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The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. Additionally we are shipping ZP2 Antibodies (23) and ZP2 Proteins (7) and many more products for this protein.
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The central peptide of ZP2 (190-505) is immunogenic and contains zona pellucida-specific epitopes.
ZP2(51-149) sperm-binding domain is necessary for mouse gamete recognition and penetration through the zona pellucida.
Studies indicate that eggs from mZP2-/- and mZP3-/- females lack a zona pellucida (ZP), and the mice are completely infertile due to a severely reduced number of ovulated eggs in their oviducts.
Sperm arylsulfatase A (show ARSA ELISA Kits) binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner.
Recombinant ovastacin (show ASTL ELISA Kits) cleaved ZP2 in native zonae pellucidae, documenting that ZP2 was a direct substrate of this metalloendoprotease.
Cytoplasmic tails are necessary to prevent intracellular oligomerization while ensuring incorporation of processed ZP2 and ZP3 (show ZP3 ELISA Kits) into the zona pellucida.
data indicate that sperm-egg recognition depends on the cleavage status of ZP2 and that binding at the surface of the zona is not sufficient to induce sperm acrosome exocytosis
stoichiometric disposition of ZP1 (show ZP1 ELISA Kits), ZP2, and ZP3 (show ZP3 ELISA Kits) in the ovarian zona matrix revealed by double and triple immunolocalization studies
Results indicate that ZP2 and ZP3 (show ZP3 ELISA Kits) traffic independently through the oocyte prior to assembly into the zona pellucida.
Mutations in ZP2 and ZP3 (show ZP3 ELISA Kits) have dosage effects which can cause female infertility in humans.
ZP2(51-149) sperm-binding domain is necessary for human gamete recognition and penetration through the zona pellucida.
Studies indicate that eggs from mice lacking an ortholog of ZP2 do not contain a zona pellucida (ZP), and the mice are completely infertile due to a severely reduced number of ovulated eggs in their oviducts.
observed sequence variations in exons of ZP2 gene in women with infertility of unknown origin who exhibit abnormal zona pellucida; sperm-ovum interactions appear relatively normal in these patients [CASE REPORTS]
Of all zona pellucida (ZP) proteins, recombinant human ZPA demonstrates the highest binding activity toward acrosin (show ACR ELISA Kits)
Polymorphism of Zp2 and the Zp3 (show ZP3 ELISA Kits) did not show any contribution to reproductive isolation between the bovine species.
The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed primarily of three or four glycoproteins with various functions during fertilization and preimplantation development. The protein encoded by this gene is a structural component of the zona pellucida and functions in secondary binding and penetration of acrosome-reacted spermatozoa. The nascent protein contains a N-terminal signal peptide sequence, a conserved ZP domain, a consensus furin cleavage site, and a C-terminal transmembrane domain. It is hypothesized that furin cleavage results in release of the mature protein from the plasma membrane for subsequent incorporation into the zona pellucida matrix. However, the requirement for furin cleavage in this process remains controversial based on mouse studies.
zona pellucida glycoprotein ZP2
, zona pellucida protein A
, zona pellucida sperm-binding protein 2
, zona pellucida A protein
, zona pellucida 2 glycoprotein
, 75-kDa rabbit zona pellucida protein