Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | Q9EQF4 |
express system | HEK293 |
product tag | C-His |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Izumo1 is the only essential sperm-egg fusion protein currently known on mammalian sperm, and its egg receptor (Juno; formerly Folr4) was recently discovered. Male knockout mice for Izumo1 and female knockout mice for Juno are both healthy but sterile. Here, both sperm-egg binding proteins are shown to be evolving under positive selection. Juno's presence in mammals alone, suggesting a recent mammalian-specific duplication and neofunctionalization of the ancestral folate receptor. |
molecular weight | The protein has a predicted MW of 24.7 kDa. Due to glycosylation, the protein migrates to 35-40 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Mouse FOLR4/Juno Protein 3562
$300.00 – $1,000.00
Summary
- Expression: HEK293
- Pure: Yes (HPLC)
- Amino Acid Range: Gly20-Gly222
Mouse FOLR4/Juno Protein 3562
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Izumo1 is the only essential sperm-egg fusion protein currently known on mammalian sperm, and its egg receptor (Juno; formerly Folr4) was recently discovered. Male knockout mice for Izumo1 and female knockout mice for Juno are both healthy but sterile. Here, both sperm-egg binding proteins are shown to be evolving under positive selection. Juno's presence in mammals alone, suggesting a recent mammalian-specific duplication and neofunctionalization of the ancestral folate receptor. |
Protein names Sperm-egg fusion protein Juno (Folate receptor 4) (Folate receptor delta) (FR-delta) (Folate-binding protein 3) (IZUMO1 receptor protein JUNO) |
Gene names Izumo1r,Izumo1r Folbp3 Folr4 Juno |
Protein family Folate receptor family |
Mass 10090Da |
Function Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for species-specific gamete recognition and fertilization (PubMed:24739963, PubMed:26859261, PubMed:27309808, PubMed:27416963). The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion (PubMed:24739963, PubMed:26859261, PubMed:27309808). The ligand-receptor interaction probably does not act as a membrane 'fusogen' (PubMed:24739963, PubMed:26859261, PubMed:27309808). Does not bind folate (PubMed:24739963). |
Subellular location Cell membrane ; Lipid-anchor, GPI-anchor. Note=GPI-anchored at the oolemma. |
Tissues Widely expressed with higher expression in thymus, spleen and lung (PubMed:11111049). Present at the cell surface of unfertilized oocytes, while it is barely detectable 30 to 40 minutes after fertilization (at protein level) (PubMed:24739963). |
Structure Monomer (PubMed:26859261). Interacts with IZUMO1; the interaction is direct (PubMed:24739963, PubMed:25209248, PubMed:26859261, PubMed:27309808, PubMed:27416963, PubMed:32484434). IZUMO1 and IZUMO1R/JUNO form a complex with 1:1 stoichiometry (By similarity). |
Post-translational modification The protein is rapidly cleaved following fertilization, being only weakly detectable in zona-intact fertilized eggs at telophase II and undetectable at the pronuclear stage (PubMed:24739963). Sheding is probably required to block to polyspermy and ensuring egg fusion with a single sperm (PubMed:24739963). |
Target Relevance information above includes information from UniProt accession: Q9EQF4 |
The UniProt Consortium |
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The purity of Mouse FOLR4 is greater than 95% as determined by SEC-HPLC. |
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Mouse FOLR4 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. |
Publications
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