Recombinant Mouse Prolactin R

Recombinant Mouse Prolactin R

Product No.: P299

[product_table name="All Top" skus="P299"]

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Alternate Names
Prolactin Receptor, Mammotropin, Luterotropic Hormone, Lutetropin
Product Type
Recombinant Protein
Expression Host
NS0 Cells
Species
Mouse
Applications
ELISA Cap

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Select Product Size
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Background

Prolactin Receptor (PRLR) is a member of the cytokine receptor superfamily member that lacks an intrinsic kinase domain and relies on the cytoplasmic Jak tyrosine kinases to transduce signals (1). Prolactin receptors have been localized in a number of peripheral tissues, including tissues involved in reproduction (2). It is also expressed both in the stromal and epithelial compartment of the mammary gland (3). Within the immune system, multiple isoforms of the prolactin receptor serve to mediate the effects of its ligand prolactin. These isoforms are structurally and functionally distinct, causing significant differences in ligand affinities, kinetics of transduction and the transduction proteins activated. Differential activation of these pathways may contribute to the pleiotropism of prolactin action in tissues of the immune system (4). Prolactin receptor is required for normal maternal glucose homeostasis during pregnancy (5).

Protein Details

Purity
>90% by SDS-PAGE and analyzed by silver stain.
Endotoxin Level
<0.1 EU/µg as determined by the LAL method
Fusion Protein Tag
Fc Fusion Protein
Protein Accession No.
Amino Acid Sequence
sppgkpeihk crspdketft cwwnpgsdgg lptnysltys kegekntyec pdyktsgpns cffskqytsi wkiyiitvna tnemgsstsd plyvdvtyiv epepprnltl evkqlkdkkt ylwvkwlppt itdvktgwft meyeirlkse eadeweihft ghqtqfkvfd lypgqkylvq trckpdhgyw srwgqeksie ipndftlkdd iegrmdpksc dkthtcppcp apellggpsv flfppkpkdt lmisrtpevt cvvvdvshed pevkfnwyvd gvevhnaktk preeqynsty rvvsvltvlh qdwlngkeyk ckvsnkalpa piektiskak gqprepqvyt lppsrdeltk nqvsltclvk gfypsdiave wesngqpenn ykttppvlds dgsfflyskl tvdksrwqqg nvfscsvmhe alhnhytqks lslspgk
N-terminal Sequence Analysis
Ser21
State of Matter
Lyophilized
Predicted Molecular Mass
The predicted molecular weight of Recombinant Mouse PRL is Mr 51 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is Mr 60-68 kDa, reducing conditions kDa.
Predicted Molecular Mass
51
Formulation
This recombinant protein was 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 with no calcium, magnesium, or preservatives.
Storage and Stability
This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
Country of Origin
USA
Shipping
Next Day Ambient
NCBI Gene Bank

Leinco Protein Advisor

Powered by AI: AI is experimental and still learning how to provide the best assistance. It may occasionally generate incorrect or incomplete responses. Please do not rely solely on its recommendations when making purchasing decisions or designing experiments.

Recombinant Mouse Prolactin (rPRL) is a valuable tool for research applications due to its well-characterized biological activity and versatility in studying prolactin-related physiological and pathological processes. Here are several reasons why you should consider using Recombinant Mouse Prolactin in your research:

1. Biological Activity and Functional Relevance

Recombinant Mouse Prolactin is fully biologically active and can mimic the effects of endogenous prolactin in various experimental systems. Studies have demonstrated that recombinant mouse prolactin retains its ability to:

  • Stimulate lactation and mammary gland development in vivo.
  • Promote cell proliferation and differentiation in bioassays (e.g., using rat Nb2-11 cells).
  • Influence adipocyte differentiation and gene expression in 3T3-L1 cells, confirming its functional activity in metabolic and developmental contexts.

2. High Purity and Consistency

Recombinant Mouse Prolactin is typically purified to high levels (>99% purity), ensuring reproducibility and reliability in experimental results. This is especially important for dose-response studies and mechanistic investigations.

3. Cost-Effective and Scalable Production

Production methods using E. coli expression systems allow for cost-effective and scalable production of recombinant mouse prolactin. This makes it accessible for large-scale experiments and long-term studies.

