SNRNP70 Antibody

What is SNRNP70 and why is it important in cellular function?

SNRNP70 (Small Nuclear Ribonucleoprotein 70kDa) is a critical component of the U1 small nuclear ribonucleoprotein (snRNP) complex that plays an essential role in pre-mRNA splicing. This protein recognizes and binds to the 5' splice site of pre-mRNA, initiating the assembly of the spliceosome complex. The importance of SNRNP70 lies in its fundamental role in RNA processing, which directly impacts gene expression regulation. Recent research has demonstrated that SNRNP70 regulates alternative splicing events in various genes, including CD55, WARS1, ABI1, EML3, SNHG5, PPFIBP1, and IFI16 . The dysregulation of SNRNP70 has been implicated in several pathological conditions, particularly in cancer progression, where altered splicing patterns can lead to the expression of protein isoforms that promote oncogenic processes. Understanding SNRNP70 function is therefore crucial for elucidating the molecular mechanisms underlying normal cellular processes and disease development.

What types of SNRNP70 antibodies are available for research?

Researchers have access to several types of SNRNP70 antibodies that target different epitopes of the protein, each with specific applications in molecular biology research:

• N-terminal targeting antibodies: These antibodies recognize epitopes in the N-terminal region of SNRNP70. For example, rabbit polyclonal antibodies are available that target a synthetic peptide corresponding to the N-terminal sequence "PHNDPNAQGD AFKTLFVARV NYDTTESKLR REFEVYGPIK RIHMVYSKRS" . These antibodies typically demonstrate broad species cross-reactivity, including human, mouse, rat, dog, cow, zebrafish, guinea pig, and horse samples .

• C-terminal targeting antibodies: These recognize the C-terminal region of SNRNP70 and may offer different specificity profiles compared to N-terminal antibodies.

• PrecisionAb Polyclonal antibodies: These are purified rabbit polyclonal IgG antibodies that have undergone rigorous validation to ensure reliable performance in techniques such as Western blotting. They detect SNRNP70 at approximately 58 kDa in cell lysates, particularly in Jurkat cells .

Most commercially available SNRNP70 antibodies are in purified IgG liquid form, prepared by affinity chromatography, and formulated in phosphate-buffered saline with preservatives such as 0.09% sodium azide and 2% sucrose .

How are SNRNP70 antibodies validated for specificity?

Validation of SNRNP70 antibodies involves multiple complementary approaches to ensure specificity and reliability in research applications. The primary validation methods include:

• Western blotting validation: Antibodies are tested on cell lysates known to express SNRNP70, such as Jurkat cells, where they should detect a specific band at approximately 58 kDa . This confirms the antibody recognizes a protein of the expected molecular weight.

• Cross-reactivity testing: Antibodies are evaluated across multiple species to determine their range of applicability. For example, SNRNP70 antibodies may show predicted reactivity with various species including human, mouse, rat, cow, dog, guinea pig, rabbit, horse, and zebrafish samples .

• Immunohistochemistry validation: Antibodies are tested on fixed tissue sections to evaluate their performance in detecting the spatial distribution of SNRNP70 in intact tissues .

• Antibody depletion studies: For advanced validation, knockdown or knockout cell lines can be used to confirm the specificity of the antibody signal. As demonstrated in research, siRNA-mediated knockdown of SNRNP70 results in reduced antibody staining, confirming specificity .

• Performance validation programs: Some antibodies, like those with the PrecisionAb label, undergo additional validation within established programs that evaluate performance against defined criteria, ensuring consistency and reliability across batches .

What are the primary applications of SNRNP70 antibodies in molecular biology?

SNRNP70 antibodies serve multiple critical functions in molecular biology research, with applications extending beyond basic protein detection:

• Western Blotting (WB): This represents the most common application, where SNRNP70 antibodies detect the protein at approximately 58 kDa in cell lysates. The recommended dilution for Western blotting is typically 1/1000 , though optimization may be necessary depending on the specific antibody and sample type. Western blotting allows researchers to quantify SNRNP70 expression levels across different experimental conditions or tissue samples.

