Recombinant Perforin: Function, Mechanisms, and Applications


Intro
Recombinant perforin is a significant protein within the immune system. It plays an essential role in eliminating infected or malignant cells. The understanding of its structure, function, and production methods can yield new therapeutic options, especially in the realm of cancer and infectious diseases. This article seeks to explore these different aspects, providing crucial insights into how recombinant perforin can be harnessed to improve health outcomes.
The following sections will delve into research methodologies adopted in recent studies, as well as interpret findings in the context of existing literature.
Research Methodology
Description of research design and approach
The research on recombinant perforin typically adheres to a systematic approach focusing on both experimental and observational methodologies. Oftentimes, scientists utilize a variety of techniques such as molecular biology, protein purification, and functional assays to study its properties. By integrating both in vitro and in vivo methods, researchers can gain a comprehensive understanding of perforin’s role in cellular immunity.
Materials and methods used in the study
Key materials in the study of recombinant perforin include:
- Genetically modified organisms (e.g., bacteria or yeast) for protein expression.
- Specific reagents for protein purification, such as affinity chromatography.
- Experimental models to assess cytotoxic activity.
- Analytical tools like flow cytometry for cell analysis.
Through these materials and methods, researchers can generate large quantities of perfion for testing, allowing deeper investigations into its mechanism of action.
Discussion and Interpretation
Interpretation of results in the context of existing literature
Results from recent studies have shown a promising correlation between recombinant perforin and enhanced immune responses. This builds upon earlier research which highlighted the protein's potential in targeting cancer cells. Various publications support the efficacy of perforin, illustrating its capacity to facilitate apoptosis in compromised cells effectively.
Implications for future research or practical applications
The advances in recombinant perforin research present a pathway for future explorations in immunotherapy. Researchers are encouraged to concentrate on optimizing production methods further, as well as researching potential combinations with other immunotherapeutic agents, like monoclonal antibodies. The ongoing developments suggest that recombinant perforin may hold significant promise for treating cancer and infections more efficiently than traditional methods.
"Recombinant perforin could redefine therapeutic strategies in oncology and virology, opening avenues for novel treatments."
Clearly, the role of recombinant perforin in modern medicine cannot be overstated. Its study necessitates a detailed approach to ensure beneficial applications in healthcare.
Foreword to Recombinant Perforin
Recombinant perforin is a critical element in the discourse surrounding immunology and therapeutic development. Its intricate role in targeting and destroying infected or malignant cells underscores its significance. By understanding perforin, researchers can tap into its therapeutic applicability, particularly in cancer treatment and infectious disease management. This section provides foundational insights about recombinant perforin and sets the stage for a comprehensive exploration of its structure, functionality, and applications.
Definition and Overview
Recombinant perforin refers to the artificially synthesized form of perforin protein. This protein is essential in the immune response, particularly in cell-mediated cytotoxicity. Perforin itself is a pore-forming protein secreted by cytotoxic T cells and natural killer cells. It facilitates the entry of granzymes into the target cells, leading to apoptosis or programmed cell death. Recombinant versions of this protein allow for controlled studies of its properties and functions, enabling easier examination of its role in immune responses.
The advantages of recombinant perforin are substantial. For one, it allows for the mass production of purified proteins, making it feasible to use in laboratory settings and potential therapies. Furthermore, understanding its properties in a recombinant form can lead to innovations in how it is applied in various treatments.
Historical Context
The understanding of perforin dates back to the 1990s, when it was first identified as a key component in the immune system’s arsenal against infected or cancerous cells. Early research highlighted its role in granule-mediated cytotoxicity, paving the way for further investigation into its molecular structure and function.
As the field of genetic engineering evolved, so did the methodologies to produce recombinant forms of biologically active proteins. The ability to clone the perforin gene and express it in various systems, such as bacteria and yeast, marked a turning point. This facilitated not just research into its basic biology but also its application in therapeutic contexts. Advances in protein design and production have since spurred interest in its role beyond basic immunity, exploring implications in personalized medicine and innovative cancer therapies. Understanding this historical background is essential to appreciate the ongoing research and potential applications of recombinant perforin today.
"The evolution of recombinant DNA technology has provided unprecedented control over protein expression, paving pathways for novel therapeutic applications."
In summary, the introduction of recombinant perforin into the scientific discourse serves as an important milestone in immunology, particularly regarding therapeutic advancements. The continued exploration of its functions and potential applications remains a vibrant area of research that holds promise for future innovations.
