have to represent a number of technical variables:
Solvent Selection: The selection of reconstitution media (e.g., sterilized water, bacteriostatic water, or phosphate-buffered saline) can affect the final solution’s pH and ionic toughness.
Concentration Slopes: Speculative designs normally need a range of focus to properly map dose-response contours in cellular or animal models.
Adsorption Factors: Peptides normally follow typical glass and plastic laboratory vessels; making use of low-binding polypropylene vials is important for preserving precise concentration measurements.
Scientific Background
Peptide Signaling and Molecular Kinetics
Peptide signaling represents a foundational device where complicated biological microorganisms preserve interior homeostasis. Tiny chains of amino acids operate as chemical carriers, binding to specific cell-surface receptors to cause downstream intracellular waterfalls. In the context of neuropeptide research study, comprehending the architectural factors that dictate receptor fondness and metabolic half-life is a primary objective.
Artificial Peptide Study usually includes modifying normally taking place series to research the relationship between framework and feature. The addition of the Pro-Gly-Pro sequence to the tuftsin core is a timeless instance of this approach. In scientific literary works, this alteration is shown to profoundly modify the molecular kinetics of the compound, rendering it a very resistant design for researching long term peptide signaling without the instant confounding variable of quick chemical clearance.
Areas of Ongoing Investigation
Existing literary works relating to Selank Peptide continues to broaden throughout several distinctive sub-fields of life science research study:
- Enzymatic Inhibition Designs: Checking out whether Selank competes with other endogenous peptides for binding websites on degrading enzymes.
- Expression Profiling: Assessing adjustments in mobile mRNA expression adhering to direct exposure to differing focus of the peptide in controlled in vitro settings.
- Relative Peptide Characteristics: Examining the functional distinctions between Selank and other artificial tuftsin derivatives to establish the precise influence of incurable amino acid series.
Storage and Handling Standards
Correct storage and careful research laboratory handling are vital to prevent the deterioration of Selank Peptide and to keep reproducible speculative end results.
Temperature Considerations
Lyophilized Selank Peptide shows high stability at room temperature level for quick durations during transportation. However, upon arrival at the study center, lasting storage should be maintained at a continuous temperature level of -20 ° C or lower. When the peptide is reconstituted into a fluid state, its stability window reduces dramatically. Reconstituted solutions have to be kept under chilled problems at 2 ° C to 8 ° C and need to be utilized within a marked experimental window to stay clear of hydrolysis and microbial contamination.
Dampness and Light Protection
Peptides are naturally hygroscopic– indicating they conveniently soak up dampness from the surrounding environment. Direct exposure to ambient moisture can launch early degradation or change of the lyophilized matrix. Vials should continue to be hermetically sealed up until the precise moment of reconstitution. Furthermore, Selank should be protected from direct UV light exposure, which can cleave sensitive peptide bonds and compromise chemical purity.
Reconstitution Best Practices
When preparing Selank Peptide for lab analysis, the reconstitution procedure must be performed with accuracy:
Temperature Equilibration: Allow the lyophilized vial to get to space temperature before presenting the solvent. This stops condensation from developing inside the vial, which can change measurement accuracy.
Gentle Dissolution: Introduce the reconstitution solvent (such as clean and sterile bacteriostatic water) gradually down the inner wall surface of the glass vial. Do not shake the vial vigorously, as mechanical shear anxiety can denature the peptide chain. Instead, carefully swirl the vial in a round motion up until the lyophilized cake totally dissolves right into a clear, colorless solution.
Frequently Asked Questions
What is Selank?
Selank is an artificial heptapeptide developed as an analogue of the normally taking place immunomodulatory peptide tuftsin. It features an extended amino acid sequence created to boost security for research laboratory research applications.
Just how should Selank be saved?
In its lyophilized kind, Selank needs to be kept at -20 ° C for long-term conservation. Once reconstituted right into a solution, it should be kept cooled at 2 ° C to 8 ° C and used promptly to stop destruction.
What does lyophilized peptide imply?
Lyophilization is a freeze-drying procedure that eliminates water from the peptide option through sublimation. This leaves a steady powder or cake matrix that protects the structural stability of the peptide for transportation and storage space.
Is Selank intended for research study usage?
Yes. Selank Peptide is purely produced and dispersed for laboratory study, chemical evaluation, and scientific investigation. It is not intended for human or vet use.
What is peptide reconstitution?
Peptide reconstitution is the process of liquifying a lyophilized peptide powder into a fluid solvent, such as sterile water or typical saline, to prepare it for specific volumetric measurement and laboratory screening.
What is a neuropeptide?
A neuropeptide is a tiny protein-like particle made use of by neurons to communicate and signal within organic systems. They serve as chemical messengers that affect numerous mobile paths.
Why is pureness important for Selank Research Peptide?
High pureness (greater than 98%) ensures that speculative monitorings are driven completely by the Selank particle itself, eliminating confounding variables introduced by artificial by-products or chemical impurities.
Can Selank be saved in a common frost-free fridge freezer?
Criterion frost-free freezers undergo routine temperature spikes throughout their defrost cycles, which can trigger temperature variations that speed up peptide deterioration. A dedicated laboratory freezer that keeps a constant -20 ° C temperature is extremely recommended.
Research Notes
Notice: This product is classified exclusively as a research chemical. It is intended solely for laboratory experimentation, in vitro analysis, and controlled scientific testing within authorized institutional frameworks. This material is not a drug, cosmetic, food additive, or medical device, and any form of human administration or clinical application is strictly prohibited. The educational data provided on this page serves as a literature review of historical and current research trends and does not constitute technical instruction or endorsement for non-laboratory utilization.
Scientific References
For advanced study and validation of the biochemical profiles discussed, researchers are encouraged to consult resources available through the following authoritative databases and indexes:
- Peer-Reviewed Journals: Journal of Peptide Science, Regulatory Peptides, Peptides, and Bulletin of Experimental Biology and Medicine.
- Scientific Databases: The National Center for Biotechnology Information (NCBI) PubChem database, ChemSpider, and the European PubMed Central repository.
- Research Institutions: Publications and historical archives maintained by the Institute of Molecular Genetics at the Russian Academy of Sciences.
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⚠ Intended Use
All products are intended for in vitro laboratory research use only.
They are strictly prohibited for administration to humans or animals, and must not be used for diagnostic, therapeutic, or clinical applications.
Storage and Handling
Store lyophilized powder at –20°C.
After reconstitution (for laboratory analysis), store at 2–8°C.
Avoid repeated freeze-thaw cycles.
Maintain aseptic technique during handling.






