Recombinant Nauphoeta cinerea Periviscerokinin-2

Shipped with Ice Packs
In Stock

Product Specs

Form
Lyophilized powder. We will ship the format we have in stock. If you have special format requirements, please note them when ordering, and we will fulfill your request.
Lead Time
Delivery times vary depending on purchase method and location. Consult your local distributor for specific delivery times. All proteins are shipped with standard blue ice packs. For dry ice shipping, please contact us in advance; additional fees apply.
Notes
Avoid repeated freezing and thawing. Working aliquots can be stored at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening to collect contents at the bottom. Reconstitute the protein in sterile deionized water to a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on several factors: storage conditions, buffer components, storage temperature, and protein stability. Generally, the liquid form has a shelf life of 6 months at -20°C/-80°C, while the lyophilized form is stable for 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon arrival. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type is determined during manufacturing. If you require a specific tag, please inform us, and we will prioritize developing it.
Synonyms
; Periviscerokinin-2; PVK-2
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-11
Protein Length
Cytoplasmic domain
Purity
>85% (SDS-PAGE)
Species
Nauphoeta cinerea (Cinereous cockroach) (Gray cockroach)
Target Protein Sequence
GSSGLISMPR V
Uniprot No.

Target Background

Function
Mediates visceral muscle contractile activity (myotropic activity).
Protein Families
Periviscerokinin family
Subcellular Location
Secreted.

Q&A

Experimental Design for Studying Periviscerokinin-2

Q: What experimental design can be used to study the effects of recombinant Nauphoeta cinerea Periviscerokinin-2 on insect physiology? A: To study the effects of recombinant Periviscerokinin-2, researchers can use a bioassay setup similar to that described for isolating myotropins from insect perisympathetic organs. This involves using isolated muscle preparations (e.g., hyperneural muscle) to assess the peptide's myotropic activity. Additionally, injecting the peptide into insects and monitoring physiological responses such as muscle contraction or changes in metabolic activity can provide valuable insights into its biological functions .

Data Analysis and Contradiction Resolution

Q: How can researchers resolve contradictions in data when studying the effects of Periviscerokinin-2 across different insect species? A: Resolving data contradictions involves several steps:

  • Comparative Analysis: Compare the experimental conditions, including the concentration of Periviscerokinin-2 used and the specific insect species.

  • Statistical Methods: Use robust statistical methods to analyze data, considering factors like sample size and variability.

  • Literature Review: Consult existing literature on neuropeptide studies to identify potential species-specific differences in response to similar peptides .

Advanced Research Questions: Neuropeptide Evolution

Q: What insights can be gained from studying the evolutionary conservation of Periviscerokinin-2 across different insect species? A: Studying the evolutionary conservation of Periviscerokinin-2 can provide insights into the peptide's conserved functions across different species. This involves comparing the peptide sequences and their biological activities in various insects. Such studies can highlight how neuropeptide systems adapt to different ecological niches and physiological requirements .

Methodological Considerations for Neuropeptide Synthesis

Q: What methodological considerations are important when synthesizing recombinant Periviscerokinin-2? A: When synthesizing recombinant Periviscerokinin-2, it is crucial to ensure proper amidation at the C-terminus, as this is essential for its biological activity. Chemical synthesis methods should be validated by mass spectrometry and bioassays to confirm the peptide's structure and activity. Additionally, using specific ion-pairing reagents during purification (e.g., reversed-phase HPLC) can help achieve high purity .

Biological Activity and Physiological Roles

Q: What are the known biological activities and physiological roles of Periviscerokinin-2 in insects? A: Periviscerokinin-2 is known to act as a myotropic neurohormone, influencing muscle contraction in the nanomolar range. Its specific physiological roles may include regulating gut motility or other muscle-related functions within the insect body. Further research is needed to fully elucidate its roles in different physiological processes .

Transcriptomic and Peptidomic Analysis

Q: How can transcriptomic and peptidomic analyses contribute to understanding the regulation and function of Periviscerokinin-2? A: Transcriptomic analysis can help identify the genes involved in Periviscerokinin-2 synthesis and regulation, while peptidomic analysis can confirm the presence and modification of the peptide in different tissues. These approaches provide a comprehensive view of how Periviscerokinin-2 is produced and functions within the insect neuropeptidome .

Comparison with Other Neuropeptides

Q: How does Periviscerokinin-2 compare with other insect neuropeptides in terms of structure and function? A: Periviscerokinin-2 shares structural similarities with other myotropic neuropeptides but is distinct in its specific sequence and biological activity. Comparing its structure and function with other neuropeptides like adipokinetic hormones (AKHs) or diuretic hormones can provide insights into the diversity and specialization of neuropeptide systems in insects .

Future Research Directions

Q: What are some future research directions for studying Periviscerokinin-2 and its role in insect physiology? A: Future research should focus on elucidating the specific physiological roles of Periviscerokinin-2, exploring its potential applications in pest management, and investigating its evolutionary conservation across different insect orders. Additionally, studying its interactions with other hormones and signaling pathways can reveal complex regulatory networks in insects .

Example Data Table: Neuropeptide Comparison

NeuropeptideStructureBiological ActivitySpecies
Periviscerokinin-2Gly-Ser-Ser-Ser-Gly-Leu-Ile-Ser-Met-Pro-Arg-Val-NH2MyotropicNauphoeta cinerea
AKHVaried sequences, typically decapeptidesMobilizes energy reservesVarious insects
Diuretic HormoneSimilar to corticotropin-releasing factorStimulates fluid secretionLocusta migratoria

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