Recombinant Proteins

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MRPL1 Human

Mitochondrial Ribosomal Protein L1 Human Recombinant

MRPL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (51-325) and having a molecular mass of 33.8kDa. MRPL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13352
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

MRPL13 Human

Mitochondrial Ribosomal Protein L13 Human Recombinant

MRPL13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-178 a.a.) and having a molecular mass of 23.1kDa. MRPL13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13417
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

MRPL2 Human

Mitochondrial Ribosomal Protein L2 Human Recombinant

MRPL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (84-202 a.a) and having a molecular mass of 15.5kDa.
MRPL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13479
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

MRPL28 Human

Mitochondrial Ribosomal Protein L28 Human Recombinant

MRPL28 Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (56-256) and having a molecular mass of 25.8 kDa. MRPL28 is fused to 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13545
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

MRPL48 Human

Mitochondrial Ribosomal Protein L48 Human Recombinant

MRPL48 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (29-212 a.a) and having a molecular mass of 23.1kDa.
MRPL48 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13634
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

MRPS23 Human

Mitochondrial Ribosomal Protein S23 Human Recombinant

MRPS23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190 a.a) and having a molecular mass of 24.2kDa.
MRPS23 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13691
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

MRPS25 Human

Mitochondrial Ribosomal Protein S25 Human Recombinant

MRPS25 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (1-173) and having a molecular mass of 22.5kDa.
MRPS25 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13768
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

MRPS28 Human

Mitochondrial Ribosomal Protein S28 Human Recombinant

MRPS28 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (72-187a.a) and having a molecular mass of 15.5kDa. MRPS28 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13825
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.
Definition and Classification

Mitochondrial ribosomal proteins (MRPs) are essential components of the mitochondrial ribosome, which is responsible for protein synthesis within the mitochondria. Unlike cytoplasmic ribosomes, mitochondrial ribosomes are specialized for the translation of mitochondrial DNA-encoded proteins. MRPs are classified into two main subunits: the small subunit (28S) and the large subunit (39S). Each subunit comprises a unique set of proteins and ribosomal RNA (rRNA) molecules.

Biological Properties

Key Biological Properties: MRPs are characterized by their unique amino acid sequences and structural properties that enable them to function within the mitochondrial environment. They are highly conserved across species, reflecting their critical role in cellular metabolism.

Expression Patterns: The expression of MRPs is tightly regulated and varies across different tissues. High expression levels are typically observed in tissues with high metabolic activity, such as the heart, brain, and skeletal muscles.

Tissue Distribution: MRPs are ubiquitously expressed in all tissues, but their abundance is particularly high in tissues that rely heavily on oxidative phosphorylation for energy production.

Biological Functions

Primary Biological Functions: The primary function of MRPs is to facilitate the translation of mitochondrial mRNA into functional proteins. These proteins are integral to the mitochondrial respiratory chain and ATP production.

Role in Immune Responses: Emerging evidence suggests that MRPs may play a role in modulating immune responses. They can influence the production of reactive oxygen species (ROS) and the activation of signaling pathways involved in inflammation.

Pathogen Recognition: MRPs may also be involved in the recognition of pathogenic infections. Certain MRPs have been shown to interact with viral proteins, potentially influencing the host’s antiviral response.

Modes of Action

Mechanisms with Other Molecules and Cells: MRPs interact with various mitochondrial and cytoplasmic proteins to ensure proper mitochondrial function. These interactions are crucial for the assembly and stability of the mitochondrial ribosome.

Binding Partners: MRPs bind to mitochondrial rRNA and other ribosomal proteins to form functional ribosomal subunits. They also interact with mitochondrial translation factors and tRNAs during protein synthesis.

Downstream Signaling Cascades: MRPs can influence downstream signaling pathways by modulating mitochondrial function. For example, changes in mitochondrial protein synthesis can affect cellular energy status and activate AMP-activated protein kinase (AMPK) signaling.

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression of MRPs is regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms. Transcription factors such as nuclear respiratory factors (NRFs) and peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α) play key roles in regulating MRP gene expression.

Transcriptional Regulation: MRP genes are transcribed in the nucleus and then imported into the mitochondria. Their transcription is coordinated with the expression of other mitochondrial genes to ensure efficient mitochondrial biogenesis.

Post-Translational Modifications: MRPs undergo various post-translational modifications, such as phosphorylation and acetylation, which can influence their stability, localization, and activity.

Applications

Biomedical Research: MRPs are valuable tools in biomedical research for studying mitochondrial function and dysfunction. They are used to investigate the molecular mechanisms underlying mitochondrial diseases and aging.

Diagnostic Tools: Alterations in MRP expression or function can serve as biomarkers for mitochondrial disorders and other diseases. For example, mutations in certain MRP genes are associated with mitochondrial myopathies and neurodegenerative diseases.

Therapeutic Strategies: Targeting MRPs and their regulatory pathways holds potential for developing novel therapeutic strategies. Modulating MRP activity could help restore mitochondrial function in diseases characterized by mitochondrial dysfunction.

Role in the Life Cycle

Role Throughout the Life Cycle: MRPs play a critical role throughout the life cycle, from development to aging. During development, they are essential for the rapid proliferation and differentiation of cells. In aging, changes in MRP function can contribute to the decline in mitochondrial function and the onset of age-related diseases.

Development: During embryogenesis, MRPs are crucial for the proper development of tissues and organs that require high energy levels.

Aging and Disease: As organisms age, the efficiency of mitochondrial protein synthesis declines, leading to reduced mitochondrial function. This decline is associated with various age-related diseases, including neurodegenerative disorders and metabolic syndromes.

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