Cat: IPD-X41310

Recombinant Pig SIGLEC1 Protein ,His & Myc

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Analytical Data

  • Gene name

    SIGLEC1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    pSn;Sialic acid-binding Ig-like lectin 1;Siglec-1;p210

  • Species

    Pig

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    A7LCJ3

  • Expression Region

    20-153aa

  • Molecular Weight

    22.3 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.

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Protein Description

SIGLEC1 (Sialic Acid Binding Immunoglobulin-like Lectin 1), also known as sialoadhesin, is a type of cell surface receptor predominantly expressed on macrophages and dendritic cells. It plays a crucial role in the immune system by recognizing sialylated glycoproteins and glycolipids, which are often found on the surface of pathogenic organisms and infected cells. The study of SIGLEC1 has garnered attention due to its potential implications in various diseases, including infections, cancers, and autoimmune disorders. Researchers have been exploring the functional aspects of SIGLEC1, investigating how its binding mechanisms can influence immune responses and contribute to the regulation of inflammation. Additionally, there has been a growing interest in developing SIGLEC1 recombinant proteins for therapeutic applications, such as targeted drug delivery and as biomarkers for disease diagnosis. The engineering of SIGLEC1 as a recombinant protein allows for detailed studies of its structure-function relationships and opens avenues for using it in the development of novel immunotherapies, aimed at modulating immune responses for disease treatment. Understanding the complexities of SIGLEC1 interactions at the molecular level is essential for harnessing its potential in clinical applications and advancing our knowledge of immune system regulation.

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