Molecular Structure of Perforin
The molecular structure of perforin is integral to its function in the immune response. Understanding this structure is essential as it informs researchers about how perforin interacts with target cell membranes, ultimately leading to cell death. The arrangement of amino acids, the presence of specific domains, and the overall conformation of the protein are all critical features that determine its effectiveness in cytotoxic actions.
Perforin is synthesized as an inactive precursor. Upon activation, it forms a complex structure that allows it to associate with the cell membrane of target cells. The molecular structure is designed to facilitate the formation of pores in the target cell membrane, a critical step in its cytotoxicity. This ability to form pores is what distinguishes perforin from other cytotoxic molecules.
Key Structural Elements
Key structural elements of perforin include several important features that contribute to its membrane-targeting abilities:
- Pore-forming Domain: This region contains hydrophobic amino acids that interact with lipid bilayers, allowing perforin to insert itself into the membrane.
- Poly-Ethylene Glycol (PEG) Linker: It provides flexibility and aids in the formation of pores, crucial for the protein's function.
- Membrane-Binding Region: Specific sequences that facilitate the initial binding to the target cell, showcasing the importance of precise interactions for optimal functionality.


Each element of perforin's structure is fine-tuned to ensure its effective delivery of cytotoxicity to diseased cells.
Functional Domains
The functional domains of perforin play distinct yet interconnected roles in its overall activity. These domains include:
- Cytotoxic Domain: This area is specifically responsible for initiating pore formation.'
- Lipid Bilayer Interaction Sites: These domains ensure perforin can anchor itself to the lipid bilayer, enabling it to perform its action effectively.
- Regulatory Domains: Such domains can modulate perforin's activity, which is vital to prevent unintended damage to healthy cells during the immune response.
Understanding how these structural and functional elements work together is crucial for developing therapeutic strategies involving recombinant perforin. Their configuration not only affects its interaction with membranes but also its overall cytotoxic efficacy.
Mechanism of Action
Cell Membrane Targeting
The mechanism of action of recombinant perforin is fundamentally critical in understanding its role in immune responses. One essential aspect is its ability to target cell membranes. This focused activity is vital for its effectiveness against diseased cells, such as those infected by viruses or transformed by cancer. Recombinant perforin binds to proteins expressed on the surface of these compromised cells. This targeting is achieved through a specific interaction with membrane components, allowing perforin to recognize and distinguish between healthy and pathological cells.
The precision inherent in this binding reduces collateral damage to surrounding healthy cells. As perforin binds to a target cell's membrane, it aligns itself for the subsequent steps that culminate in apoptosis or cell death.
Pore Formation and Cytotoxicity
Once recombinant perforin has successfully targeted the cell membrane, its action transitions into pore formation. This is a pivotal step in its cytotoxic effects. The recruitment of perforin monomers leads to oligomerization, resulting in the formation of pores within the targeted cell's membrane. These pores are large enough to disrupt the osmotic balance of the cell, leading to cell lysis and ultimately death.
The cytotoxicity of recombinant perforin is thus a result of this pore-forming ability, as it allows for the entry of granzymes - serine proteases that also play a crucial role in inducing apoptosis. The efficiency of perforin's action underlines its potential application in therapies aimed at eliminating malignant or infected cells.
In summary, the mechanism of action showcases recombinant perforin’s essential role as an immune effector. Its dual function of selectively targeting membranes and forming destructive pores exemplifies its significant therapeutic potential in immunological applications.
Genetic Engineering Techniques
The exploration of genetic engineering techniques is essential as it directly contributes to understanding and producing recombinant perforin. Through these methods, researchers can harness the molecular machinery of cells to generate this crucial protein in a controlled and efficient manner, ensuring both quality and yield. By employing precise genetic modifications, scientists can manipulate the expression of perforin to enhance its functional attributes, thus broadening its applications in medical therapies. The ability to produce recombinant perforin not only provides necessary quantities for research but also opens avenues for therapeutic innovations in oncology and infectious diseases.
Methods of Recombinant Production
Recombinant perforin is primarily produced using several key techniques. One popular method is the use of the Escherichia coli expression system. This system is advantageous because it is well-understood and allows for rapid protein production. E. coli can be genetically modified to include the DNA sequence that codes for perforin. Once transformed, these bacteria can rapidly multiply, resulting in high quantities of the protein.
