Recombinant Proteins

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SSR1 Human

Signal Sequence Receptor, Alpha Human Recombinant

Recombinant human SSR1 protein was produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 209 amino acids (amino acids 22-207) with a molecular mass of 23.1 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26789
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

SSR2 Human

Signal Sequence Receptor, Beta Human Recombinant

Recombinant human SSR2, expressed in E. coli, is available as a non-glycosylated polypeptide chain. This single-chain protein consists of 155 amino acids (18-149a.a), resulting in a molecular weight of 16.8 kDa. A 23 amino acid His-tag is fused to the N-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26889
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

SSR4 Human

Signal Sequence Receptor, Delta Human Recombinant

Recombinant human SSR4, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 144 amino acids (specifically, residues 24-144). With a molecular weight of 16.1 kDa, this protein features a 23-amino acid His-tag fused to its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26969
Source
Escherichia Coli.
Appearance
Clear, sterile, and filtered solution.
Definition and Classification

The Signal Sequence Receptor (SSR) is a glycoprotein located in the membrane of the endoplasmic reticulum (ER). It plays a crucial role in the translocation of nascent polypeptides across the ER membrane. SSR is classified as an integral membrane protein with a single membrane-spanning segment .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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

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 .

Applications

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 .

Role in the Life Cycle

Role Throughout the Life Cycle: SSR plays a vital role throughout the life cycle of a cell. From the development stage, where it ensures proper protein synthesis and folding, to aging and disease, where its dysfunction can lead to various pathologies .

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