• Immunohistochemistry (IHC): SNRNP70 antibodies enable visualization of protein localization within tissue sections, providing spatial information about expression patterns . This technique is particularly valuable for examining SNRNP70 distribution in normal versus pathological tissues, such as comparing primary tumors with metastatic samples.

• RNA Immunoprecipitation (RIP): SNRNP70 antibodies are used to precipitate SNRNP70-RNA complexes, allowing identification of RNA targets. Research has employed this technique to confirm direct interactions between SNRNP70 and target pre-mRNAs such as CD55 .

• Protein-Protein Interaction Studies: Through co-immunoprecipitation experiments, SNRNP70 antibodies help identify protein binding partners involved in splicing regulation and other cellular processes.

• Chromatin Immunoprecipitation (ChIP): Although less common, SNRNP70 antibodies can be used in ChIP assays to investigate potential associations with chromatin, which may provide insights into the coupling between transcription and splicing.

Each application requires specific optimization of antibody concentration, incubation conditions, and detection methods to achieve reliable and reproducible results.

How can SNRNP70 antibodies be used in cancer research?

SNRNP70 antibodies have emerged as valuable tools in cancer research, particularly for investigating altered splicing mechanisms that contribute to tumor progression:

• Expression analysis in cancer tissues: Recent research has utilized SNRNP70 antibodies to demonstrate upregulation in osteosarcoma (OS) tissues, where elevated expression correlates with poor prognosis in patients . Similar approaches can be applied to other cancer types to identify potential biomarkers.

• Functional studies: SNRNP70 antibodies help monitor the effects of experimental manipulation (overexpression or knockdown) on cancer cell behavior. For instance, researchers have shown that SNRNP70 overexpression enhances proliferation and metastasis of OS cells in vitro, while its depletion reduces these capabilities in vivo .

• Mechanistic investigations: Combining SNRNP70 antibodies with splicing analysis techniques helps elucidate how this protein regulates alternative splicing events in cancer. Research has revealed that SNRNP70 directly interacts with CD55, modulating its alternative splicing to promote tumor progression in OS .

• Therapeutic target validation: SNRNP70 antibodies can assess the efficacy of targeting splicing factors in cancer treatment. Studies have confirmed that SNRNP70 knockdown inhibits OS progression and metastasis, supporting its potential as a therapeutic target .

• Immunohistochemical evaluation: Using SNRNP70 antibodies for IHC staining of tumor sections provides insights into protein distribution within the tumor microenvironment. This approach can reveal associations between SNRNP70 expression and specific cell populations or tumor regions.

The application of SNRNP70 antibodies in cancer research has already contributed to understanding the role of alternative splicing in tumor biology and identified potential new therapeutic approaches.

What role does SNRNP70 play in alternative splicing analysis?

SNRNP70 is a key regulatory factor in alternative splicing processes, and antibodies against this protein are instrumental in dissecting its specific functions:

• Identification of regulated splicing events: Research using SNRNP70 antibodies has revealed that this protein regulates specific alternative splicing events in several genes. For example, SNRNP70 positively correlates with the splicing of CD55, WARS1, and ABI1, while negatively correlating with the splicing of EML3, SNHG5, PPFIBP1, and IFI16 .

• Characterization of splicing mechanisms: Studies have identified specific types of alternative splicing regulated by SNRNP70, including exon skipping (e.g., skipping of exon 10 in CD55 pre-mRNA), exon inclusion (e.g., inclusion of exon 10 in PPFIBP1 pre-mRNA), mutually exclusive exons (e.g., exons 7 and 8 in IFI16 pre-mRNA), intron retention, and alternative 3′ splice site (A3SS) selection (e.g., involving exons 21 and 22 in EML3 pre-mRNA) .

• RNA-protein interaction studies: SNRNP70 antibodies are employed in RNA immunoprecipitation (RIP) assays to identify direct interactions between SNRNP70 and target pre-mRNAs. This approach, combined with RNA pulldown assays, has experimentally validated the interaction between SNRNP70 and CD55 .

