Izumo Sperm-Egg Fusion 1 (IZUMO1) ELISA Kits

Cow (Bovine) Izumo Sperm-Egg Fusion 1 (IZUMO1) interaction partners

1. These findings indicate that impaired fertilizing ability of bull cryopreserved spermatozoa with damaged acrosomes is related partially to the aberrant translocation of IZUMO1 which may be followed by the loss of intact IZUMO1.

Human Izumo Sperm-Egg Fusion 1 (IZUMO1) interaction partners

1. crystal structures of human IZUMO1, JUNO and the IZUMO1-JUNO complex, establishing the structural basis for the IZUMO1-JUNO-mediated sperm-oocyte interaction

2. crystal structures of human IZUMO1 and JUNO in unbound and bound conformations

3. these findings indicate that human sperm expresses Izumo protein, and the immunoinfertile female sera have circulating isoantibodies against this protein.

4. human sperm contain Izumo and addition of the antibody against human Izumo left the sperm unable to fuse with zona-free hamster eggs [Izumo]

5. We observed in our populations two combinations of four polymorphisms that appeared to be preferentially linked (CGG-CG and TAA-TT) without any significant difference between different genotype repartitions.

Mouse (Murine) Izumo Sperm-Egg Fusion 1 (IZUMO1) interaction partners

1. IZUMO1 interacts with JUNO during sperm binding.Trp62 of JUNO interacts with hydrophobic residues on the alpha-helical core region of IZUMO1.

2. These data support the hypothesis that dynamic movement of IZUMO1 is essential for gamete fusion during mouse fertilization.

3. The crystal structure of Izumo1 reveals a membrane distal region composed of a four-helix bundle connected to a carboxy-terminal immunoglobulin (Ig)-like domain through a beta-hairpin stabilized by disulfide bonds. Remarkably, different regions of Izumo1 display significant structural similarities to two proteins expressed by the invasive sporozoite stage of Plasmodium parasites: SPECT1, and TRAP.

4. Mice without the cytoplasmic tail of IZUMO1 showed normal fertility but decreased the amount of protein, indicating that whilst this region is important for the expression level of IZUMO1, it is dispensable for fertilisation in the mouse

5. Five IZUMO BCE were identified: DLVLDCL177-183, YSFYRV196-201 (named BCE-2), YLT217-219, SMVGPED221-227, and DAGNY228-232. Active immunization with the BCE-2 vaccine sharply decreased the fertility rate in female mice in a safe and reversible manner.

6. Robust IZUMO1-dependent adhesion of sperm with an oocyte accompanies the dimerization of IZUMO1.

7. Binding of sperm protein Izumo1 and its egg receptor Juno drives Cd9 accumulation in the intercellular contact area prior to fusion during mammalian fertilization.

8. identification of folate receptor 4 (Folr4) as the receptor for Izumo1 on the mouse egg.

9. 'IZUMO1 putative functional fragment (IZUMO1PFF) maintains binding ability on the egg surface of Cd9(-/-) eggs. IZUMO1PFF is composed of an N-terminal unfolded structure and a C-terminal ellipsoidal helix dimer.

10. Translocation of IZUMO1 during the fertilization process determined by time lapse imaging.

11. four phosphopeptide changes came from Izumo1, the sperm-egg fusion protein, in the cytoplasmic segment of the protein. 2D-PAGE confirmed that Izumo1 is post-translationally modified during epididymal transit.

12. co-localization of TMEM190 with IZUMO1 and complex formation with other sperm proteins.

13. identified an IZUMO1-interacting protein in sperm, which was identified as testis specific ACE homologue ACE3.

14. Results suggest that Izumo 1 might be involved in organizing or stabilizing a multiprotein complex essential for the function of the membrane fusion machinery.

15. identification of a mouse sperm fusion-related antigen and show that the antigen is a novel immunoglobulin superfamily protein

16. These data suggest that glycosylation is not essential for the function of IZUMO, but has a role in protecting it from fragmentation in cauda epididymis.

17. pCXN2-mIzumo plasmid possesses appreciable anti-fertility potential.

18. Data indicate that the Ig-like domain of Izumo plays an important role in the fertilization process, as verified by the dose-dependent reduction in fertilization rates in mouse IVF trials and mouse mating assay.