Another commonly used approach includes yeast expression systems, such as Pichia pastoris. This type of system can perform post-translational modifications, which are often crucial for the proper functionality of proteins. Thus, using yeast can lead to more biologically active forms of recombinant perforin.
Additionally, mammalian cell systems like CHO (Chinese Hamster Ovary) cells are frequently employed for their ability to produce complex proteins with correct folding and modifications. Though this method is more expensive and time-consuming, it yields proteins that are structurally more similar to naturally occurring perforin, making them potentially more effective in therapeutic contexts.
Challenges in Production
Despite advancements in recombinant technology, several challenges remain in the production of perforin. One significant issue is the solubility of the produced protein. Recombinant proteins often aggregate, leading to inclusion bodies, which are non-functional and difficult to purify. Finding strategies to prevent aggregation is critical for utilizing produced perforin effectively.
Moreover, optimizing expression levels is a complex task. High expression may not always correlate with high-quality proteins. If proteins are overexpressed, they may misfold, leading to reduced functionality. Striking a balance between yield and functional integrity is an ongoing challenge.
"The production of recombinant perforin requires a careful consideration of the expression system and optimization of conditions to ensure both yield and functionality."
Finally, scaling up the production process from laboratory to industrial scale introduces additional layers of complexity. Regulatory demands and quality control mechanisms must be meticulously adhered to, especially for proteins intended for human therapeutic use. Addressing these challenges will be vital for the successful application of recombinant perforin in clinical settings.
Therapeutic Applications
The exploration of recombinant perforin and its therapeutic applications is vital in understanding its relevance in modern medicine. This protein holds potential for addressing significant health issues, primarily cancer and infectious diseases. Its role in the immune system is central to navigating the treatments for these conditions. Integrating recombinant perforin into therapeutic strategies may provide targeted approaches, minimizing damage to healthy tissue while maximizing the cytotoxic effects on diseased cells.
Adopting recombinant perforin in medicine not only enhances the efficacy of existing treatments, but also opens avenues for developing novel therapeutic interventions. This pursuit balances immune system engagement with the possible adverse consequences associated with cellular therapy. The continual investigation into its applications highlights a promising future in medical science.
Utilization in Cancer Treatment
Recombinant perforin is emerging as a powerful agent in cancer treatment. One of the primary roles it plays is in inducing apoptosis in malignant cells, predominantly due to its pore-forming ability that leads to cellular disruption. This selective targeting of cancer cells makes it invaluable; it allows for the killing of tumor cells while preserving surrounding healthy tissue. This mechanism is integral in innovative therapeutic strategies like Cancer Immunotherapy, where the immune response is harnessed to combat tumors.
Furthermore, studies have shown that when perforin is paired with other cytotoxic agents, the resultant synergistic effects can significantly enhance the overall treatment effectiveness. For instance, combining perforin with granzyme B has been shown to result in higher rates of cancer cell apoptosis. Such strategies showcase the adaptability and potency of recombinant perforin in addressing various tumor types.
Role in Infectious Disease Management
The role of recombinant perforin extends beyond oncology to infectious diseases, particularly in the realm of viral infections. Viruses often evade the immune response, and perforin can help counteract this evasion by punch holes in the infected cells, leading to their destruction. This is particularly critical when dealing with robust viruses that can persist in the body or hijack immune responses, such as HIV.
Moreover, recombinant perforin can be engineered to target specific pathogens, thereby reducing infection rates and improving patient outcomes. The focus on enhancing this protein's efficacy against diverse pathogens points to its substantial relevance in public health. Human clinical trials and experimental studies have begun to illustrate how perforin’s applications can effectively manage and mitigate infectious threats.
Advancements in Immunotherapy


Recent advancements in immunotherapy underscore recombinant perforin's significance in medical research. New methodologies are being developed to optimize the efficacy of perforin-based therapies. For instance, scientists are examining how various delivery mechanisms can be enhanced to ensure precise targeting to affected areas, thus improving safety and reducing side effects.
Innovations in genetic engineering facilitate the creation of enhanced recombinant perforin variants with higher specificity and lower immunogenicity. The result is the potential for personalized immunotherapy, where each patient receives tailored treatments based on their unique genetic makeup. This area of research is rapidly progressing and shows immense promise in addressing complex diseases.