• Functional consequences of splicing regulation: By manipulating SNRNP70 expression and using antibodies to confirm changes in protein levels, researchers have demonstrated that SNRNP70-mediated alternative splicing of CD55 (specifically the CD55-Δe10 isoform) promotes oncogenic properties in osteosarcoma cells .

• Splicing factor complex analysis: SNRNP70 antibodies help identify components of splicing complexes through co-immunoprecipitation experiments, providing insights into the molecular mechanisms of splicing regulation.

These applications highlight the central role of SNRNP70 in splicing regulation and the value of SNRNP70 antibodies in advancing our understanding of this complex process.

What are the optimal conditions for using SNRNP70 antibodies in Western blotting?

Optimizing Western blotting protocols for SNRNP70 detection requires careful consideration of several experimental parameters:

• Sample preparation:

  • Cell lysates should be prepared using RIPA buffer containing protease inhibitors to prevent protein degradation

  • Jurkat cell lysates serve as positive controls, as they consistently express detectable levels of SNRNP70

  • Protein concentration should be determined and standardized (typically 20-30 μg total protein per lane)

• Antibody dilution and incubation:

  • The recommended starting dilution for most SNRNP70 antibodies is 1/1000

  • Primary antibody incubation is typically performed overnight at 4°C for optimal binding

  • For challenging samples, extending incubation time or adjusting antibody concentration may improve signal

• Detection parameters:

  • SNRNP70 antibodies detect a band of approximately 58 kDa in Western blots

  • Enhanced chemiluminescence (ECL) detection systems provide adequate sensitivity for most applications

  • For quantitative analysis, ensure exposure times remain in the linear range of detection

• Secondary antibody selection:

  • For rabbit polyclonal SNRNP70 antibodies, an anti-rabbit IgG HRP-conjugated secondary antibody is appropriate

  • Products like Goat anti-Rabbit IgG (H/L):HRP (e.g., STAR208P) are compatible with these primary antibodies

  • Secondary antibody dilution typically ranges from 1:5,000 to 1:10,000

• Optimization considerations:

  • If background is high, increasing blocking time or adding 0.1% Tween-20 to wash buffers may help

  • If signal is weak, reducing wash stringency or increasing antibody concentration may improve detection

  • For multiple protein detection, stripping and reprobing should be minimized as it may reduce SNRNP70 signal

These conditions should be systematically optimized for each experimental system to ensure consistent and reproducible results.

How should researchers design immunohistochemistry experiments with SNRNP70 antibodies?

Designing effective immunohistochemistry (IHC) experiments with SNRNP70 antibodies requires attention to sample preparation, antigen retrieval, and detection methods:

• Tissue preparation:

  • Tissues should be fixed in 10% neutral-buffered formalin and embedded in paraffin

  • Section thickness of 4-6 μm is generally optimal for SNRNP70 detection

  • For tumor samples, inclusion of adjacent normal tissue provides internal control for expression comparison

• Antigen retrieval:

  • Heat-induced epitope retrieval (HIER) using citrate buffer (pH 6.0) is typically effective for SNRNP70 detection

  • Pressure cooker or microwave-based retrieval methods for 15-20 minutes often yield optimal results

  • Cooling sections slowly to room temperature after retrieval prevents tissue detachment

• Antibody incubation:

  • Blocking with 5% normal serum (matching the species of the secondary antibody) reduces background

  • Primary SNRNP70 antibody dilution should be determined empirically, starting with manufacturer recommendations

  • Incubation overnight at 4°C typically provides optimal staining with minimal background

• Detection systems:

  • For brightfield microscopy, HRP-based detection systems with DAB substrate are commonly used

  • For fluorescence detection, fluorophore-conjugated secondary antibodies allow co-localization studies

  • Amplification systems (e.g., tyramide signal amplification) may enhance sensitivity for low-abundance detection

• Controls and validation:

  • Positive control tissues known to express SNRNP70 should be included in each experiment

  • Negative controls (omitting primary antibody) help identify non-specific binding

  • When possible, include SNRNP70 knockdown samples as specificity controls, as demonstrated in research where SNRNP70 knockdown resulted in reduced IHC staining

• Evaluation metrics:

  • Both staining intensity and percentage of positive cells should be assessed

  • Semi-quantitative scoring systems (e.g., H-score) enable comparison across experimental groups

  • Digital image analysis can provide objective quantification of staining patterns

These methodological considerations ensure reliable and reproducible SNRNP70 detection in tissue samples, facilitating accurate interpretation of expression patterns.

