RELM g Mouse

RELM-Gamma Mouse Recombinant
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Description

Molecular Structure and Production

RELM-γ is a non-glycosylated, homodimeric protein produced in E. coli for research purposes. Key structural features include:

PropertyDescriptionSource
Molecular Weight18.9 kDa (dimer; 89 amino acids per monomer)
His-Tagged Variant11 kDa (86 amino acids + 16 His-tag residues)
Amino Acid SequenceMEGTLESIVEKKVKELLANRDDCPSTVTKTFSCTSITASGRLASCPSGMTVTGCACGYGCGSWDIRDGNTCHCQCSTMDWATARCCQLA
FormulationLyophilized from sterile-filtered solutions (0.1% TFA or acetate buffer pH 4)

Recombinant RELM-γ is purified via chromatography and is available in various concentrations (e.g., 0.1–0.5 mg/mL) for experimental use .

Tissue Expression and Secretion

RELM-γ exhibits restricted tissue-specific expression, primarily in hematopoietic and epithelial compartments:

TissueExpression LevelCell TypesSource
Bone MarrowHighHematopoietic progenitors
SpleenHighImmune cells (granulocytes, macrophages)
LungModerateEpithelial cells, granulocytes
IntestineLowEpithelial cells
Peripheral BloodModerateGranulocytes

RELM-γ is secreted and functions as a cytokine-like molecule, influencing cellular differentiation and immune responses .

Functional Roles in Biological Processes

RELM-γ participates in diverse physiological and pathological processes:

Promyelocytic Differentiation

Transfection of promyelocytic HL60 cells with RELM-γ increases proliferation rates and alters retinoic acid-induced granulocytic differentiation, suggesting a regulatory role in myeloid lineage commitment .

Insulin Sensitivity and Metabolism

In rodents, RELM-γ modulates nutrient-associated insulin sensitivity in the intestinal tract, though its exact mechanism remains under investigation .

Immune Response Regulation

During Th2-mediated immune responses (e.g., nematode infections), RELM-γ expression is upregulated in the intestine, alongside RELM-α and RELM-β, to combat parasitic infections .

Regulation and Transcriptional Control

RELM-γ expression is influenced by transcriptional regulators and immune pathways:

RegulatorMechanismSource
Cdx2No direct regulation; Cdx2 selectively induces RELM-β in gastric epithelium
Th2 CytokinesInduces RELM-γ in intestinal goblet cells during nematode infections
Retinoic AcidAlters granulocytic differentiation in RELM-γ-expressing HL60 cells

Unlike RELM-β, which is Cdx2-dependent, RELM-γ expression is linked to adaptive immune responses rather than developmental transcription factors .

Applications in Research and Experimental Use

Recombinant RELM-γ is utilized in:

  • Cellular Studies: Investigating granulocytic differentiation and proliferation .

  • Immunological Research: Studying Th2-mediated responses to parasitic infections .

  • Biochemical Assays: ELISA, Western blotting, and protein-protein interaction studies .

Physicochemical Properties and Handling

PropertyRecommendationSource
SolubilityReconstitute in sterile water (0.1 mg/mL) or acetate buffer (pH 4)
StorageLyophilized at -20°C; reconstituted aliquots at -80°C (with BSA/HSA)
Endotoxin Level<0.1 EU/µg (ensure sterile filtration before cell culture use)

Product Specs

Introduction
RELM-gamma, a member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats, shows repressed mRNA expression in nasal respiratory epithelium of rats exposed to cigarette smoke. Its expression is highest in hematopoietic tissues, suggesting a cytokine-like role. RELM-gamma mRNA is found in bone marrow, spleen, lung, and peripheral blood granulocytes. Promyelocytic HL60 cells overexpressing RELM-gamma exhibit increased proliferation and altered response to retinoic acid-induced differentiation, indicating a potential role in promyelocytic differentiation.
Description
Recombinant Mouse RELM g, produced in E. coli, is a non-glycosylated homodimer with two 89 amino acid chains, resulting in a molecular weight of 18.9 kDa. The protein is purified using proprietary chromatographic methods.
Physical Appearance
Sterile white lyophilized powder.
Formulation
Lyophilized from a sterile solution containing 0.1% trifluoroacetic acid (TFA).
Solubility
Reconstitute the lyophilized RELM g in sterile 18 megaohm-cm H2O to a concentration of 100 µg/ml. This solution can be further diluted with aqueous solutions.
Stability
Lyophilized RELM g is stable at room temperature for 3 weeks. For long-term storage, store desiccated below -18°C. Reconstituted RELM g should be stored at 4°C for 2-7 days or below -18°C for future use. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid freeze-thaw cycles.
Purity
Greater than 95% purity as determined by SDS-PAGE.
Synonyms

Resistin-like gamma, RELMgamma,RELM-γ, RELM-g. 

