A Functional Systems Review of Cellular Nucleic Acid Metabolism and Regulatory Enzymes in Gene Expression, RNA Homeostasis, and Immune Defense
A Functional Systems Review of Cellular Nucleic Acid Metabolism and Regulatory Enzymes in Gene Expression, RNA Homeostasis, and Immune Defense
Intracellular nucleic acids are not static carriers of genetic information, but rather dynamic molecular systems that continuously undergo synthesis, processing, modification, transport, recognition, degradation, and reutilization. Supporting the operation of this system is a functional network composed of nucleic acid metabolic enzymes, nucleic acid regulatory enzymes, nucleic acid-sensing factors, and multiple macromolecular complexes. On the one hand, this network determines whether gene expression programs can be accurately established and executed; on the other hand, it determines whether RNA can maintain an appropriate abundance, structure, and functional state, while also undertaking the surveillance and clearance of aberrant endogenous nucleic acids and exogenous pathogen-derived nucleic acids.
Keywords: nucleic acid metabolism; nucleic acid regulatory enzymes; gene expression; RNA homeostasis; RNA processing; RNA degradation; RNA editing; nucleic acid sensing; innate immunity; quality control
I. Fundamental Components of Cellular Nucleic Acid Metabolism and Regulatory Enzymes
1.1 Enzymes related to nucleic acid precursor synthesis and polymerization
(1) Nucleotide metabolic enzymes
These enzymes mainly participate in de novo synthesis, salvage synthesis, and interconversion of purine and pyrimidine nucleotides, thereby determining the abundance and balance of intracellular NTP and dNTP pools. Nucleic acid polymerization, replication, repair, and transcription all depend on this precursor supply system. Accordingly, nucleotide metabolism is not merely a peripheral metabolic background, but the substrate foundation of the nucleic acid functional system.
(2) Nucleic acid polymerases
DNA polymerases and RNA polymerases respectively undertake the core tasks of genetic information replication, repair, and transcriptional RNA synthesis, forming the direct catalytic machinery of nucleic acid generation. Different polymerases differ in substrate preference, proofreading capacity, processivity, and subcellular division of labor, and together determine the accuracy and efficiency of nucleic acid synthesis.
1.2 Enzymes associated with DNA metabolism and transcriptional regulation
(1) DNA replication- and repair-related enzymes
These include helicases, ligases, topoisomerases, endonucleases, exonucleases, and multiple classes of repair-associated polymerases. This system is responsible for DNA strand unwinding, break repair, lesion bypass, replication fork stabilization, and topological tension control, and thus serves as a core support for genome stability.
(2) Enzymes related to chromatin and transcriptional regulation
These include DNA methyltransferases, demethylation-associated enzymes, histone acetyltransferases, deacetylases, and ATPases associated with chromatin remodeling complexes. By altering chromatin accessibility, nucleosome arrangement, and transcription factor accessibility, they determine whether gene expression programs can be effectively initiated and maintained.
1.3 Enzymes associated with RNA processing, modification, and editing
(1) RNA maturation and processing enzymes
These include 5′ capping-associated enzymes, 3′ end cleavage factors, poly(A) polymerases, spliceosome-associated catalytic factors, and RNA helicases. These enzymes convert primary transcripts into mature RNA molecules that are export-competent, translation-competent, and molecularly recognizable, thereby serving as the starting point for post-transcriptional fate allocation.
(2) RNA modification and editing enzymes
These include m6A methyltransferases, demethylases, pseudouridylation-associated enzymes, and RNA editing enzymes such as ADAR. Their function is not limited to “adding chemical marks,” but rather lies in rewriting the functional output and immunological properties of RNA by altering base recognition, structural stability, and protein-binding patterns.
1.4 Enzymes related to RNA degradation and quality control
(1) RNA degradation-associated enzymes
These include deadenylation complexes, decapping enzymes, 5′-3′ exonucleases, 3′-5′ exonucleases, and the exosome complex. Together, they constitute the major pathways of RNA turnover and clearance, thereby determining RNA lifespan, abundance, and renewal kinetics.
(2) RNA quality control-associated factors
These include factors involved in nonsense-mediated decay, nonstop decay, and translational stalling surveillance. These systems are responsible for recognizing aberrantly spliced RNAs, premature termination-containing RNAs, translationally defective transcripts, or structurally abnormal RNAs, thereby preventing erroneous transcripts from entering long-term expression programs.