What controls should be included when using SNRNP70 antibodies in research?

Rigorous experimental design with appropriate controls is essential for generating reliable data with SNRNP70 antibodies:

• Positive controls:

  • Cell lines with known SNRNP70 expression: Jurkat cells are particularly useful as they consistently express detectable levels of SNRNP70 protein

  • Tissues with established SNRNP70 expression patterns: For IHC experiments, including tissues known to express SNRNP70

  • Recombinant SNRNP70 protein: Can serve as a positive control for antibody specificity testing

• Negative controls:

  • Primary antibody omission: Samples processed identically but without primary antibody addition help identify non-specific binding of secondary antibodies

  • Isotype controls: Using non-specific IgG from the same species as the primary antibody helps distinguish specific from non-specific binding

  • SNRNP70 knockdown/knockout samples: As demonstrated in research, siRNA-mediated SNRNP70 knockdown samples provide the most stringent specificity control

• Experimental validation controls:

  • Loading controls for Western blotting: Probing for housekeeping proteins (e.g., GAPDH, β-actin) ensures equal protein loading

  • Tissue architecture controls for IHC: H&E staining of adjacent sections confirms tissue integrity

  • Transfection efficiency controls: When overexpressing or knocking down SNRNP70, confirming the modification at both protein and mRNA levels is essential

• Cross-reactivity controls:

  • Testing antibodies on samples from multiple species when cross-species reactivity is claimed

  • Peptide competition assays: Pre-incubating the antibody with the immunizing peptide should abolish specific signal

  • Testing on cell lines with variable SNRNP70 expression levels to confirm signal correlation with expression

• Technical replicates and biological replicates:

  • Multiple technical replicates minimize procedural variability

  • Independent biological replicates (different patients/animals/cell preparations) confirm biological relevance

Implementing these controls ensures the reliability and reproducibility of results obtained with SNRNP70 antibodies, facilitating accurate interpretation of experimental findings.

What are common issues encountered with SNRNP70 antibodies and how can they be resolved?

Researchers working with SNRNP70 antibodies may encounter several technical challenges that can be addressed through systematic troubleshooting:

• Weak or absent signal in Western blotting:

  • Issue: Insufficient protein or antibody concentration

  • Resolution: Increase protein loading (up to 50 μg), optimize antibody dilution, extend incubation time, or use more sensitive detection systems

  • Issue: Protein degradation

  • Resolution: Use fresh samples, add additional protease inhibitors, maintain cold temperatures during preparation

• Multiple bands or non-specific binding:

  • Issue: Cross-reactivity with related proteins

  • Resolution: Increase blocking time/concentration, optimize antibody dilution, perform more stringent washes, or consider a different antibody targeting a different epitope

  • Issue: Detection of splice variants or post-translationally modified forms

  • Resolution: Confirm band identity through knockdown experiments or mass spectrometry analysis

• High background in immunohistochemistry:

  • Issue: Insufficient blocking or non-specific binding

  • Resolution: Extend blocking time, use additional blocking agents (e.g., BSA, normal serum), optimize antibody dilution, or include additional wash steps

  • Issue: Endogenous peroxidase activity

  • Resolution: Include hydrogen peroxide treatment step before antibody incubation

• Inconsistent immunoprecipitation results:

  • Issue: Inefficient antibody binding or protein capture

  • Resolution: Increase antibody amount, extend incubation time, optimize buffer conditions, or use magnetic beads instead of agarose

  • Issue: Co-precipitating proteins mask target detection

  • Resolution: Use more stringent wash conditions or denaturing elution methods

• Variable results across experiments:

  • Issue: Antibody lot-to-lot variation

  • Resolution: Validate each new lot against previous lots, maintain consistent experimental conditions

  • Issue: Sample variability

  • Resolution: Standardize sample collection and processing methods, include appropriate controls

By systematically addressing these issues, researchers can optimize SNRNP70 antibody performance and generate reliable, reproducible results in their experiments.

