Cat: IPD-X25651

Recombinant Human Nicastrin Protein (HEK293),His

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Analytical Data

  • Gene name

    Nicastrin

  • 简介

    Nicastrin Protein, a crucial gamma-secretase complex subunit, catalyzes intramembrane cleavage of Notch receptors and APP.Operating in Notch and Wnt signaling, the complex modulates regulatory proteins and CTNNB1 levels.Collaborating with PSEN1/2, APH1A/B, and PSENEN/PEN2, Nicastrin binds to proteolytically processed C83 and C99 fragments, emphasizing its pivotal role in molecular pathways and cellular processes.Nicastrin Protein, Human (HEK293, His) is the recombinant human-derived Nicastrin protein, expressed by HEK293 , with C-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Nicastrin; NCSTN; KIAA0253

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    Q92542-1

  • Expression Region

    N34-E669

  • AA Sequence

    NSVERKIYIPLNKTAPCVRLLNATHQIGCQSSISGDTGVIHVVEKEEDLQWVLTDGPNPPYMVLLESKHFTRDLMEKLKGRTSRIAGLAVSLTKPSPASGFSPSVQCPNDGFGVYSNSYGPEFAHCREIQWNSLGNGLAYEDFSFPIFLLEDENETKVIKQCYQDHNLSQNGSAPTFPLCAMQLFSHMHAVISTATCMRRSSIQSTFSINPEIVCDPLSDYNVWSMLKPINTTGTLKPDDRVVVAATRLDSRSFFWNVAPGAESAVASFVTQLAAAEALQKAPDVTTLPRNVMFVFFQGETFDYIGSSRMVYDMEKGKFPVQLENVDSFVELGQVALRTSLELWMHTDPVSQKNESVRNQVEDLLATLEKSGAGVPAVILRRPNQSQPLPPSSLQRFLRARNISGVVLADHSGAFHNKYYQSIYDTAENINVSYPEWLSPEEDLNFVTDTAKALADVATVLGRALYELAGGTNFSDTVQADPQTVTRLLYGFLIKANNSWFQSILRQDLRSYLGDGPLQHYIAVSSPTNTTYVVQYALANLTGTVVNLTREQCQDPSKVPSENKDLYEYSWVQGPLHSNETDRLPRCVRSTARLARALSPAFELSQWSSTEYSTWTESRWKDIRARIFLIASKELE

  • Protein Length

    Extracellular Domain

  • Molecular Weight

    105-125 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.

Quality inspection process

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Protein Description

Neuroligin-1 (NLGN1) is a crucial postsynaptic protein that plays a significant role in the formation and function of synapses in the central nervous system. It is involved in mediating excitatory and inhibitory synaptic transmission and is essential for maintaining synaptic stability and plasticity. Research has indicated that mutations or alterations in NLGN1 expression are linked to various neurodevelopmental disorders, including autism spectrum disorders and intellectual disabilities. The study of NLGN1 recombinant proteins is important for understanding its structure-function relationships, as well as its interaction with presynaptic partners, such as neurexins. These insights can help elucidate the molecular mechanisms underlying synaptogenesis and synaptic dysfunction associated with neurological diseases. Furthermore, exploring the therapeutic potential of NLGN1-targeted interventions may lead to new approaches for treating synaptic disorders. As such, the recombinant production of NLGN1 allows researchers to investigate its biophysical properties, binding affinities, and functional roles, thereby advancing our understanding of synaptic biology and its implications in health and disease.

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