1.5 Enzymes associated with small RNA biogenesis and silencing regulation
(1) miRNA processing-associated enzymes
These include Drosha, Dicer, and Argonaute-associated components, which are responsible for precursor miRNA cleavage, maturation, and target RNA silencing regulation, forming an important effector system for fine-tuning post-transcriptional gene expression.
(2) Enzymes associated with the siRNA and piRNA pathways
These factors participate in repetitive sequence silencing, transposable element suppression, and clearance of specific exogenous nucleic acids, and are particularly important in genome stability and germline protection.
1.6 Enzymes associated with nucleic acid sensing and immune defense
(1) Nucleic acid clearance enzymes
These include TREX1, RNase H, and RNase L, which are primarily responsible for the degradation and clearance of aberrant DNA or RNA, thereby preventing inappropriate persistence of misplaced nucleic acids in the cytoplasm or other unsuitable compartments.
(2) Nucleic acid editing- and restriction-associated enzymes
These include ADAR, selected members of the APOBEC family, and SAMHD1. These molecules participate not only in maintaining endogenous nucleic acid homeostasis, but also in restrictive regulation of viral nucleic acids, reverse transcription intermediates, and aberrant double-stranded nucleic acids.
Table 1. Major Types of Cellular Nucleic Acid Metabolic and Regulatory Enzymes and Their Functional Positioning
Category | Representative enzymes/complexes | Major functional positioning |
Enzymes related to nucleic acid precursor metabolism | Purine/pyrimidine synthesis-associated enzymes, ribonucleotide reductase, nucleotide kinases | Maintain NTP and dNTP supply and support replication, transcription, and repair |
Enzymes related to nucleic acid polymerization | DNA polymerases, RNA polymerases | Catalyze DNA replication, repair, and RNA transcription |
Enzymes related to DNA metabolism | Helicases, ligases, topoisomerases, endonucleases/exonucleases | Participate in DNA unwinding, ligation, break repair, and topological regulation |
Enzymes related to chromatin and transcriptional regulation | DNA methyltransferases, histone-modifying enzymes, chromatin-remodeling ATPases | Regulate transcriptional accessibility and gene expression activity |
Enzymes related to RNA maturation and processing | Capping enzymes, poly(A) polymerases, spliceosome-associated enzymes, RNA helicases | Promote precursor RNA maturation and determine post-transcriptional fate |
Enzymes related to RNA modification and editing | m6A methyltransferases, demethylases, ADAR | Alter RNA marks, stability, translational efficiency, and immunogenicity |
Enzymes related to RNA degradation | Deadenylation complexes, decapping enzymes, XRN family proteins, exosome complex | Mediate RNA turnover, clearance, and homeostatic maintenance |
RNA quality control-associated factors | Nonsense-mediated decay factors, translational stalling surveillance factors | Recognize aberrant RNA and prevent erroneous expression output |
Small RNA pathway-associated enzymes | Drosha, Dicer, Argonaute, PIWI family proteins | Mediate miRNA/siRNA/piRNA biogenesis and silencing regulation |
Enzymes related to nucleic acid sensing and immune defense | TREX1, RNase H, RNase L, SAMHD1, APOBEC | Clear aberrant nucleic acids, restrict pathogen replication, and regulate innate immunity |
II. Establishment of Gene Expression Programs Through Nucleic Acid Metabolism
2.1 Nucleotide supply defines the substrate boundaries of the expression system
(1) Nucleotide pool balance and polymerization accuracy
Gene expression first depends on the quantity and proportion of available nucleotides. Insufficient NTP supply reduces transcriptional elongation capacity, whereas dNTP imbalance increases the probability of mismatch during replication and repair. Thus, the consequences of abnormal nucleotide metabolism are not limited to “insufficient materials,” but simultaneously affect polymerization rate, polymerization fidelity, and the downstream burden of quality control.
(2) Constraints imposed by metabolic state on expression scale
Cells in states of rapid proliferation, strong immune activation, or high secretory activity display substantially increased demand for nucleic acid precursors. Under such conditions, the precursor supply system influences not only whether nucleic acid synthesis can be sustained, but also whether certain high-throughput expression programs can be completed efficiently.
2.2 Polymerase systems and the initiation, elongation, and termination of expression programs
(1) Functional division of RNA polymerases
Different RNA polymerases transcribe distinct classes of RNA, among which RNA polymerase II is most directly related to protein-coding gene expression. Its carboxy-terminal domain can recruit capping, splicing, and 3′ end processing factors, thereby tightly coupling transcription with RNA maturation.
