P21

Product Details – P21

P21 is a synthetic tetrapeptide composed of four amino acids linked by peptide bonds. It is derived from a fragment of ciliary neurotrophic factor (CNTF 148–151) and is structurally modified for use in controlled research environments.

In laboratory settings, P21 is utilized to investigate peptide interactions with intracellular regulatory systems, particularly those involved in cell cycle control. Its compact structure allows for consistent evaluation of molecular signaling pathways and enzyme modulation.

This compound is supplied strictly for laboratory research purposes and is not intended for consumption, medical, or diagnostic use.

Mechanism of Action

At the molecular level, P21 is studied for its role as a cyclin-dependent kinase inhibitor (CDKI). Cyclin-dependent kinases (CDKs) are enzymes that regulate progression through the cell cycle via interaction with cyclins.

P21 interacts with CDK-cyclin complexes, influencing their activity and modulating cell cycle progression. This interaction is analyzed in vitro to evaluate how CDK inhibition affects transcriptional regulation and intracellular signaling pathways associated with cell cycle control.

Additionally, P21 is investigated for its involvement in signaling networks associated with cellular regulation, including pathways linked to transcription factors and protein expression. These studies contribute to a broader understanding of peptide-mediated modulation of enzymatic activity under controlled experimental conditions.

Chemical Properties of P21

Attribute	Details
Compound Name	P21 Peptide
Classification	Synthetic tetrapeptide; CDK inhibitor
Molecular Formula	C27H42N6O8
Molecular Weight	Not specified
Synonyms	p21^Cip1 fragment; CNTF (148–151)
Primary Target	Cyclin-dependent kinases (CDKs)
Research Context	Cell cycle regulation and enzyme inhibition studies
Format	Research peptide (non-consumable)
Stability	Maintained under controlled laboratory storage conditions

Research Applications

Cell Cycle Regulation Studies

P21 is utilized in experimental systems to examine the interaction between cyclin-dependent kinases and regulatory peptides. Researchers analyze how CDK inhibition influences cell cycle progression at the molecular level.

Enzyme Inhibition Analysis

This compound is applied in studies investigating the modulation of enzyme activity, particularly within CDK-cyclin complexes. These analyses focus on intracellular signaling pathways and transcriptional regulation.

Peptide Signaling Research

P21 supports investigations into peptide-mediated signaling networks, including interactions with regulatory proteins and transcription factors. These studies contribute to a deeper understanding of cellular control mechanisms.

Why Choose BehemothLabz to Buy P21 for Research

BehemothLabz supplies research-grade P21 produced under controlled laboratory conditions with strict quality assurance protocols in place. Each batch undergoes detailed analytical verification to ensure consistency in molecular composition and purity.

In addition, comprehensive documentation, including laboratory testing reports and sourcing transparency, supports reproducibility across experimental applications. BehemothLabz maintains a compliance-focused approach, ensuring that all compounds are supplied exclusively for laboratory-based investigation and analytical research.

Disclaimer

P21 is intended strictly for laboratory research and analytical purposes only. It is not designed for diagnostic procedures, therapeutic applications, or any form of in vivo study.

All references to biochemical pathways, receptor interactions, and enzymatic processes are provided solely within a research context. This compound must be handled only by qualified professionals within controlled laboratory environments, in accordance with applicable regulations and safety standards.

Any use outside of these defined research conditions is strictly prohibited.

References

• Chung, D. L., Brandt-Rauf, P., Murphy, R. B., Nishimura, S., Yamaizumi, Z., Weinstein, I. B., & Pincus, M. R. (1991). A peptide from the GAP-binding domain of the ras-p21 protein as well as azatyrosine block ras-induced maturation of Xenopus oocytes. Biochemical and biophysical research communications, 181(3), 1378–1384. https://doi.org/10.1016/0006-291x(91)92091-w
• Mikecin, A. M., Walker, L. R., Kuna, M., & Raucher, D. (2014). Thermally targeted p21 peptide enhances bortezomib cytotoxicity in androgen-independent prostate cancer cell lines. Anti-cancer drugs, 25(2), 189–199. https://doi.org/10.1097/CAD.0000000000000036