Recombinant Retrotransposon-like protein 1 (retr-1), partial

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Description

Research Applications

Recombinant partial RETR-1 is primarily used to study:

  • Genomic imprinting: Mechanistic insights into paternal allele-specific expression in placental development .

  • Fetal capillary maintenance: Knockout models show late-stage fetal/neonatal death due to placental insufficiency .

  • Muscle hypertrophy: Overexpression in sheep homologs links RETR-1 to skeletal muscle overgrowth .

Notable findings from recombinant studies:

  • In vitro assays: Partial RETR-1 lacking the integrase domain retains RNA-binding capacity but cannot mediate retrotransposition .

  • Interaction networks: Binds host factors like MOV10 and SAMHD1, suggesting roles in RNP condensate formation .

Disease Associations

ConditionRETR-1 DysregulationMechanismSource
Placental insufficiencyReduced RETR-1 expressionLoss of fetal capillary integrity
CancerEpigenetic derepressionLINE-1/RETR-1 coactivation
Muscle disordersOverexpression (e.g., callipyge)miRNA dysregulation (miR-432)

Evolutionary Insights

  • Origins: RETR-1 evolved from a sushi-ishi retrotransposon ~100 million years ago, losing retrotransposition capability but retaining regulatory roles .

  • Repeat expansions: Species-specific tandem repeats (e.g., TRB, TRC in rodents) correlate with miRNA diversification (e.g., miR-434 in mice) .

Comparative analysis of RETR-1 homologs:

SpeciesRepeat TypemiRNA ProducedFunction
HumanTRBmiR-432Post-transcriptional silencing
MouseTRCmiR-434Muscle development
SheepTRAN/ACallipyge phenotype

Technical Challenges and Future Directions

  • Expression hurdles: Recombinant RETR-1 forms cytotoxic aggregates unless coexpressed with chaperones .

  • Therapeutic potential: Targeting RETR-1-associated miRNAs (e.g., antagomirs for miR-432) may mitigate placental pathologies .

Open questions:

  • How do RETR-1 condensates regulate LINE-1 retrotransposons in cancer?

  • Can partial RETR-1 be used to model imprinting disorders like Prader-Willi syndrome?

Product Specs

Form
Lyophilized powder. We will typically ship the available format. If you have specific format requirements, please note them when ordering.
Lead Time
Delivery times vary based on purchasing method and location. Contact your local distributor for specific delivery details. All proteins are shipped with standard blue ice packs. Request dry ice shipment in advance (extra fees apply).
Notes
Avoid repeated freezing and thawing. Working aliquots can be stored at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening. Reconstitute the protein in sterile deionized water to a concentration of 0.1-1.0 mg/mL. Add 5-50% glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%.
Shelf Life
Shelf life depends on storage conditions, buffer components, storage temperature, and protein stability. Liquid form typically lasts 6 months at -20°C/-80°C. Lyophilized form typically lasts 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon arrival. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type is determined during manufacturing. If you require a specific tag, please inform us, and we will prioritize its development.
Synonyms
retr-1; F44E2.2; Retrotransposon-like protein 1; EC 3.4.23.-
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Protein Length
Partial
Purity
>85% (SDS-PAGE)
Species
Caenorhabditis elegans
Target Names
retr-1
Uniprot No.

Q&A

What is Retrotransposon-like Protein 1 (RETR-1)?

While the search results don't provide specific information about RETR-1, we can note that retrotransposon-like proteins are generally involved in genomic regulation. RETR-1 would likely be characterized by domains and motifs similar to those found in retrotransposons, which are genetic elements that can copy and move themselves to new positions within a genome.

The naming convention "partial" typically indicates that the protein sequence or structure being studied represents only a portion of the complete protein, which may have implications for experimental design and interpretation of results.

How does RETR-1 differ from other retrotransposon-like proteins?

Without specific information from the search results, researchers should consider:

  • Conducting sequence alignment analyses to identify unique domains or motifs

  • Performing comparative structural analyses with related proteins

  • Examining evolutionary conservation patterns across species

Similar to how H9-RETR was characterized against other IL-2 analogues through functional assays that measured signal transduction efficiency , RETR-1 would likely need to be compared with other retrotransposon-like proteins through appropriate functional assays.

What are the common methods for producing recombinant RETR-1?