(2) Enzymatic support for transcriptional elongation
Transcription is not a simple linear movement of polymerase along the template. DNA unwinding, release of topological stress, chromatin remodeling, and conformational regulation of nascent RNA all require coordinated participation of multiple enzymes. Timely action by topoisomerases and helicases can reduce polymerase stalling and transcription-replication conflicts.
(3) Coupling of transcription termination with 3′ end processing
Termination is not merely “cessation of template reading,” but an integrated event that occurs simultaneously with RNA cleavage, tail addition, and disassembly of the transcription complex. If this step becomes imbalanced, aberrantly extended transcripts may accumulate and affect the expression of neighboring genes and the local chromatin state.
III. RNA Processing Enzyme Systems and the Allocation of RNA Maturation Fate
3.1 5′ capping and 3′ end processing establish the identity of mature RNA
(1) Structural significance of 5′ capping
Nascent mRNA undergoes capping early during transcription, which enhances resistance to exonucleolytic degradation and provides a molecular signature for nuclear export, translation initiation, and recognition as “self RNA.” When the cap structure is absent or insufficiently modified, RNA is more likely to be treated as an abnormal molecule and routed into clearance or immune-sensing pathways.
(2) 3′ end cleavage and poly(A) tail formation
3′ end processing determines the termination boundary, stability, and translational potential of mRNA. The poly(A) tail not only provides physical protection, but also influences the assembly state of mRNA-binding proteins. Differences in cleavage site choice and tail length can alter the half-life, subcellular localization, and expression strength of transcripts derived from the same gene.
3.2 Spliceosome-associated enzymes determine transcript diversity and expression accuracy
(1) Splicing is a dynamic process of conformational rearrangement
Pre-mRNA splicing depends on the coordinated action of snRNPs, ATP-dependent RNA helicases, and multiple auxiliary factors. Its core function is not merely intron removal, but rather the accurate joining of exons in the correct order through a series of recognition, rearrangement, and catalytic steps.
(2) Alternative splicing expands the complexity of the expression repertoire
Alternative splicing enables a single gene to produce multiple transcripts and protein isoforms and is a major source of expression complexity in higher eukaryotes. Subtle alterations in splicing-associated enzymes can lead to exon skipping, intron retention, or activation of cryptic splice sites, thereby profoundly altering cellular functional states.
(3) Coupling between transcriptional speed and the splicing window
Cotranscriptional splicing means that RNA polymerase speed influences the recognition window available to splicing factors. Excessively rapid transcription may compress the recognition time of weak splice sites, whereas excessively slow transcription may alter local structural exposure and protein-binding patterns. Polymerization and splicing therefore reside on the same regulatory axis.
IV. Establishment of RNA Homeostasis: Modification, Structural Remodeling, and the Balance of Degradation
4.1 RNA modification enzymes reshape RNA fate
(1) RNA modification is not a secondary accessory mark
Modifications such as m6A, m5C, and pseudouridine can alter RNA folding, protein interaction, and sensitivity to degradation. The role of RNA modification enzymes lies not in simply “adding labels,” but in recruiting specific reader proteins that allocate transcripts to distinct fate channels, such as preferential translation, temporary storage, or accelerated degradation.
(2) The dynamic nature of modification increases regulatory flexibility
The antagonistic actions of methyltransferases and demethylases make RNA modification a reversible regulatory layer. Cells can rapidly remodel the RNA modification landscape under stress, differentiation, or infection without requiring genomic changes, thereby adjusting expression programs in a highly flexible manner.
4.2 RNA editing and control of RNA structure
(1) RNA editing alters sequence-based functional output
A-to-I editing mediated by ADAR can alter codons, splice sites, miRNA pairing relationships, and the stability of RNA secondary structure. Its effects are manifested not only at the protein-coding level, but also at the level of RNA fate.
(2) RNA helicases maintain structural plasticity
RNA continuously forms hairpins, double-stranded regions, and long-range interactions within cells. RNA helicases drive ATP-dependent conformational rearrangements that allow RNA to switch structural states during splicing, export, translation, and degradation. Without helicase participation, many RNA processes would fail because of structural barriers.
(1) Deadenylation is the transition point toward degradation
Most mRNAs are not degraded randomly, but first undergo deadenylation. Once the poly(A) tail is shortened, the protective state of RNA declines, and the transcript subsequently enters either decapping-mediated or 3′ end exonucleolytic degradation pathways. Deadenylation therefore represents a key boundary between the “active expression state” and the “clearance-ready state” of RNA.