The future of recombinant perforin research in therapeutics hinges on understanding its multifaceted roles in both cancer and infectious diseases. Its potential continues to evolve as research uncovers deeper insights into its functionality and applications.
Comparative Analysis with Other Cytotoxic Mechanisms
The comparative analysis of recombinant perforin with other cytotoxic mechanisms is crucial for understanding its unique role in the immune response. It allows researchers and medical professionals to identify specific advantages and limitations of different cytotoxic strategies. By evaluating perforin alongside granzymes and other cytotoxic proteins, we gain insights into how these components interact within the immune system and their potential therapeutic implications.
Comparison with Granzymes
Granzymes are serine proteases released by cytotoxic lymphocytes, such as natural killer cells and CD8+ T cells, to induce apoptosis in target cells. This mechanism is distinct from that of perforin, yet both play complementary roles in cell-mediated immunity.
- Functionality: While perforin primarily forms pores in the target cell membrane, leading to cellular lysis, granzymes enter through these pores to trigger a cascade of cellular events that ultimately result in apoptosis.
- Targeting Mechanisms: The targeting of granzymes relies on the ability of perforin to compromise the target cell membrane. Thus, their effectiveness is significantly influenced by the action of perforin.
- Response Spectrum: Granzymes are typically more effective against transformed or infected cells, as they induce mechanisms that specifically control cell survival. Conversely, perforin presents a more immediate threat to the cell's structural integrity but is reliant on granzymes for executing the cell death program.
Understanding this interplay helps in designing combination therapies that maximize cytotoxic effects. For instance, enhancing perforin activity may improve granzyme delivery and efficacy, making it a vital area of exploration in immunotherapy.
Role of Perforin in T-cell Mediated Immunity
Perforin's role in T-cell mediated immunity is pivotal. It primarily facilitates the elimination of infected or cancerous cells by T lymphocytes. This function is defined by several key aspects:
- Activation: Upon recognition of infected or transformed cells, CD8+ T cells release perforin and granzymes, initiating a targeted immune response.
- Pore Formation: The ability of perforin to form pores enables the entry of granzymes into the cytoplasm of infected cells, leading to programmed cell death. This process is essential for controlling infections and tumor growth.
- Coordination with Other Immune Components: Perforin works synergistically with other proteins and immune modulators, enhancing overall immune responses. This coordination is critical in ensuring that adaptive immunity is effective without causing damage to surrounding healthy tissues.
In this context, examining perforin alongside granzymes and other cytotoxic mechanisms gives a comprehensive view of T-cell-mediated immune responses. It underscores how different components contribute to a balanced and effective immune defense.
Understanding the roles and interactions of perforin with other cytotoxic molecules is essential for developing effective immunotherapeutic approaches.
This section delineates the complexities involved in cytotoxic mechanisms, establishing a foundational understanding required for future research and clinical application.
Current Research Trends
Recent developments in the field of recombinant perforin have shed light on its growing significance in therapeutic applications and basic research. This section elucidates current research trends, highlighting the innovative approaches being employed, benefits derived from these studies, and considerations necessary for their implications.
Investigating Novel Applications
A substantial area of focus in current research is the exploration of novel applications of recombinant perforin. Researchers are delving into how this protein can be effectively utilized beyond its traditional roles in immunology. For example, studies are investigating its potential in enhancing the effectiveness of existing immunotherapies for cancer, such as chimeric antigen receptor (CAR) T-cell therapies. The synergistic effects of perforin when combined with these therapies could lead to more efficient eradicators of cancer cells.
Another promising area is its application in gene therapy. Recombinant perforin embedded within gene delivery systems may improve the targeted destruction of infected or malignant cells by enabling precise cellular entry. The integration of perforin into such vectors could potentially enhance the efficacy of therapeutic interventions while minimizing off-target effects.
Moreover, there are ongoing gene-editing endeavors to optimize perforin's functionality through CRISPR technology. This trend aims to produce engineered versions of perforin that could offer improved cytotoxic activity, thereby capable of overcoming certain resistance mechanisms often observed in tumor cells.
Key Studies and Findings
Numerous key studies have contributed to advancing our understanding of recombinant perforin. A significant finding from recent investigational studies has been the identification of specific molecular modifications that enhance the stability and activity of perforin. For instance, a study demonstrated that glycosylation patterns can play a critical role in the protein’s cytolytic efficiency. It was found that modifying these patterns leads to a considerable uptick in cell lysis rates in various tumor models.
