Cat: PA1000-9136

Recombinant Human ZP2 Protein,His

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Analytical Data

  • Gene name

    ZP2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ZP2;ZPA;Zona pellucida sperm-binding Protein 2

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q05996

  • Expression Region

    1-736aa

  • AA Sequence

    MACRQRGGSWSPSGWFNAGWSTYRSISLFFALVTSGNSIDVSQLVNPAFP GTVTCDEREITVEFPSSPGTKKWHASVVDPLGLDMPNCTYILDPEKLTLR ATYDNCTRRVHGGHQMTIRVMNNSAALRHGAVMYQFFCPAMQVEETQGLS ASTICQKDFMSFSLPRVFSGLADDSKGTKVQMGWSIEVGDGARAKTLTLP EAMKEGFSLLIDNHRMTFHVPFNATGVTHYVQGNSHLYMVSLKLTFISPG QKVIFSSQAICAPDPVTCNATHMTLTIPEFPGKLKSVSFENQNIDVSQLH DNGIDLEATNGMKLHFSKTLLKTKLSEKCLLHQFYLASLKLTFLLRPETV SMVIYPECLCESPVSIVTGELCTQDGFMDVEVYSYQTQPALDLGTLRVGN SSCQPVFEAQSQGLVRFHIPLNGCGTRYKFEDDKVVYENEIHALWTDFPP SKISRDSEFRNDMLLNINVESLTPPVASVKLGPFTLILQSYPDNSYQQPY GENEYPLVRFLRQPIYMEVRVLNRDDPNIKLVLDDCWATSTMDPDSFPQW NVVVDGCAYDLDNYQTTFHPVGSSVTHPDHYQRFDMKAFAFVSEAHVLSS LVYFHCSALICNRLSPDSPLCSVTCPVSSRHRRATGATEAEKMTVSLPGP ILLLSDDSSFRGVGSSDLKASGSSGEKSRSETGEEVGSRGAMDTKGHKTA GDVGSKAVAAVAAFAGVVATLGFIYYLYEKRTVSNH

  • Molecular Weight

    82.3 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

ZP2 is a vital glycoprotein found in the zona pellucida, a protective extracellular matrix surrounding mammalian oocytes. It plays a crucial role in fertilization by facilitating sperm binding and recognition, thereby initiating the process of sperm-egg fusion. The study of ZP2 recombinant protein has gained significance as it offers insights into reproductive biology and offers potential applications in fertility treatments and contraceptive development. Research has demonstrated that mutations in the ZP2 gene can lead to female infertility, highlighting its importance in normal reproductive function. Moreover, as a model for studying protein interactions during fertilization, ZP2 contributes to our understanding of species-specific sperm-egg recognition mechanisms. In recent years, advances in molecular biology techniques have enabled the production of ZP2 as a recombinant protein, allowing for detailed characterization and functional studies. This recombinant form is crucial for exploring its structural properties, binding affinities, and interactions with sperm, providing a powerful tool for elucidating the mechanisms underlying fertilization. The ongoing research on ZP2 not only enhances our understanding of reproductive physiology but also opens avenues for developing novel therapeutic strategies to address fertility issues in humans and other mammals. Thus, the exploration of ZP2 recombinant protein is integral to both fundamental biological research and applied reproductive medicine.

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