(2) Bidirectional degradation improves clearance efficiency
Following decapping, 5′-3′ exonucleases can rapidly degrade RNA; in parallel, the exosome complex mediates 3′-5′ degradation. This bidirectional clearance mechanism increases RNA metabolic throughput and reduces the risk of long-term accumulation of aberrant RNA species.
(3) Quality control-directed degradation safeguards expression accuracy
Nonsense-mediated decay, nonstop decay, and translational stalling surveillance couple RNA quality assessment to translational behavior. Rather than passively handling errors only after RNA generation, cells continuously supervise transcript quality during expression and eliminate transcripts that are not suitable for continued participation in gene expression.
V. Small RNA Pathways and Post-Transcriptional Reprogramming of Gene Expression
5.1 Core roles of the miRNA processing enzyme system
(1) Stepwise processing establishes mature miRNA
miRNA precursors must be sequentially cleaved by Drosha and Dicer and ultimately loaded into Argonaute to form mature silencing complexes. This multistep process demonstrates that small RNAs are not intrinsically functional, but instead rely heavily on the precise action of endonucleases.
(2) miRNA reshapes post-transcriptional expression networks
Mature miRNAs broadly regulate the cell cycle, metabolism, differentiation, and stress responses by promoting target mRNA degradation, repressing translation, or altering mRNA stability. Their defining feature is the ability to rapidly rewrite the protein output landscape without changing transcriptional rates.
5.2 Defensive and stabilizing functions of the siRNA and piRNA pathways
(1) siRNA pathways are biased toward handling aberrant double-stranded RNA
When double-stranded RNA appears in cells, Dicer-related systems can cleave it into small RNAs and guide subsequent silencing or degradation. This mechanism is important for restricting exogenous RNA, repetitive sequence-derived transcripts, and certain aberrant endogenous RNAs.
(2) piRNA maintains germline homeostasis
The piRNA pathway is particularly important in germ cells, where its core function is to suppress activation of transposable elements and repetitive sequences, thereby preventing long-term genome instability. This pathway illustrates that nucleic acid metabolic enzymes regulate not only current cellular expression, but also protection of genetic information across generations.
VI. Recognition and Clearance Systems of Nucleic Acid Metabolic Enzymes in Innate Immunity
6.1 Molecular boundaries between self nucleic acids and abnormal nucleic acids
(1) Normal self nucleic acids must be correctly processed
Cells do not mount strong immune responses against most self nucleic acids not because the recognition system “cannot see” them, but because these nucleic acids undergo proper capping, tailing, editing, packaging, and compartmentalization, thereby acquiring defined “self signatures.”
(2) Processing failure can confer danger-associated properties on endogenous nucleic acids
Once RNA is improperly capped, insufficiently edited, or DNA/RNA appears in an inappropriate subcellular compartment, these molecules may be recognized as aberrant nucleic acids. Thus, nucleic acid metabolic enzymes are responsible not only for nucleic acid processing, but also for defining the recognition boundaries of the immune system.
6.2 Nucleic acid clearance enzymes are critical buffers of immune homeostasis
(1) DNA clearance and control of cytosolic immune activation
Cytosolic DNA is itself a highly sensitive danger signal, and exonucleases such as TREX1 must therefore continuously remove DNA fragments that should not persist in the cytosol. Defects in such clearance enzymes allow endogenous DNA to chronically drive interferon and inflammatory pathways.
(2) RNA clearance and the balance of double-stranded RNA surveillance
If endogenous double-stranded RNA, repetitive sequence-derived transcripts, or improperly processed RNA are not promptly edited or degraded, they may be erroneously interpreted by RNA-sensing systems as virus-associated molecules, thereby triggering abnormal immune activation. RNA degradation enzymes and RNA editing enzymes therefore jointly undertake the task of “de-immunogenicizing” RNA.
VII. Functional Stratification of Nucleic Acid Metabolic Enzymes in Antiviral and Anti-Transposon Defense
7.1 Direct restriction of pathogen nucleic acid replication
(1) Clearance of pathogen RNA through cleavage
Certain inducible ribonucleases can rapidly cleave viral RNA, as well as selected host RNAs, under antiviral conditions, thereby directly suppressing translation and replication and establishing an intense antiviral environment. Although this mechanism carries a substantial cost, it is highly efficient in acute infection control.
