SSR1 is part of the heterotetrameric TRAP complex (TRAPα/SSR1, TRAPβ/SSR2, TRAPγ/SSR3, TRAPδ/SSR4), which facilitates:
Preproinsulin Translocation: TRAPα/SSR1 deficiency reduces insulin biosynthesis by impairing signal peptide recognition and ER membrane insertion.
ER Retention of Resident Proteins: Binds calcium to regulate ER homeostasis.
Cooperation with Sec61 Translocon: Assists in post-translational translocation of proteins with suboptimal signal peptides.
Production Methods
Expression Systems: Primarily E. coli and HEK293 cells, yielding 80–95% purity via affinity chromatography.
Storage: Lyophilized or in Tris/PBS buffers with glycerol at -20°C/-80°C.
Research Applications
Application
Use Case
Protein Interaction Studies
Identifies binding partners like Sec61 and ribosomes via co-immunoprecipitation.
Insulin Biosynthesis Research
CRISPR/Cas9 knockout models reveal impaired proinsulin processing in pancreatic β-cells.
Structural Analysis
Cryoelectron microscopy maps TRAPα/SSR1 interactions with ribosomes and translocons.
Diagnostic Assays
ELISA and Western blot validation using anti-SSR1 antibodies (e.g., Boster Bio A06993-1).
Key Research Findings
Deficiency Phenotypes:
Loss of TRAPα/SSR1 reduces proinsulin biosynthesis by 50–70% in β-cells, mimicking type 2 diabetes pathology.
Overexpression of TRAPα/SSR1 rescues translocation defects caused by TRAPβ/SSR2 or TRAPδ/SSR4 knockdown.
Mechanistic Insights:
The N-terminal cytosolic domain interacts with ribosomes to position signal peptides for Sec61 transfer.
Luminal domains stabilize nascent chains during translocation, preventing misfolding.
Future Directions
Current research focuses on:
Therapeutic Targeting: Modulating TRAPα/SSR1 to enhance insulin production in diabetes.
ERAD Mechanisms: Exploring SSR1’s role in degrading misfolded proteins.
Structural Dynamics: Resolving conformational changes during translocon-ribosome coupling.
Product Specs
Form
Lyophilized powder Note: We will prioritize shipping the format that
we have in stock. However, if you have a specific format requirement, please indicate it in your
order notes. We will prepare the product according to your request.
Lead Time
Delivery time
may vary depending on the purchasing method or location. Please consult your local distributors
for specific delivery times. Note: All our proteins are shipped with
standard blue ice packs. If you require dry ice shipping, please notify us in advance as
additional fees will apply.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Reconstitution
We recommend centrifuging the vial briefly before opening to ensure the contents are at the
bottom. Reconstitute the protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. We
suggest adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at
-20°C/-80°C. Our default final glycerol concentration is 50%, which can serve as a reference.
Shelf Life
Shelf life is influenced by various factors including storage conditions, buffer composition, storage temperature,
and the inherent stability of the protein.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized
form is 12 months at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquoting is essential for multiple uses. Avoid repeated freeze-thaw
cycles.
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during the production process. If
you have a specific tag type preference, please inform us, and we will prioritize the development of the specified tag.
Synonyms
SSR1; Translocon-associated protein subunit alpha; TRAP-alpha; Signal sequence receptor subunit alpha; SSR-alpha
TRAP proteins are components of a complex that binds calcium to the ER membrane, thereby regulating the retention of ER resident proteins. They may be involved in the recycling of the translocation apparatus after the completion of the translocation process or may function as a membrane-bound chaperone facilitating the folding of translocated proteins.