Another pivotal research highlighted the role of perforin in autoimmune diseases, suggesting that its controlled application could help in modulating immune responses. By selectively targeting dysfunctional immune cells, it could provide a novel strategy to manage conditions like multiple sclerosis, where the immune system attacks the body’s own tissues.
In addition, integrative approaches have emerged, combining recombinant perforin with other immune modulators. One such study unveiled that the combination of perforin with cytokine therapies led to enhanced antitumor effects, showcasing its potential to bridge together disparate immunotherapeutic avenues.
Recent trends underscore the ability of recombinant perforin to transform future therapeutic modalities, improving patient outcomes in challenging diseases like cancer and autoimmune disorders.
In summary, current research trends denote an exciting phase for recombinant perforin. As scientists continue to innovate and discover new applications for this vital protein, the implications for therapeutic interventions grow increasingly significant. The exploration of its functions combined with high-throughput screening and advanced genetic engineering methods could redefine treatment paradigms in modern medicine.
Ethical Considerations
In recent years, the use of recombinant perforin in therapeutic applications has prompted significant ethical discussions. These discussions revolve around the safety and efficacy of such treatments, as well as the broader implications for patients and the healthcare system. Ethical considerations are critical, particularly when dealing with therapies that alter immune responses in humans. Ensuring that these treatments are safe and effective is paramount not only for patient wellbeing but also for maintaining public trust in biotechnological advances.
Safety in Therapeutic Applications
The safety of recombinant perforin therapies comes under scrutiny as potential risks must be evaluated thoroughly. Possible adverse effects can arise from improper dosing, unintended immune responses, or interactions with other treatments. Research has shown that the appropriate handling and application of recombinant perforin can mitigate such risks.
- Clinical trials are essential. They help in understanding the short-term and long-term effects of these therapies on patients.
- Comprehensive testing must adhere to guidelines to minimize side effects.
- Transparent communication with patients ensures that they are fully informed about possible risks.
An emerging area of concern is how these therapies interact with diverse patient biology. Individual variations can lead to different reactions to the same treatment. Thus, a strong emphasis on patient monitoring during treatment is advisable. The potential for serious adverse reactions raises questions about who should be eligible for these treatments and under what conditions.
Regulatory Perspectives


Regulatory bodies such as the Food and Drug Administration (FDA) in the United States play a crucial role in overseeing recombinant therapies. These agencies are responsible for ensuring that any new treatment involving recombinant perforin meets rigorous standards before reaching clinical use.
Key aspects of regulatory frameworks for recombinant perforin include:
- Review Processes: Regulatory agencies conduct thorough evaluations of clinical trial designs, manufacturing processes, and the data on safety and efficacy. This includes the examination of potential risks versus the anticipated benefits.
- Post-Market Surveillance: After approval, ongoing surveillance of treatment outcomes is necessary to identify any long-term adverse effects that may not have been evident in earlier trials.
- Ethical Guidelines: Regulations also dictate ethical standards for conducting clinical trials, ensuring informed consent and protection of participants.
Investing in strong regulatory oversight not only protects patients but also enhances the credibility of recombinant therapies. Achieving a balance between innovation and patient safety is crucial in the realm of recombinant perforin advancements.
In summary, careful consideration of ethical implications ensures that recombinant perforin therapies are developed and implemented in a manner that prioritizes patient safety and regulatory compliance, ultimately fostering trust in these potentially transformative medical interventions.
Through thoughtful ethical review, the safe application of recombinant perforin can lead to significant advancements in therapeutic options for patients.
Future Directions in Recombinant Perforin Research
Research into recombinant perforin has gained momentum, reflecting its potential as a transformative tool in therapeutic applications. Understanding its future directions is crucial for optimizing its use in various medical fields. As we contemplate the trajectory of recombinant perforin, several specific elements stand out. These elements are not just beneficial but also necessary for advancing knowledge and application in immunotherapy.
The exploration of novel therapeutic potentials poses a significant area for future investigation. Recombinant perforin can be engineered to enhance its efficacy in targeting malignant cells more effectively. This could lead to improved treatment outcomes in different types of cancer. Researchers are actively exploring various modifications of the perforin molecule to increase specificity, reduce side effects, and improve the overall safety of treatments. With advances in genetic engineering, we may soon witness customized versions of perforin that align precisely with individual patient profiles.