(2) Inhibition of reverse transcription and replication through substrate limitation
Metabolic enzymes such as SAMHD1 restrict the nucleic acid synthesis of retroviruses and certain DNA viruses by depleting available dNTP pools. This demonstrates that anti-infective defense does not necessarily depend on direct recognition and cleavage, but can also be achieved through metabolic substrate deprivation.
7.2 Reduction of pathogen activity through editing and mutagenesis
(1) Nucleic acid editing-based restriction factors
Selected members of the APOBEC family can edit pathogen nucleic acids, increasing their mutational burden and weakening replicative capacity. Such mechanisms convert nucleic acid metabolic enzymes into restrictive immune factors that achieve defense through disruption at the level of genetic information.
(2) Defensive effects must be strictly constrained
If editing- and cleavage-based anti-infective mechanisms remain chronically hyperactivated, they may damage host nucleic acids and lead to mutation accumulation or expression imbalance. Cells therefore typically impose strict regulation through inducible conditions, temporal control, and compartmental localization.
VIII. Mechanistic Links Between Nucleic Acid Metabolic Imbalance and Disease Development
8.1 Dysregulated gene expression in tumors and developmental abnormalities
(1) Processing abnormalities cause mismatched expression programs
Abnormalities in capping, splicing, modification, or degradation pathways can all lead to accumulation of erroneous transcripts, imbalance in isoform proportions, and shifts in translational output profiles. In tumors, such imbalance often manifests as sustained activation of proliferation-associated pathways, suppression of apoptosis, and metabolic reprogramming.
(2) Defects in post-transcriptional regulation can amplify developmental deviations
During development, many cell fate transitions depend on precise switching of RNA processing and degradation systems. Defects in the relevant enzymes often affect not just a single gene, but entire groups of development-associated transcripts, and the resulting phenotypes are therefore frequently systemic.
8.2 RNA homeostasis defects in neurodegenerative and stress-related diseases
(1) Imbalance of long-lived RNA and RNP homeostasis
The nervous system depends heavily on precise and durable control of RNA homeostasis. Once RNA unwinding, modification, transport, or clearance becomes abnormal, aberrant accumulation of RNP granules, dysregulated local translation, and defects in stress granule metabolism readily emerge.
(2) Coupling between RNA abnormalities and proteotoxicity
RNA metabolic defects alter not only RNA itself, but also further amplify cellular injury through erroneous translation, generation of truncated proteins, and protein aggregation. Many diseases therefore essentially represent a dual collapse of homeostasis at both the nucleic acid and protein levels.
8.3 Failure of nucleic acid clearance and autoimmune-like inflammation
(1) Persistent exposure of endogenous nucleic acids to sensing pathways
If clearance or editing systems such as TREX1, RNase H, or ADAR fail, cells remain continuously exposed to signals derived from aberrant self nucleic acids, thereby chronically activating interferon and inflammatory pathways.
(2) Failure of nucleic acid quality control is an upstream cause
These diseases are not simply states of “excessive immunity.” More fundamentally, the upstream problem often lies in failure of nucleic acid metabolism and quality control, which allows nucleic acids that should have been processed, compartmentalized, or cleared to persist in environments where they can be sensed.
IX. Integration of Functional Systems from Research and Application Perspectives
9.1 A single enzyme expression level cannot substitute for overall mechanistic judgment
(1) Enzymatic activity state is more critical than expression level
The function of many nucleic acid metabolic enzymes depends on complex assembly, post-translational modification, subcellular localization, and substrate accessibility. Therefore, simple comparison of mRNA or total protein expression is often insufficient to explain the true phenotype.
(2) Analysis must integrate both the substrate layer and the outcome layer
More mechanistically informative strategies should simultaneously examine substrate accumulation, product changes, nucleic acid structural states, protein-binding profiles, and functional endpoints, rather than focusing only on upregulation or downregulation of a single enzyme.
9.2 Key directions in translational research
(1) Targeting RNA homeostasis as an intervention entry point
Intervention strategies centered on splicing regulation, RNA modification, RNA degradation, and miRNA processing are becoming important directions for controlling aberrant expression networks. Their advantage lies in the ability to rapidly influence protein output without directly editing the genome.
(2) Using nucleic acid sensing balance as an entry point for immune regulation
In antiviral therapy, anticancer therapy, and autoimmune diseases, how to balance nucleic acid recognition, nucleic acid editing, and nucleic acid clearance remains a major issue for future development. Excessive suppression of sensing reduces defensive capacity, whereas excessive amplification of sensing may induce autoinflammatory responses; accordingly, more refined threshold-regulation strategies are required.
