Cat: PAX2000-11309

Recombinant Human SILV Protein,His

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Analytical Data

  • Gene name

    SILV

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    95 kDa melanocyte specific secreted glycoprotein; 95 kDa melanocyte-specific secreted glycoprotein; D12S53E; gp100; M-beta; ME20; ME20 M/ME20 S; ME20-M; ME20-S; ME20M; ME20M/ME20S; ME20S; Melanocyte lineage specific antigen GP100 ; Melanocyte protein mel 17 ; Melanocyte protein Pmel 17; Melanocyte protein Pmel 17 precursor ; Melanocytes lineage-specific antigen GP100; Melanoma associated ME20 antigen; Melanoma gp100; Melanoma-associated ME20 antigen; Melanosomal matrix protein 17; Melanosomal matrix protein17; P1; p100; p26; PMEL 17; PMEL; PMEL_HUMAN; PMEL17; Premelanosome protein; Secreted melanoma-associated ME20 antigen; SI; SIL; SILV; Silver (mouse homolog) like; Silver homolog; Silver locus protein homolog; Silver. mouse. homolog of

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P40967

  • Expression Region

    25-467 aa

  • AA Sequence

    KVPRNQDWLGVSRQLRTKAWNRQLYPEWTEAQRLDCWRGGQVSLKVSNDGPTLIGANASFSIALNFPGSQKVLPDGQVIWVNNTIINGSQVWGGQPVYPQETDDACIFPDGGPCPSGSWSQKRSFVYVWKTWGQYWQVLGGPVSGLSIGTGRAMLGTHTMEVTVYHRRGSRSYVPLAHSSSAFTITDQVPFSVSVSQLRALDGGNKHFLRNQPLTFALQLHDPSGYLAEADLSYTWDFGDSSGTLISRALVVTHTYLEPGPVTAQVVLQAAIPLTSCGSSPVPGTTDGHRPTAEAPNTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEVISTAPVQMPTAESTGMTPEKVPVSEVMGTTLAEMSTPEATGMTPAEVSIVVLSGTTAAQVTTTEWVETTARELPIPEPEGPDASSIMSTESITGSLGPLLDGTATLRLV

  • Molecular Weight

    49.0kDa 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

SILV, or Sialic Acid-Binding Immunoglobulin-Like Lectin V, is a type of protein that plays a crucial role in various biological processes, particularly in the immune response and cell signaling. The research on SILV recombinant proteins has gained significant attention due to their potential applications in biomedicine and biotechnology. One key area of interest is the understanding of how SILV interacts with sialylated glycoproteins and glycolipids on cell surfaces, which can influence cell adhesion, migration, and immune evasion mechanisms in pathogens and cancer cells. The ability to produce SILV as a recombinant protein enables researchers to investigate its structural and functional characteristics in detail. By employing various expression systems, scientists have successfully generated recombinant SILV in quantities sufficient for functional assays and structural studies. This research aims to elucidate the molecular mechanisms underlying SILV's interactions, which could lead to the development of novel therapeutic strategies targeting diseases where these interactions play a critical role, such as autoimmune disorders and cancer. Furthermore, exploring the potential use of SILV-based fusion proteins in drug delivery and targeted therapies holds promise for enhancing the efficacy of existing treatments. Thus, the ongoing studies on SILV recombinant proteins not only contribute to our fundamental understanding of cellular interactions but also pave the way for innovative approaches in disease management and treatment.

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