Recombinant Human TMEM106B Fc Chimera Protein, CF Summary
- R&D Systems HEK293-derived Recombinant Human TMEM106B Fc Chimera Protein (11644-TM)
- Quality control testing to verify active proteins with lot specific assays by in-house scientists
- All R&D Systems proteins are covered with a 100% guarantee
Product Specifications
| MD | Human IgG1 (Pro100-Lys330) | IEGR | Human TREM106B (Pro118-Gln274) Accession # NP_001127704.1 |
| N-terminus | C-terminus | ||
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
11644-TM
| Formulation | Supplied as a 0.2 μm filtered solution in PBS with Trehalose. |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Recombinant Human TMEM106B Fc Chimera Protein (Catalog # 11644-TM) binds Recombinant SARS-CoV-2 Spike RBD His-tag (HEK293 Expressed) (10500-CV) with ED50 < 2.00 μg/mL
Reconstitution Calculator
Background: TMEM106B
SARS-CoV-2 is associated with broad tissue tropism, a characteristic often determined by the availability of entry receptors on host cells. TMEM106B, a lysosomal transmembrane protein, can serve as an alternative receptor for SARS-CoV-2 entry into angiotensin-converting enzyme 2 (ACE2)-negative cells. Spike substitution E484D increased TMEM106B binding, thereby enhancing TMEM106B-mediated entry (1). ACE2-independent entry was dependent on endogenous TMEM106B, which binds to the receptor binding domain (RBD). Binding is augmented by mutation E484D (3). TMEM106B-specific monoclonal antibodies blocked SARS-CoV-2 infection, demonstrating a role of TMEM106B in viral entry. Using X-ray crystallography, cryogenic electron microscopy (cryo-EM), and hydrogen-deuterium exchange mass spectrometry (HDX-MS), shows that the luminal domain (LD) of TMEM106B engages the receptor-binding motif of SARS-CoV-2 spike (1). The large loop (RBD@471-491) could anchor TMEM106B, which was then firmly locked by another loop (RBD@444-451) (2). TMEM106B also promotes spike-mediated syncytium formation, suggesting a role of TMEM106B in viral fusion. Findings have identified an ACE2-independent SARS-CoV-2 infection mechanism that involves cooperative interactions with the receptors heparan sulfate and TMEM106B (1).
FAQs
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