Recombinant Proteins
Product List
SSR4 Human
Signal Sequence Receptor, Delta Human Recombinant
SSR4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SSR1 Human
Signal Sequence Receptor, Alpha Human Recombinant
SSR2 Human
Signal Sequence Receptor, Beta Human Recombinant
Introduction
Key Biological Properties: SSR is synthesized with a cleavable amino-terminal signal sequence and contains a classical membrane-spanning segment. It shows a remarkable charge distribution with a highly negatively charged amino terminus and a positively charged cytoplasmic carboxyl terminus .
Expression Patterns and Tissue Distribution: SSR is ubiquitously expressed in cells that have a high demand for protein synthesis and secretion. It is predominantly found in the rough ER, where it interacts with the signal recognition particle (SRP) and nascent polypeptides .
Primary Biological Functions: The primary function of SSR is to facilitate the translocation of nascent polypeptides into the ER lumen. This process is essential for the proper folding and modification of proteins destined for secretion or for use in the cell membrane .
Role in Immune Responses and Pathogen Recognition: While SSR itself is not directly involved in immune responses, the proper functioning of SSR is critical for the synthesis of proteins that play roles in immune responses, such as antibodies and cytokines .
Mechanisms with Other Molecules and Cells: SSR interacts with the SRP and its receptor in the ER membrane. Upon binding to the signal sequence of a nascent polypeptide, SSR facilitates the transfer of the polypeptide into the ER lumen .
Binding Partners and Downstream Signaling Cascades: SSR primarily interacts with the SRP and the Sec61 translocon complex. This interaction is crucial for the translocation of polypeptides across the ER membrane .
Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of SSR are regulated at multiple levels, including transcriptional regulation and post-translational modifications. Phosphorylation of SSR in its cytoplasmic tail has been shown to regulate its function .
Transcriptional Regulation and Post-Translational Modifications: SSR can be phosphorylated in its cytoplasmic tail, which suggests a regulation of its function. This phosphorylation can occur both in intact cells and in cell-free systems .
Biomedical Research: SSR is a critical component in the study of protein translocation and folding. Understanding its function can provide insights into various diseases related to protein misfolding and secretion .
Diagnostic Tools and Therapeutic Strategies: SSR can be targeted in therapeutic strategies aimed at enhancing or inhibiting protein translocation. This can be particularly useful in diseases where protein misfolding plays a role .