X. Aladdin-Related Products
10.1 Enzymes Related to Cellular Nucleic Acid Metabolism, Processing Regulation, and Nucleic Acid Clearance
Catalog No. | Product Name | Grade & Purity |
Deoxyribonuclease I from bovine pancreas | lyophilized powder, Protein≥85 %,≥400 Kunitz units/mg protein | |
Recombinant RNase A | DNase free, EnzymoPure™, Protease Free, ActiBioPure™, Bioactive, High Performance, Recombinant, ≥90%(SDS-PAGE), 100 mg/mL | |
RNase H | 600U | |
RNase Inhibitor | pharmaceutical grade, PharmPure™, ≥95%, 1000U/μl | |
T4 DNA Ligase | -- | |
T4 Polynucleotide Kinase | Animal Free, Carrier Free, Bioactive, ActiBioPure™, EnzymoPure™, sterile, DNase, RNase free, 10 U/μL | |
T4 RNA Ligase 2, truncated | Bioactive, ActiBioPure™, EnzymoPure™, Animal Free, Carrier Free, sterile, DNase, RNase free, Protease Free, ≥95%(SDS-PAGE), 200 U/µL | |
T4 RNA Ligase 1 | BioReagent, PCR Reagent, for DNA synthesis, Suitable for molecular biology, EnzymoPure™, for DNA and RNA applications, 30 U/μl | |
E. coli Poly(A) Polymerase | pharmaceutical grade, PharmPure™ | |
T7 RNA Polymerase | BioReagent,endotoxin tested,Suitable for molecular biology,EnzymoPure™,RNase free,Recombinant,≥98.0%,50 U/μL | |
E.coli DNA Polymerase I | EnzymoPure™, free of other DNA exonucleases or endonucleases, free of RNase. | |
Omnipotent nuclease | ActiBioPure™, Bioactive, EnzymoPure™, Carrier Free, sterile, ≥99%(SDS-PAGE), ≥250 U/uL | |
Recombinant UltraNuclease | Carrier Free,Bioactive,ActiBioPure™,EnzymoPure™,His Tag,≥99%(SDS-PAGE) | |
Salt Active UltraNuclease | Carrier Free, Bioactive, ActiBioPure™, EnzymoPure™, Recombinant, ≥99%(SDS-PAGE), 250U/μL, expressed in E. coli | |
Binuclease | Bioactive,Recombinant,ActiBioPure™,endotoxin tested,High Performance,EnzymoPure™,expressed in Pichia pastoris, Protein Content ≥95% (Biuret test); ≥20 KU/mg enzyme powder | |
Ribonuclease A | EnzymoPure™, ≥ 60 Kunitz units/mg Lyophilized Powder | |
RNase A | EnzymoPure™, DNase free, Protease Free, sterile, ≥90%(SDS-PAGE), 10 mg/mL | |
Ribonuclease A from bovine pancreas | EnzymoPure™, ≥ 50 Kunitz units/mg | |
Ribonuclease A from bovine pancreas | Bioactive, ActiBioPure™, High Performance, EnzymoPure™, ≥90%(SDS-PAGE), ≥60 Kunitz units/mg protein | |
Ribonuclease A from bovine pancreas | Bioactive, ActiBioPure™, High Performance, EnzymoPure™, ≥90%(SDS-PAGE), ≥100 KU/mg protein | |
Ribonuclease A from bovine pancreas (DNase & Protease Free) | Bioactive,ActiBioPure™,Native,High Performance,EnzymoPure™,DNase free,Protease Free,≥2,000 units/mg protein | |
Ribonuclease A from bovine pancreas (Purified) | EnzymoPure™, ≥3,000 units/mg dry weight | |
Ribonuclease A from bovine pancreas (Purified Solution) | EnzymoPure™, ≥3,000 units/mg protein | |
RNase | from bovine pancreas | |
Ribonuclease B from bovine pancreas | EnzymoPure™, ≥1,000 units/mg dry weight | |
RNase B, Bovine Pancreas | -- | |
Ribonuclease H (RNase H) | from Escherichia coli H 560 pol A1 | |
Ribonuclease T2, Aspergillus oryzae | -- | |
Deoxyribonuclease I from bovine pancreas | Type II-S, lyophilized powder, Protein≥80 %,≥2,000 units/mg protein | |
Deoxyribonuclease I from bovine pancreas | Type II, lyophilized powder, Protein≥80 %,≥2,000 units/mg protein | |
Deoxyribonuclease I from bovine pancreas | Type IV, lyophilized powder,≥2,000 Kunitz units/mg protein | |
Deoxyribonuclease I bovine | Recombinant, expressed in Pichia pastoris, buffered aqueous glycerol solution,≥5,000 units/mg protein | |
DNase I | Recombinant, PharmPure™, endotoxin tested, EnzymoPure™, ≥95%, 1.8KU/ml-2.2KU/ml | |