Based on methodological approaches for other recombinant proteins:

  • Expression systems: Selection between bacterial (E. coli), yeast, insect, or mammalian cell systems

  • Vector design: Incorporation of appropriate promoters, selection markers, and fusion tags

  • Purification strategies: Affinity chromatography methods based on incorporated tags

Researchers might consider approaches similar to those used for IL-2 variants, which employed site-directed mutagenesis to create modified proteins that retained specific binding characteristics while altering others .

What are the key considerations for designing experiments involving recombinant RETR-1?

While specific information is lacking in the search results, researchers should:

  • Establish appropriate controls for recombinant protein activity

  • Consider potential interference from fusion tags or expression system artifacts

  • Validate protein folding and post-translational modifications

Similar to studies of IL-2 variants, which assessed multiple parameters of signaling (pSTAT5, pERK1/2, S6 ribosomal protein) , a comprehensive approach to evaluating RETR-1 function would be recommended.

How can I assess the functional activity of recombinant RETR-1?

Researchers might consider:

  • Binding assays to identify interaction partners

  • Cellular localization studies using fluorescent tags

  • Transcriptional impact assessment using RNA-seq or specific target gene analysis

As seen with H9-RETR, which was evaluated for its effects on different cell types and compared to other variants , RETR-1 would likely need to be assessed across multiple biological contexts.

What are the challenges in ensuring reproducibility in RETR-1 experiments?

Drawing from principles in the third search result about researcher bias:

  • Pre-register experimental protocols to avoid bias in analysis and reporting

  • Consider multiverse analysis approaches when exploring novel properties

  • Document all data cleaning and processing steps transparently

  • Clearly report any prior access to data that might influence interpretations

How can I design experiments to study RETR-1 interactions with chromatin remodeling complexes?

Advanced approaches might include:

  • Chromatin immunoprecipitation (ChIP) assays adapted for RETR-1

  • Proximity labeling techniques (BioID or APEX) to identify interaction partners

  • CRISPR-based screens to identify genetic dependencies

Similar to how ChIP-Seq was used to evaluate STAT5 binding in response to IL-2 variants , genome-wide approaches would likely provide valuable insights into RETR-1 function.

What computational approaches are recommended for analyzing RETR-1 evolutionary history?

Researchers might consider:

  • Phylogenetic analyses across diverse species

  • Synteny analysis to understand genomic context conservation

  • Detection of selection signatures to identify functionally important domains

These approaches should be combined with experimental validation, similar to how functional assays confirmed computational predictions for IL-2 variant activities .

How can contradictory data about RETR-1 function be reconciled?

Based on principles from the paper on researcher bias in data analysis:

What purification strategies are most effective for obtaining high-quality recombinant RETR-1?

While specific information is not available from the search results, researchers might consider:

  • Multi-step purification protocols combining affinity, ion exchange, and size exclusion chromatography

  • Optimization of buffer conditions to maintain protein solubility and stability

  • Quality control assays including mass spectrometry and circular dichroism to verify structural integrity

How should researchers approach experimental design when studying partial protein constructs?

Based on general principles and drawing from experience with other partial protein constructs:

  • Carefully define domain boundaries based on structural predictions

  • Compare results between different construct designs to identify potential artifacts

  • Consider the impact of missing domains on protein folding, stability, and function

  • Include full-length protein controls when feasible

What are the best practices for detecting potential artifacts in RETR-1 functional assays?

Researchers should:

  • Include appropriate negative controls and vehicle-only treatments

  • Test multiple independent protein preparations

  • Validate findings using complementary methodological approaches

  • Consider dose-response relationships to identify non-specific effects

This approach mirrors the rigorous validation used in studies of IL-2 variants, where multiple signaling readouts and functional assays were employed to characterize protein activity .

How can I determine if observed phenotypes are specific to RETR-1 function?

Researchers should:

  • Implement rescue experiments with wild-type protein

  • Use structure-guided mutagenesis to identify critical functional residues

  • Compare effects across multiple cell types or model systems

  • Apply appropriate statistical methods to distinguish specific from non-specific effects

What statistical approaches are recommended for analyzing RETR-1 experimental data?

Drawing from principles discussed in the paper on researcher bias:

  • Pre-register analytical approaches when possible

  • Consider multiple testing corrections appropriate to the experimental design

  • Implement sensitivity analyses to evaluate robustness of findings

  • Report effect sizes and confidence intervals rather than just p-values

How should apparent contradictions in RETR-1 functional data be approached?

Based on principles from the paper on researcher bias:

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