4. Versatility in Research Applications

Recombinant Mouse Prolactin can be used in a wide range of research applications, including:

  • Lactation and Mammary Gland Studies: Investigating the role of prolactin in lactation, mammary gland development, and milk production.
  • Metabolic and Adipocyte Research: Studying the effects of prolactin on adipocyte differentiation, lipid metabolism, and energy homeostasis.
  • Neuroendocrinology: Exploring the role of prolactin in neuroendocrine functions and maternal behaviors.
  • Cell Proliferation and Differentiation Assays: Using bioassays to assess the proliferative and differentiative effects of prolactin on various cell types.

5. Cross-Species Compatibility

Recombinant Mouse Prolactin can be used in both mouse and rat models, making it a versatile tool for comparative studies and translational research. Its activity in different species allows for broader applicability in preclinical studies.

6. Support for Mechanistic Studies

The availability of recombinant mouse prolactin enables detailed mechanistic studies, such as:

  • Investigating the signaling pathways activated by prolactin.
  • Examining the effects of prolactin on gene expression and protein synthesis.
  • Assessing the impact of prolactin on cellular and tissue functions.

7. Quality Control and Validation

Recombinant Mouse Prolactin is often validated through rigorous quality control measures, including:

  • SDS-PAGE and Western blot analysis to confirm purity and identity.
  • Cell-based assays to verify biological activity.
  • Cytotoxicity analysis to ensure safety for use in cell culture and in vivo experiments.

8. Relevance to Human Health

While the focus is on mouse prolactin, the insights gained from these studies can inform our understanding of human prolactin biology and its role in health and disease. This is particularly relevant for conditions such as lactation disorders, metabolic diseases, and neuroendocrine disorders.

Conclusion

Recombinant Mouse Prolactin is a robust and reliable reagent for a wide range of research applications. Its high biological activity, purity, and versatility make it an essential tool for advancing our understanding of prolactin's role in various physiological and pathological processes. Whether you are studying lactation, metabolism, neuroendocrinology, or cell biology, recombinant mouse prolactin can provide the necessary support for your research goals.

Yes, recombinant Mouse Prolactin (PRL) protein can be used as a standard for quantification or calibration in ELISA assays, provided it is properly validated and formulated for this purpose.

Essential context and supporting details:

  • Formulation for ELISA: Recombinant Mouse Prolactin is commonly supplied either with a carrier protein (such as BSA) or carrier-free. For use as an ELISA standard, the formulation with BSA is generally recommended because it enhances stability and allows for accurate dilution and handling. Carrier-free formulations are suitable if BSA would interfere with your assay.

  • Validation: It is critical to ensure that the recombinant PRL standard is immunologically equivalent to the native protein detected by your ELISA antibodies. Most commercial recombinant PRL proteins are validated for use as ELISA standards, but you should confirm this in the product documentation or by running a pilot standard curve.

  • Preparation and Dilution: When preparing standards, follow the recommended reconstitution and dilution protocols. Large dilution steps (from μg/mL to pg/mL) can introduce error, so meticulous pipetting and mixing are essential. Assign the concentration of your standard based on its measured value in the ELISA, not just the mass on the vial, due to possible lot-to-lot variation in immunoreactivity.

  • Standard Curve: For quantitative ELISA, a standard curve must be generated using known concentrations of the recombinant PRL standard. This curve is then used to interpolate the concentrations of unknown samples. The accuracy of quantification depends on the quality and consistency of the standard curve.

  • Best Practices:

    • Use the same buffer and matrix for standard preparation as for your samples to minimize matrix effects.
    • Avoid repeated freeze-thaw cycles of the standard to maintain protein integrity.
    • Validate recovery and linearity by spiking known amounts of recombinant PRL into sample matrices.

Additional relevant information:

  • Regulatory Note: Recombinant standards are for research use only and not for diagnostic or therapeutic procedures.
  • Reference Standards: For absolute quantification, some assays use international reference standards (e.g., WHO reference reagents), but recombinant PRL is suitable for routine calibration in most research ELISAs.

Summary Table: Use of Recombinant Mouse Prolactin as ELISA Standard

AspectRecommendation/Note
FormulationPrefer BSA-containing for ELISA; carrier-free if needed
ValidationConfirm immunoreactivity with assay antibodies
PreparationFollow reconstitution/dilution instructions
Standard CurveGenerate fresh for each assay
Recovery/LinearityValidate with spiked samples
Regulatory StatusFor research use only

In conclusion, recombinant Mouse Prolactin is widely used as a standard for ELISA quantification, but proper validation and handling are essential for accurate results.