Deoxyribonuclease II from bovine spleen | Type V, essentially salt-free, lyophilized powder,≥1,000 units/mg protein | |
Deoxyribonuclease II from porcine spleen | EnzymoPure™, ≥800 units/mg dry weight | |
Deoxyribonuclease II from porcine spleen (Purified, Solution) | EnzymoPure™, ≥12,000 units/mg protein | |
Recombinant DNase I, RNase-free | EnzymoPure™, ≥95%(SDS-PAGE), 1 U/μl | |
Butelase 1 ligase | -- | |
L189 | ≥98% | |
T3 DNA Ligase | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,3 KU/μl | |
T4 DNA Ligase (Fast) | EnzymoPure™ | |
T4 RNA Ligase | ActiBioPure™, Bioactive, EnzymoPure™, Animal Free, Carrier Free, sterile, DNase, RNase free, 10 U/µL | |
T4 RNA Ligase 2, truncated KQ | Animal Free, DNase, RNase free, Protease Free, sterile, Carrier Free, Bioactive, ActiBioPure™, EnzymoPure™, ≥95%(SDS-PAGE), 200 U/µL | |
T7 DNA Ligase | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,3 KU/μl;expressed in E.coli | |
Taq DNA Ligase | EnzymoPure™, 40U/μl | |
E. coli DNA Ligase | Bioactive,Recombinant,ActiBioPure™,High Performance,EnzymoPure™,10 U/μl | |
Endonuclease VIII | ActiBioPure™, Animal Free, Carrier Free, Bioactive, EnzymoPure™, DNase, RNase free, sterile, ≥95%(SDS-PAGE), 10 U/μL | |
Lambda Exonuclease | Animal Free, Carrier Free, ActiBioPure™, Bioactive, EnzymoPure™, sterile, RNase free, ≥95%(SDS-PAGE), 5.0 U/μL | |
Exonuclease VIII, truncated | Animal Free, Carrier Free, Bioactive, ActiBioPure™, EnzymoPure™, sterile, RNase free, 10 U/μL | |
AK Taq DNA Polymerase V2 | Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,5 U/μL | |
Epitech HS Taq DNA Polymerase | Recombinant,Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,5 U/μL | |
Epitech Taq DNA Polymerase | Recombinant,Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,5 U/μL | |
FastTaq DNA Polymerase(5'→3' exo-) | -- | |
Golden Taq DNA Polymerase | -- | |
HiFi Seq Hotstart DNA polymerase | 1U/μL | |
HiFi Seq Hotstart DNA Polymerase | Recombinant,Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,1 U/μL | |
Hotstart HiTaq DNA Polymerase | Recombinant,Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,5 U/μL | |
Hotstart HiTaq Ⅱ DNA Polymerase | Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,5 U/μL | |
Pfu DNA Polymerase | EnzymoPure™, 2.5U/μl | |
Poly(U) Polymerase | ActiBioPure™, Bioactive, EnzymoPure™, Animal Free, Carrier Free, sterile, DNase, RNase free, 2.0 U/µL | |
PowerResist Taq Polymerase | Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,5 U/μL | |
ProPrime Taq DNA Polymerase | Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,5 U/μL | |
Rock DNA Polymerase | EnzymoPure™,Suitable for molecular biology,2.5 U/μL | |
SP6 RNA Polymerase | Animal Free, Carrier Free, Bioactive, ActiBioPure™, EnzymoPure™, RNase free, sterile, 20 U/µL | |
T3 RNA Polymerase | EnzymoPure™, ActiBioPure™, Bioactive, Animal Free, Carrier Free, sterile, RNase free, 50 U/µL | |
T4 DNA Polymerase | EnzymoPure™, Animal Free, Carrier Free, Bioactive, ActiBioPure™, sterile, RNase free, 5.0 U/μL | |
T4 DNA Polymerase | Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,3 U/μL | |
T7 RNA Polymerase | ActiBioPure™, Carrier Free, Bioactive, EnzymoPure™, 1KU/μL | |
Taq DNA Polymerase | Recombinant,Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,≥99%(SDS-PAGE),5 U/μl | |
Taq DNA Polymerase | Recombinant,Suitable for molecular biology,EnzymoPure™,for DNA and RNA applications,5 U/μL | |
Whole Blood polymerase | EnzymoPure™, 1.25U/μl | |
Taq-HS DNA Polymerase | EnzymoPure™ | |
AbTaq DNA Polymerase | EnzymoPure™ | |
Hot Start Taq DNA Polymerase | EnzymoPure™, 5U/μL | |
Taq DNA Polymerase, Glycerol-free | -- | |
Taq DNA Polymerase | EnzymoPure™ | |