Source

Escherichia Coli.

Amino Acid Sequence

MEGTLESIVE KKVKELLANR DDCPSTVTKT FSCTSITASG RLASCPSGMT VTGCACGYGC GSWDIRDGNT CHCQCSTMDW ATARCCQLA.

Q&A

Experimental Design for RELM-γ Studies

Q: How should I design experiments to study the role of RELM-γ in mice, considering factors like genetic variability and environmental influences?

A: When designing experiments involving RELM-γ in mice, it's crucial to consider genetic and environmental factors that can affect outcomes. Ensure that you use genetically identical strains to minimize variability. Perform pilot studies to understand how your specific assay affects the phenotype and to determine the appropriate sample size for statistical power. Consider the 3Rs (Replacement, Refinement, Reduction) to ensure ethical and reproducible research .

Data Analysis and Contradiction Resolution

Q: How do I analyze data from RELM-γ experiments to resolve potential contradictions with existing literature?

A: Analyzing data from RELM-γ experiments involves using statistical models that account for variability and potential confounding factors. If contradictions arise with existing literature, consider re-evaluating experimental conditions, sample sizes, and statistical methods. Use tools like R for robust data analysis and interpretation . Additionally, reviewing the literature on similar studies can help identify gaps or methodological differences that might explain discrepancies.

Advanced Research Questions: Mechanism of Action

Q: What are the advanced research questions regarding the mechanism of action of RELM-γ in mice, and how can they be addressed?

A: Advanced research questions might include how RELM-γ influences promyelocytic differentiation and insulin sensitivity in the intestine. To address these, use techniques like in vitro assays to study differentiation and metabolic assays to assess insulin sensitivity. Consider using knockout or overexpression models to elucidate the role of RELM-γ in these processes .

Methodological Considerations for RELM-γ Studies

Q: What methodological considerations are crucial when studying RELM-γ in mice, especially regarding its secretion and function?

Interpretation of Results in Context of Existing Literature

Q: How should I interpret my results in the context of existing literature on RELM-γ, especially if they seem to contradict previous findings?

A: When interpreting results that contradict existing literature, consider factors like differences in experimental design, mouse strains used, or specific conditions under which RELM-γ was studied. Reviewing the literature systematically can help identify methodological differences or gaps in current knowledge that might explain discrepancies. Consider publishing your findings to contribute to the ongoing discussion and refinement of understanding RELM-γ's role .

Example Data Table: RELM-γ Functions

FunctionTissue InvolvedMethod of Study
Promyelocytic DifferentiationBone Marrow, Peripheral BloodIn Vitro Assays
Insulin Sensitivity RegulationIntestineMetabolic Assays
SecretionPeripheral Blood Granulocytes, Intestine, LungRecombinant Protein Studies

This table highlights the diverse roles of RELM-γ and the methods used to study them, demonstrating the complexity of its biological functions.

Product Science Overview

Structure and Characteristics

Recombinant mouse RELM-γ is a non-glycosylated protein dimer, containing 89 amino acids and having a molecular mass of approximately 9.4 kDa . It is produced in E. coli and is available as a sterile filtered white lyophilized (freeze-dried) powder . The protein is stable when lyophilized at -20°C and should be reconstituted with sterile water at 0.1 mg/mL for further use .

Function and Role

RELM-γ plays a significant role in promoting and regulating promyelocytic differentiation, as well as regulating nutrient-associated insulin sensitivity in the intestinal tract . It is primarily expressed in hematopoietic tissues, suggesting a cytokine-like role . Studies have shown that RELM-γ mRNA is detectable in bone marrow, spleen, lung, and peripheral blood granulocytes .

Research and Applications

RELM-γ is used in various research applications, including studies on promyelocytic differentiation and insulin sensitivity. It is also used to investigate its role in inflammatory responses and its potential as a therapeutic target . Recombinant RELM-γ is available for research purposes and is not intended for human, animal, or diagnostic applications .

Handling and Storage

The lyophilized product is very stable at -20°C. Once reconstituted, it should be aliquoted and frozen at -20°C for long-term storage. It is recommended to add a carrier protein (0.1% HSA or BSA) for long-term storage . The reconstituted protein can be stored at 4°C for a limited period and remains stable for up to two weeks .

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