Recombinant Mouse Prolactin (mPRL) has been validated for several applications in published research, primarily focusing on its biological activity and functional effects in both in vitro and in vivo settings. Key applications include:

  1. Bioassays and Functional Activity Testing

    • Recombinant Mouse Prolactin has been used in bioassays to assess its biological activity, including its ability to stimulate precursor cells in the adult mouse hippocampus and influence adipocyte differentiation in 3T3-L1 cells.
    • Studies have confirmed its activity in cell-based assays, such as evaluating mRNA expression of genes related to adipocyte differentiation (e.g., C/EBPβ, FAS, PPARγ) and assessing cell viability and cytotoxicity.
  2. In Vivo Assays

    • Recombinant Mouse Prolactin has been applied in in vivo studies to investigate its effects on lactation, galactopoiesis, and metabolic adaptations.
    • Engineered variants of prolactin (e.g., Prolactin-XL) have been tested for their ability to restore lactation in mouse models and for their pharmacokinetic properties in both nulliparous and lactating mice.
  3. Purification and Structural/Functional Stability Studies

    • The protein has been validated for use in purification studies, where its structural and functional stability were assessed through methods such as SDS-PAGE, Western blot, and chromatography.
    • These studies highlight the protein's suitability for biochemical and biological research due to its high purity and retained bioactivity.
  4. Research on Prolactin Receptor Signaling

    • Recombinant Mouse Prolactin is used to study prolactin receptor (PRLR) signaling pathways, including their roles in metabolic adaptations during pregnancy and in hormone-dependent cancers.

These applications demonstrate that Recombinant Mouse Prolactin is a versatile tool for studying prolactin's physiological roles, receptor interactions, and potential therapeutic implications in both basic and translational research.

To reconstitute and prepare Recombinant Mouse Prolactin R protein for cell culture experiments, follow these steps:

  • Centrifuge the vial briefly to ensure all lyophilized protein is at the bottom before opening.
  • Reconstitute the protein in sterile deionized water or sterile PBS. The recommended concentration is typically 0.1–1.0 mg/mL.
  • If specified by the product datasheet, you may add a carrier protein such as 0.1% bovine serum albumin (BSA) to stabilize the solution, especially for low concentrations or repeated freeze-thaw cycles.
  • Gently mix by inversion or slow pipetting. Avoid vigorous shaking to prevent foaming and protein denaturation.
  • Allow the protein to dissolve at room temperature for 15–30 minutes with gentle agitation.
  • For enhanced stability, especially for long-term storage, you may add glycerol (5–50% final concentration) to the reconstituted solution.
  • Aliquot the solution to avoid repeated freeze-thaw cycles and store at –20°C to –80°C.

Preparation for cell culture:

  • Dilute the reconstituted stock into your cell culture medium to the desired working concentration, typically in the range of ng/mL to μg/mL, depending on your experimental design and cell type.
  • Ensure the final solution is sterile and compatible with your cell culture system.

Best practices:

  • Always consult the specific product datasheet for any unique requirements regarding buffer composition, pH, or additives.
  • Use sterile technique throughout to prevent contamination.
  • If using for functional assays, confirm protein activity with a pilot experiment.

Summary Table: Recombinant Mouse Prolactin R Protein Reconstitution

StepDetails
Centrifuge vialBriefly spin to collect powder at bottom
ReconstitutionSterile deionized water or PBS, 0.1–1.0 mg/mL
Carrier proteinOptional: 0.1% BSA for stability
MixingGentle inversion or pipetting, avoid foaming
Dissolution time15–30 min at room temperature
Glycerol additionOptional: 5–50% for long-term storage
AliquotingStore in small volumes, avoid freeze-thaw cycles
Storage–20°C to –80°C
Cell culture useDilute to working concentration in sterile medium

This protocol ensures optimal solubility, stability, and bioactivity for cell culture applications.

References & Citations

1. Lindeman, GJ. et al. (2003) J. Biol. Chem. 278:32929
2. Makrigiannakis, A. et al. (2005) Reproductive Biomed. 10:339
3. Talamantes, F. et al. (2001) J. of Endocrinol. 171:85
4. Clevenger, CV. et al. (2001) Lupus. 10:706
5. Mastro, M. et al. (2003) J. Appl. Physiol. 94:518
Elisa Sandwich Protocol

Certificate of Analysis

IMPORTANT Use lot specific datasheet for all technical information pertaining to this recombinant protein.
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Disclaimer AlertProducts are for research use only. Not for use in diagnostic or therapeutic procedures.