Potential for Novel Therapeutics
The quest for novel therapeutics using recombinant perforin presents an intriguing frontier. Researchers are experimenting with creating fusion proteins that combine perforin with targeting agents or other cytotoxic molecules. This approach aims to amplify the impact of perforin on target cells, ensuring a more efficient destruction of cancer or infected cells.
Some potential applications include:
- Combination therapies: Using recombinant perforin in conjunction with existing treatments like checkpoint inhibitors.
- Targeted delivery systems: Engineering delivery mechanisms, such as nanoparticles, to transport perforin directly to tumor sites, minimizing systemic exposure.
The continued development of these novel therapeutics has the potential to revolutionize cancer treatments. Importantly, safety and efficacy must be at the forefront of this research. Long-term studies will be essential to assess both individual and cumulative effects of such therapies on patients.
Integration with Personalized Medicine
Personalized medicine leverages genetic and molecular profiling to tailor treatments for individual needs. The integration of recombinant perforin into this approach holds considerable promise. With advances in genomics and biotechnology, the potential to design tailored perforin therapies based on a patient’s unique genetic makeup is emerging.
Key considerations in this integration include:
- Biomarker identification: Establishing biomarkers that indicate responsiveness to perforin-based therapy.
- Patient stratification: Classifying patients based on their likelihood of benefitting from specific perforin modifications.
This personalized approach enhances the potential of recombinant perforin to function effectively within a highly specific therapeutic context, which could improve patient outcomes significantly. As research deepens, we may observe a move towards more individualized treatment plans that harness the unique properties of recombinant perforin.
The future of recombinant perforin research is not just about advancements in technique but also about the profound implications these advancements may have for human health and disease management.
Closure
The conclusion of this article encapsulates the salient points regarding recombinant perforin and its implications in contemporary immunology. The understanding of recombinant perforin emphasizes its multifaceted role in the immune response. It aids in the elimination of infected and malignant cells, and offers a promising avenue for therapeutic innovation.
Recapitulation of Key Insights
A number of critical insights emerge from the discussion surrounding recombinant perforin. First, the molecular structure reveals specific functional domains responsible for its cytotoxic actions. These actions are essential for T-cell mediated immunity. Understanding its precise mechanism of action provides a framework for enhancing its efficacy in therapeutic applications. By utilizing genetic engineering techniques, researchers are able to produce recombinant forms that have enhanced stability and activity in vitro and in vivo.
Additionally, the therapeutic applications explored in this article highlight recombinant perforin's potential in cancer treatment and management of infectious diseases. Research trends indicate a growing interest in harnessing its properties for immunotherapy, paving the way for innovative cancer treatments. As companies and research institutions invest in this area, recombinant perforin could lead to breakthroughs in how immune responses are leveraged against diseases.
Implications for Future Research
Recombinant perforin presents extensive opportunities for future research and development. Investigators are encouraged to explore its integration with other immune therapies, which can enhance its therapeutic potential. Personalized medicine strategies that aim to tailor treatments based on individual genetic profiles may further augment the advantages of recombinant perforin.
Moreover, understanding the regulatory landscape surrounding its therapeutic use is vital. Addressing safety concerns through rigorous testing will be crucial in advancing recombinant perforin towards clinical application. The intersection of ethics in production methods and application must also be continuously evaluated as this field evolves.
Importance of Citing Sources
Citing sources is vital for several reasons:
- Credibility: Valid sources lend weight to the assertions made within the article.
- Transparency: Readers can trace back to the original research for more in-depth understanding.
- Academic Integrity: Proper citations prevent plagiarism and uphold the standards of academic writing.
Moreover, the references reflect the diversity of research available on recombinant perforin. This encompasses studies focusing on its molecular structure, mechanisms of action, and therapeutic applications in both oncology and infectious disease.
Elements to Include in References
When compiling references, attention should be given to:
- Author(s) Names: Ensure that names are spelled correctly and in the appropriate format.
- Publication Year: Include the year of publication to provide context in terms of relevance and recency.
- Title of the Work: The title should be fully cited, offering insights into the focus of the study or review.
- Journal Name and Volume: This informs the reader about where to find the original research and its significance.
End
In summary, the references section significantly enhances the article's value by supporting the claims made and providing avenues for further exploration. Readers, including students, researchers, and professionals, can rely on this section to delve deeper into the science of recombinant perforin, reinforcing the overall objective of contributing to a well-rounded understanding of this important immune protein.