Analytical Data
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Gene name
ZPBP2
- Application
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Alternative Names
Zona pellucida-binding protein 2. ZPBP-like protein
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6X784
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Expression Region
1-315 aa
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AA Sequence
MRTCVLLSAVLWCLTGDKIYVELHQNSPVLICMDFKLSKKEIVDPTYLWIGPNEKTLTGNNRINITETGQLMVKDFLEPLSGLYTCTLSYKTVKAETQEEKTVKKRYDFMVFAYREPDYSYQMAVRFTTRSCIGRYNDVFFRVLKKILDSLISDLSCHVIEPSYKCHSVEIPEHGLIHELFIAFQVNPFAPGWKGACNGSVDCEDTTNHNILQARDRIEDFFRSQAYIFYHNFNKTLPAMHFVDHSLQVVRLDSCRPGFGKNERLHSNCASCCVVCSPATFSPDVNVTCQTCVSVLTYGAKSCPQTSNKNQQYED
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Molecular Weight
62.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
ZPBP2, or ZP domain-containing protein 2, has gained attention in recent years due to its critical role in reproductive biology and the formation of the zona pellucida, a glycoprotein matrix surrounding oocytes and early embryos. The zona pellucida is essential for fertilization, providing a structural barrier and facilitating sperm binding. Research indicates that ZPBP2 is a key player in the integrity and functionality of this matrix. Understanding the structure and function of ZPBP2 through recombinant protein studies can elucidate its contributions to reproductive processes and potential implications for fertility treatments and contraceptive development. Moreover, abnormalities in ZPBP2 expression or function may relate to infertility or developmental disorders. Recent advances in molecular biology techniques have enabled researchers to produce and characterize ZPBP2 recombinantly, allowing for detailed studies of its biochemical properties, interaction with other zona pellucida proteins, and its role in sperm-egg recognition. Investigating ZPBP2 could provide insights into both fundamental biological mechanisms and applied sciences, particularly in improving reproductive health and addressing related medical challenges.











