Cat: PA2000-8856

Recombinant Human LCA5 Protein,GST

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Analytical Data

  • Gene name

    LCA5

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    LCA5; C6orf152Lebercilin; Leber congenital amaurosis 5 protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    GST-tag at N-terminal

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q86VQ0

  • Expression Region

    1-697aa

  • AA Sequence

    MGERAGSPGTDQEREAGKHHYSYSSDFETPQSSGRSSLVSSSPASVRRKNPKRQTSDGQVHHQAPRKPSPKGLPNRKGVRVGFRSQSLNREPLRKDTDLVTKRILSARLLKINELQNEVSELQVKLAELLKENKSLKRLQYRQEKALNKFEDAENEISQLIFRHNNEITALKERLRKSQEKERATEKRVKDTESELFRTKFSLQKLKEISEARHLPERDDLAKKLVSAELKLDDTERRIKELSKNLELSTNSFQRQLLAERKRAYEAHDENKVLQKEVQRLYHKLKEKERELDIKNIYSNRLPKSSPNKEKELALRKNAACQSDFADLCTKGVQTMEDFKPEEYPLTPETIMCYENKWEEPGHLTLDLQSQKQDRHGEAGILNPIMEREEKFVTDEELHVVKQEVEKLEDEWEREELDKKQKEKASLLEREEKPEWETGRYQLGMYPIQNMDKLQGEEEERLKREMLLAKLNEIDRELQDSRNLKYPVLPLLPDFESKLHSRERSPKTYRFSESSERLFNGHHLQDISFSTPKGEGQNSGNVRSPASPNEFAFGSYVPSFAKTSERSNPFSQKSSFLDFQRNSMEKLSKDGVDLITRKEKKANLMEQLFGASGSSTISSKSSGPNSVASSKGDIDPLNFLPGNKGSRDQEHDEDEGFFLSEGRSFNPNRHRLKHADDKPAVKAADSVEDEIEEVALR

  • Molecular Weight

    106.9 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

LCA5 (Lysosome-Associated Protein 5) is a protein associated with the lysosomal function in cells and plays a critical role in the processes of phagocytosis and lysosomal degradation. Its relevance has gained attention due to its association with several inherited retinal diseases, particularly the rare condition known as LCA (Leber Congenital Amaurosis), which leads to severe vision impairment in early childhood. Research into LCA5 has been driven by the need to understand the molecular mechanisms underlying these diseases, as mutations in the LCA5 gene disrupt normal cellular processes, leading to photoreceptor cell dysfunction and subsequent retinopathy. Advances in recombinant protein production techniques have enabled researchers to produce LCA5 in vitro, facilitating the study of its structure and function. Investigations into the recombinant LCA5 protein aims to elucidate its role in lysosomal trafficking and its potential interaction with other cellular components. This knowledge can provide insights into potential therapeutic strategies, including gene replacement therapies that target the underlying genetic defects in patients. As understanding improves, the hope is to develop effective interventions that could restore vision or halt the progression of retinal degeneration in affected individuals. Overall, research on LCA5 recombinant protein holds promise for advancing our understanding of lysosomal disorders and paving the way for innovative treatments in the field of ophthalmology.

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