The zona pellucida is an extracellular matrix thatnsurrounds the oocyte and early embryo. It is composed primarily ofnthree or four glycoproteins with various functions duringnfertilization and preimplantation development. The protein encodednby this gene is a structural component of the zona pellucida andnfunctions in primary binding and induction of the sperm acrosomenreaction. The nascent protein contains a N-terminal signal peptidensequence, a conserved ZP domain, a C-terminal consensus furinncleavage site, and a transmembrane domain. It is hypothesized thatnfurin cleavage results in release of the mature protein from thenplasma membrane for subsequent incorporation into the zonanpellucida matrix. However, the requirement for furin cleavage innthis process remains controversial based on mouse studies. Anvariation in the last exon of this gene has previously served asnthe basis for an additional ZP3 locus; however, sequence andnliterature review reveals that there is only one full-length ZP3nlocus in the human genome. Another locus encoding a bipartitentranscript designated POMZP3 contains a duplication of the lastnfour exons of ZP3, including the above described variation, andnmaps closely to this gene.
应用类型
WB
免疫原
This ZP3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 353-380 amino acids from the C-terminal region of human ZP3.
