ZP2 antibody can be used for detection of ZP2 by ELISA at 1:62500. ZP2 antibody can be used for detection of ZP2 by western blot at 2.5 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 - 100,000.
限制
仅限研究用
状态
Lyophilized
溶解方式
Add 100 ?L of distilled water. Final antibody concentration is 1 mg/mL.
浓度
1 mg/mL
缓冲液
Antibody is lyophilized in PBS buffer with 2 % sucrose.
注意事项
As with any antibody avoid repeat freeze-thaw cycles.
储存条件
4 °C/-20 °C
储存方法
For short periods of storage (days) store at 4 °C. For longer periods of storage, store ZP2 antibody at -20 °C.
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. ZP2 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.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.