Cat: IPD-X28458

Recombinant Human CLIP1 Protein,Strep & His

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Analytical Data

  • Gene name

    CLIP1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CYLN1; RSN

  • Species

    Human

  • Source

    E. coli

  • Tag

    Strep;His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P30622-3

  • Expression Region

    A181-T339

  • Protein Length

    Partial

  • 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

CLIP1, also known as CAP-1, is a member of the cysteine-rich protein family and is primarily recognized for its role in cellular processes such as cytoskeletal organization, cell adhesion, and intracellular transport. Research into CLIP1 has gained momentum due to its involvement in crucial biological functions, including neuronal differentiation and synaptic stabilization, which are vital for proper brain function. Additionally, aberrations in CLIP1 expression have been linked to various neurological disorders, prompting investigations into its potential as a therapeutic target. The development of recombinant CLIP1 proteins enables researchers to study its structure-function relationships and interaction with other proteins in greater detail. By expressing and purifying CLIP1 in various systems, scientists can explore its biochemical properties, regulatory mechanisms, and roles in physiological and pathological contexts. This foundational understanding is essential for elucidating the potential of CLIP1 in drug discovery and the development of novel therapeutic strategies for diseases associated with its dysregulation.

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