How can researchers verify the specificity of bands detected by SNRNP70 antibodies?

Verifying the specificity of bands detected by SNRNP70 antibodies is crucial for accurate data interpretation and requires multiple complementary approaches:

• Molecular weight verification:

  • SNRNP70 should be detected at approximately 58 kDa in Western blots

  • Precision protein markers should be used to accurately determine band size

  • Any additional bands should be critically evaluated for potential splice variants or post-translational modifications

• Gene silencing approaches:

  • siRNA/shRNA-mediated knockdown: As demonstrated in research, transfection of cells with SNRNP70 siRNA should result in significant reduction of the specific band

  • CRISPR-Cas9 knockout: Complete elimination of the target band in knockout cells provides definitive evidence of specificity

  • Observation: Both approaches should diminish or eliminate the specific SNRNP70 band while leaving non-specific bands unchanged

• Overexpression validation:

  • Transfection with SNRNP70 expression plasmids should increase band intensity at the expected molecular weight

  • Research has shown that following transfection with SNRNP70 overexpression plasmids, both protein and mRNA levels are upregulated

  • Tagged SNRNP70 constructs (e.g., FLAG, HA) allow detection with tag-specific antibodies for confirmation

• Peptide competition assays:

  • Pre-incubating the antibody with the immunizing peptide should specifically block binding to SNRNP70

  • The target band should disappear or be significantly reduced while non-specific bands remain unchanged

  • Titration of blocking peptide can determine the specificity threshold

• Multiple antibody validation:

  • Using different antibodies targeting distinct epitopes of SNRNP70 should yield consistent results

  • Comparison of N-terminal and C-terminal targeting antibodies can help identify specific isoforms

  • Monoclonal antibodies may provide higher specificity than polyclonal antibodies in some applications

• Mass spectrometry confirmation:

  • For definitive identification, the band of interest can be excised and analyzed by mass spectrometry

  • This approach provides unambiguous protein identification based on peptide sequence

These verification methods, especially when used in combination, provide robust evidence for the specificity of bands detected by SNRNP70 antibodies, ensuring reliable interpretation of experimental results.

What approaches can be used to address cross-reactivity concerns with SNRNP70 antibodies?

Cross-reactivity can compromise the reliability of SNRNP70 antibody-based experiments, but several strategies can mitigate this concern:

• Epitope selection and antibody design:

  • Choose antibodies targeting unique regions of SNRNP70 with minimal sequence homology to related proteins

  • The N-terminal region of SNRNP70 contains sequences with less conservation across paralogs, potentially offering greater specificity

  • Consider monoclonal antibodies that recognize a single epitope for applications requiring high specificity

• Experimental optimization:

  • Titrate antibody concentration to find the optimal balance between specific signal and background

  • For Western blotting, increase blocking time and stringency of wash conditions

  • For IHC, optimize antigen retrieval and detection systems to minimize non-specific binding

  • Include detergents like Tween-20 in wash buffers to reduce hydrophobic interactions causing cross-reactivity

• Validation in knockout/knockdown systems:

  • Generate or obtain SNRNP70 knockout or knockdown samples as definitive controls

  • Compare antibody reactivity in wild-type versus SNRNP70-depleted samples

  • Research has demonstrated that SNRNP70 knockdown results in reduced antibody staining, confirming specificity

• Species-specific considerations:

  • When working across species, select antibodies validated for the species of interest

  • Review predicted reactivity information (e.g., Cow: 100%, Dog: 100%, Guinea Pig: 100%, Horse: 100%, Human: 100%, Mouse: 100%, Rabbit: 100%, Rat: 100%, Zebrafish: 100%)

  • For novel species applications, conduct preliminary validation experiments

• Advanced specificity techniques:

  • Peptide competition assays: Pre-incubating the antibody with the immunizing peptide should abolish specific signal

  • Dual detection strategies: Using antibodies against different epitopes of SNRNP70 should yield overlapping signals

  • Orthogonal detection methods: Confirm findings using alternative techniques (e.g., mass spectrometry, RNA-seq for splicing changes)

• Data interpretation strategies:

  • Always examine the entire blot/image rather than cropped regions

  • Report all observed bands and their molecular weights

  • Consider potential splice variants or post-translational modifications that might explain unexpected bands

By implementing these approaches, researchers can minimize cross-reactivity concerns and increase confidence in the specificity of SNRNP70 antibody-based results.

