Recombinant Callithrix jacchus Serpin B10 (SERPINB10)
Description
Origin and Expression System
The recombinant SERPINB10 protein from Callithrix jacchus is produced via yeast-based expression systems. This method ensures high yield and proper post-translational modifications, with a His-tag added for purification purposes. The protein spans amino acids 1–397, corresponding to the full-length native sequence .
Protein Characteristics
| Parameter | Specification |
|---|---|
| Host Organism | Yeast |
| Tag | His-tag |
| Purity | >90% (ELISA-validated) |
| Molecular Weight | ~45–50 kDa (predicted) |
| Applications | ELISA, Western Blot, Functional Assays |
Biological Function
SERPINB10 belongs to the serpin family of protease inhibitors, which regulate enzymes involved in inflammation, apoptosis, and immune responses. In primates, including Callithrix jacchus, SERPINB10 is implicated in:
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Protease Regulation: Inhibits serine proteases, balancing tissue remodeling and immune activation .
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Immune Pathways: Associates with neutrophil and monocyte activity, as shown in genome-wide association studies (GWAS) linking SERPINB10 variants to cutaneous leishmaniasis susceptibility .
Disease Models
SERPINB10 is used in studies of leishmaniasis, where its expression correlates with lesion severity and cytokine profiles (e.g., IFN-γ/TNF balance) .
Functional Assays
The recombinant protein is tested in:
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ELISA: Validates antibody specificity for SERPINB10 epitopes.
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Western Blot: Detects protein expression in primate tissues or cell lysates.
Comparative Analysis with Other Species
| Species | Host | Purity | Tag |
|---|---|---|---|
| Callithrix jacchus | Yeast | >90% | His |
| Mouse | Insect Cells | >94% | C-His |
| Human | HEK293T | >85% | C-Myc/DDK |
Research Implications
SERPINB10’s role in protease regulation positions it as a therapeutic target for inflammatory disorders. Its expression in primate models (e.g., Callithrix jacchus) facilitates translation of findings to human diseases .
Limitations
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Functional activity testing is incomplete for the yeast-expressed variant .
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Species-specific differences in protease binding require further validation .
This recombinant protein represents a valuable tool for elucidating SERPINB10’s mechanisms in primate immunobiology, with applications spanning infectious disease research and protease biology.
Product Specs
Target Background
KEGG: cjc:100407965
STRING: 9483.ENSCJAP00000012445
