Human Siglec-8 Protein, Fc Tag

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SI8-H5254-100ug
$395.00
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SI8-H5254-1mg (500ug X 2)
$2,615.00
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SI8-H5254
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Synonyms

Siglec-8, SAF-2, SIGLEC8, SAF2

Source

Human Siglec-8, Fc Tag (SI8-H5254) is expressed from human 293 cells (HEK293). It contains AA Met 17 - Ala 363 (Accession # Q9NYZ4-1).

Predicted N-terminus: Met 17

Molecular Characterization

This protein carries a human IgG1 Fc tag at the C-terminus.

The protein has a calculated MW of 64.3 kDa. The protein migrates as 70-80 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>95% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

Reconstitution

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Shipping and Storage

This product is shipped at ambient temperature.

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.

Background

Siglec-8 is also known as SIGLEC8, SAF2, SIGLEC-8, SIGLEC8L and sialic acid binding Ig like lectin 8. Siglec-8 was first identified by CD33 homology screening of ESTs from a cD library generated from a patient diagnosed with idiopathic hypereosinophilic syndrome and was originally termed SAF-2 (sialoadhesin family 2). At the tissue level, Siglec-8 mR was found to be most highly expressed in lung, PBMCs, spleen, and kidney. Two splice variants of Siglec-8 exist. The initially characterized form contains 431 amino acid residues in total, subsequently, a longer form of Siglec-8, initially termed Siglec-8L. Both forms of Siglec-8 are found in eosinophils and contain a V-set domain with lectin activity and two C2-type Ig repeat domains in the extracellular region.