How is SNRNP70 involved in osteosarcoma progression?

Recent research has established SNRNP70 as a critical factor in osteosarcoma (OS) progression through several interconnected mechanisms:

• Expression and prognostic significance:

  • SNRNP70 is significantly upregulated in OS tissues compared to normal bone tissues

  • Elevated SNRNP70 expression correlates with poor prognosis in OS patients, suggesting its potential as a prognostic biomarker

  • Both differential expression and differential splicing of SNRNP70 have been observed in OS samples

• Functional impact on tumor cell behavior:

  • Overexpression of SNRNP70 enhances the proliferative capacity of OS cells in vitro

  • SNRNP70 promotes migration and invasion of OS cells, critical properties for metastasis

  • In colony formation assays, SNRNP70 overexpression significantly increases the clonogenic potential of OS cells

  • Knockdown of SNRNP70 reduces these malignant properties, confirming its pro-oncogenic role

• In vivo validation of oncogenic function:

  • SNRNP70 knockdown in OS cells significantly reduces tumor growth when implanted into mouse models

  • Both the average weight and volume of tumors are decreased in SNRNP70-knockdown xenografts compared to controls

  • Immunohistochemical analysis shows reduced Ki-67 positive cells in SNRNP70-knockdown tumors, indicating decreased proliferation

  • SNRNP70 knockdown significantly diminishes lung metastasis formation in mouse models, with smaller and fewer metastatic nodules

• Molecular mechanism involving CD55 splicing regulation:

  • SNRNP70 directly interacts with CD55 pre-mRNA, as confirmed by RNA immunoprecipitation and RNA pulldown assays

  • This interaction regulates alternative splicing of CD55, promoting the CD55-Δe10 isoform

  • The CD55-Δe10 isoform is more abundantly expressed in OS cell lines compared to normal bone cells

  • Knockdown of CD55-Δe10 inhibits the oncogenic effects of SNRNP70 overexpression, establishing a causal relationship

These findings collectively establish SNRNP70 as a promising therapeutic target for OS treatment, with potential applications in developing novel splicing-modulating therapies.

What splicing mechanisms are regulated by SNRNP70 in cancer cells?

SNRNP70 orchestrates complex splicing regulatory networks in cancer cells, influencing multiple genes through diverse splicing mechanisms:

• Types of alternative splicing events regulated:

  • Exon skipping: SNRNP70 induces skipping of exon 10 in CD55 pre-mRNA in osteosarcoma cells

  • Exon inclusion: SNRNP70 promotes inclusion of exon 10 in PPFIBP1 pre-mRNA

  • Mutually exclusive exons: SNRNP70 regulates selection between exons 7 and 8 in IFI16 pre-mRNA

  • Intron retention: SNRNP70 controls inclusion of an intron between exons 21 and 22 in EML3 pre-mRNA

  • Alternative 3′ splice site selection: SNRNP70 modulates A3SS events involving exons 21 and 22 in EML3

• Gene targets with oncogenic implications:

  • CD55 (Complement decay-accelerating factor): SNRNP70-regulated splicing produces the CD55-Δe10 isoform that promotes osteosarcoma progression

  • WARS1 (Tryptophanyl-tRNA synthetase): Splicing positively correlated with SNRNP70 expression

  • ABI1 (Abl interactor 1): Splicing positively correlated with SNRNP70 expression

  • EML3 (Echinoderm microtubule-associated protein-like 3): Splicing negatively correlated with SNRNP70 expression

  • SNHG5 (Small nucleolar RNA host gene 5): Splicing negatively correlated with SNRNP70 expression

