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Product List
SRP14 Human
Signal Recognition Particle 14kDa Human Recombinant
SRP14 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-136 a.a.) and having a molecular mass of 17.1kDa. The SRP14 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs 
Cat. No.
BT26543
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
SRP19 Human
Signal Recognition Particle 19kDa Human Recombinant
SRP19 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (1-144 a.a.) and having a molecular mass of 18.5kDa. The SRP19 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26645
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
SRP54 Human
Signal Recognition Particle 54kDa Human Recombinant
SRP54 is a full-length cDNA coding for the human SRP54 protein having a molecular mass of 62kDa (pH 8.9). SRP54 protein is fused to a hexa-histidine purification tag.
Shipped with Ice Packs
Introduction
Definition and Classification
The Signal Recognition Particle (SRP) is a ribonucleoprotein complex that plays a critical role in the targeting and translocation of nascent proteins to the endoplasmic reticulum (ER) in eukaryotic cells or the plasma membrane in prokaryotic cells. SRP is classified based on its components and function, with the eukaryotic SRP being composed of a 7S RNA molecule and six protein subunits (SRP54, SRP19, SRP68, SRP72, SRP9, and SRP14).
Biological Properties
- Key Biological Properties: SRP is essential for the co-translational targeting of proteins to the ER. It recognizes and binds to signal sequences of nascent polypeptides emerging from the ribosome.
- Expression Patterns: SRP is ubiquitously expressed in all cells, given its fundamental role in protein targeting.
- Tissue Distribution: SRP is found in all tissues, with higher activity in cells with extensive secretory functions, such as liver and pancreas cells.
Biological Functions
- Primary Biological Functions: The primary function of SRP is to recognize signal peptides of nascent proteins and direct them to the ER for proper folding and modification.
- Role in Immune Responses: SRP indirectly supports immune responses by ensuring the proper synthesis and processing of proteins, including those involved in immune functions.
- Pathogen Recognition: While SRP itself does not directly recognize pathogens, its role in protein targeting is crucial for the synthesis of proteins that participate in pathogen recognition and immune defense.
Modes of Action
- Mechanisms with Other Molecules and Cells: SRP interacts with the ribosome, signal peptides, and the SRP receptor (SR) on the ER membrane.
- Binding Partners: Key binding partners include the ribosome, nascent polypeptide chains, and the SRP receptor.
- Downstream Signaling Cascades: Upon binding to the SRP receptor, SRP facilitates the transfer of the ribosome-nascent chain complex to the translocon, initiating protein translocation into the ER.
Regulatory Mechanisms
- Expression and Activity Control: SRP expression is regulated at the transcriptional level by various transcription factors.
- Transcriptional Regulation: Specific transcription factors and regulatory elements in the SRP gene promoter region control its expression.
- Post-Translational Modifications: SRP components may undergo post-translational modifications, such as phosphorylation, to modulate their activity and interactions.
Applications
- Biomedical Research: SRP is studied to understand protein targeting and translocation mechanisms.
- Diagnostic Tools: SRP components can be used as biomarkers for certain diseases involving protein misfolding and trafficking.
- Therapeutic Strategies: Targeting SRP pathways may offer therapeutic potential for diseases related to protein misfolding and secretion.
Role in the Life Cycle
- Development: SRP is crucial during development for the proper synthesis and targeting of proteins necessary for cell growth and differentiation.
- Aging: Changes in SRP function or expression may contribute to age-related declines in protein homeostasis.
- Disease: Dysregulation of SRP function can lead to diseases such as neurodegenerative disorders, where protein misfolding and aggregation are prominent features.
