Anti-Quail Wing Bud Zone Of Polarizing Activity monoclonal antibody (DMAB9337)

Mouse anti-Quail Quail Wing Bud Zone Of Polarizing Activity monoclonal antibody for IF Datasheet

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Specifications


Host Species
Mouse
Antibody Isotype
IgG1
Clone
QCPN
Species Reactivity
Quail
Immunogen
Wing bud zone of polarizing activity from quail (wing bud ZPA).
Conjugate
Unconjugated

Target


Alternative Names
wing bud zone of polarizing activity; wing bud ZPA

Product Background


Gene summary
ZP2 (Zona Pellucida Glycoprotein 2) is a Protein Coding gene. Diseases associated with ZP2 include infertility and acheiropody. Among its related pathways are Reproduction and Ovarian Infertility Genes. GO annotations related to this gene include coreceptor activity and acrosin binding. An important paralog of this gene is ZP1. The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed of three glycoproteins with various functions during fertilization and preimplantation development. The glycosylated mature peptide is one of the structural components of the zona pellucida and functions in secondary binding and penetration of acrosome-reacted spermatozoa. Female mice lacking this gene do not form a stable zona matrix and are sterile. Alternative splicing results in multiple transcript variants.
Antigen Description
The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor. Zona pellucida sperm-binding protein 2 is a protein that in humans is encoded by the ZP2 gene. The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed primarily of three (mouse) or four (human) glycoproteins (ZP1-4) 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.

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