  • PPFIBP1 (Liprin beta 1): Splicing negatively correlated with SNRNP70 expression

  • IFI16 (Interferon gamma inducible protein 16): Splicing negatively correlated with SNRNP70 expression

• Molecular mechanisms of splicing regulation:

  • Direct RNA binding: SNRNP70 directly interacts with target pre-mRNAs through recognition of specific RNA sequences

  • Spliceosome assembly modulation: As a component of the U1 snRNP complex, SNRNP70 influences early spliceosome assembly

  • Recruitment of cofactors: SNRNP70 likely recruits additional splicing regulators to specific splice sites

  • Competition with other splicing factors: SNRNP70 may antagonize or synergize with other RNA-binding proteins at shared target sites

• Functional consequences of SNRNP70-regulated splicing:

  • Production of protein isoforms with altered function: The CD55-Δe10 isoform generated through SNRNP70-mediated splicing promotes oncogenic properties in osteosarcoma cells

  • Impact on signaling pathways: SNRNP70 expression correlates with altered ADGRE5/CD55 signaling between osteoblastic cells and macrophages

  • Metabolic reprogramming: In metastatic samples with upregulated SNRNP70, activation of metabolic pathways including the tricarboxylic acid cycle, oxidative phosphorylation, and the pentose phosphate pathway was observed

These splicing mechanisms represent potential therapeutic vulnerabilities in cancer cells, where targeting SNRNP70 could disrupt oncogenic splicing patterns.

What are emerging applications of SNRNP70 antibodies in studying disease mechanisms?

SNRNP70 antibodies are increasingly being utilized in innovative approaches to understand disease mechanisms, particularly in cancer and other splicing-related disorders:

• Single-cell analysis of splicing factor distribution:

  • SNRNP70 antibodies enable identification of cell-specific expression patterns within heterogeneous tissues

  • Single-cell RNA sequencing combined with protein analysis has revealed communication between SNRNP70-expressing osteoblastic cells and macrophages via the ADGRE5/CD55 signaling pathway

  • This approach identifies specific cell populations where SNRNP70-mediated splicing regulation is most active

• Tumor microenvironment interactions:

  • SNRNP70 antibodies help characterize tumor-immune cell interactions

  • Research has shown that metastatic osteosarcoma samples with high SNRNP70 expression exhibit increased infiltration of resting immune cells but reduced infiltration of M0 macrophages

  • Understanding these interactions may reveal how splicing regulation impacts immune surveillance and response

• Therapeutic target validation:

  • SNRNP70 antibodies are essential for monitoring the efficacy of splicing-modulating therapeutics

  • In vivo studies have demonstrated that SNRNP70 knockdown inhibits both tumor growth and metastasis in osteosarcoma models

  • Antibodies allow precise quantification of target engagement and downstream effects of SNRNP70-targeting therapies

• Biomarker development:

  • SNRNP70 expression analysis using antibodies may serve as a prognostic or predictive biomarker

  • Elevated SNRNP70 levels correlate with poor prognosis in osteosarcoma patients

  • Immunohistochemical evaluation of SNRNP70 in patient samples could guide treatment decisions

• Mechanistic studies of splicing dysregulation:

  • SNRNP70 antibodies facilitate investigation of spliceosome assembly and function

  • Chromatin immunoprecipitation with SNRNP70 antibodies can reveal co-transcriptional splicing regulation

  • Combined with RNA-seq, these approaches provide comprehensive views of splicing regulation in disease contexts

• Metabolic pathway analysis:

  • Research using SNRNP70 antibodies has revealed correlations between SNRNP70 expression and activation of specific metabolic pathways

  • In datasets where SNRNP70 was upregulated in metastatic samples, pathways including the tricarboxylic acid cycle, oxidative phosphorylation, and the pentose phosphate pathway were activated

  • This suggests broader roles for SNRNP70 in cellular metabolism beyond direct splicing regulation

These emerging applications highlight the expanding utility of SNRNP70 antibodies beyond traditional protein detection, positioning them as valuable tools for understanding complex disease mechanisms and developing novel therapeutic strategies.