Tte UvrD Helicase | -- | |
AlkB (RNA/DNA demethylase, Nuclease-free) | EnzymoPure™, ActiBioPure™, Bioactive, Animal Free, Carrier Free, sterile, RNase free, 20 U/µL | |
AluI Methyltransferase | -- | |
CpG Methyltransferase | -- | |
EcoRI Methyltransferase | -- | |
GpC Methyltransferase | -- | |
HaeIII Methyltransferase | -- | |
Hhal Methyltransferase | -- | |
dam Methyltransferase | -- | |
mRNA Cap 2'-O-methyltransferase | -- |
10.2 Supporting Reagents for Studies on Nucleic Acid Metabolism and Immune Defense Mechanisms
Name | CAS No. | Experimental Stage | Key Use | Usage Notes |
β-Amanitin | Transcription inhibition | Inhibits RNA Pol II transcription | Suitable for short-term transcriptional blockade | |
Triptolide | Transcription initiation intervention | Inhibits the transcription initiation complex | Start with a low-dose gradient | |
Flavopiridol | Transcription elongation inhibition | Inhibits CDK9-dependent elongation | Combine with nascent RNA readouts | |
Cordycepin | RNA 3′ end processing/degradation | Perturbs poly(A) metabolism and RNA homeostasis | Commonly used for transcript half-life measurements | |
Pladienolide B | Splicing intervention | Targets the SF3B complex | Suitable for monitoring pre-mRNA accumulation | |
Spliceostatin A | Splicing inhibition | Inhibits pre-mRNA splicing | More informative when combined with splice-isoform qPCR | |
Isoginkgetin | pre-mRNA splicing | Inhibits spliceosome assembly | Suitable for alternative splicing studies | |
Brr2 Inhibitor C9 | RNA helicase/splicing | Perturbs spliceosomal RNA helicase activity | Suitable for fine mechanistic dissection | |
3-Deazaadenosine | Methylation/SAH cycle | Perturbs methylation reaction flux | Note its broad effects on methylation pathways | |
Sinefungin | Methyltransferase inhibition | Inhibits nucleic acid-related methylation | Suitable for initial screening at the modification level | |
5-Azacytidine | DNA methylation regulation | Inhibits DNMT1 and remodels gene expression programs | Suitable for epigenetic-level validation | |
Decitabine | DNA demethylation | Validates the impact of DNA methylation on transcription | Suitable for long-term treatment models | |
cGAMP disodium | STING activation | Activates the cytosolic DNA-sensing pathway | Suitable for IFN readout systems | |
H-151 | STING blockade | Inhibits STING-dependent signaling | Pair with a cGAMP treatment group | |
RU.521 | cGAS inhibition | Blocks upstream recognition of cytosolic DNA | Suitable for dissection of the cGAS-STING axis | |
PKR inhibitor C16 | dsRNA response inhibition | Inhibits the PKR pathway | Combine with eIF2α and stress-response readouts | |
Ruxolitinib | Downstream IFN blockade | Inhibits JAK1/2 signaling | Suitable for validation of interferon-dependent effects | |
Tofacitinib | JAK-STAT intervention | Inhibits post-sensing signal amplification | Suitable for inflammatory transcriptional readouts |
Cellular nucleic acid metabolic and regulatory enzymes constitute a continuous functional system spanning the establishment of gene expression, the maintenance of RNA homeostasis, and the execution of immune defense. Together, they determine when nucleic acids are synthesized, how they are processed, in what form they exist, when they are degraded, and when they are recognized as danger signals. Only by understanding nucleic acid metabolism, post-transcriptional regulation, and innate immunity within a unified framework can the true mechanistic value of this system in cellular homeostasis, disease development, and intervention design be more accurately defined.