Cat: IPD-X24027

Recombinant Human OBCAM/OPCML Protein,His

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Analytical Data

  • Gene name

    OBCAM/OPCML

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    OBCAM; OPCM; IGLON1; IgLON Family Member 1; Opioid-binding cell adhesion molecule; IgLON family member 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q14982

  • Expression Region

    Pro39~Thr310

  • Molecular Weight

    34kDa

  • 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

OBCAM (Oligodendrocyte-Bound Cell Adhesion Molecule) and OPCML (Oligodendrocyte Precursor Cell Market-Like) proteins are significant in the context of neurobiology and cell adhesion research. Both proteins are members of the immunoglobulin superfamily and have been implicated in crucial processes such as oligodendrocyte development, myelination, and neuronal-glial interactions. OBCAM, predominantly expressed in oligodendrocytes, plays a role in myelin sheath formation and maintenance, impacting the overall functionality of the central nervous system. Conversely, OPCML is associated with oligodendrocyte precursor cell regulation and may exert tumor suppressive functions in various cancers, suggesting its broader relevance beyond neurobiology. Research into these proteins has gained momentum due to their potential implications in neurodegenerative diseases, such as multiple sclerosis and amyotrophic lateral sclerosis, where myelin degeneration is a critical factor. Understanding the mechanisms underlying OBCAM and OPCML functions could lead to novel therapeutic strategies aimed at promoting remyelination and restoring neuronal health. Recent advances in recombinant protein technology have enabled the study of these molecules in greater detail, facilitating insights into their structure-function relationships and interactions with other cellular components. As the scientific community continues to explore the biological roles of OBCAM and OPCML, their study represents a promising avenue for advancing our knowledge of neural cell biology and developing targeted therapies for demyelinating conditions.

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