Human Siglec-7 / CD328 Protein, His Tag (MALS verified)

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SG7-H5225-100ug
$360.00
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SG7-H5225-1mg (250ug X 4)
$2,615.00
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SG7-H5225
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Synonyms

CDw328, D-siglec, A79 membrane protein, p75, Adhesion inhibitory receptor molecule 1, AIRM-1

Source

Human Sigelc-7, His Tag (SG7-H5225) is expressed from human 293 cells (HEK293). It contains AA Gln 19 - Leu 353 (Accession # Q9Y286-1).

Predicted N-terminus: Gln 19

Molecular Characterization

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 38.8 kDa. The protein migrates as 55-65 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

The protein is designed as a dimer.

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 25 mM MES, 150 mM NaCl, pH5.5 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.

Introduction de fond

Siglec-7 is a member of the human CD33‐related Siglec receptor. The extracellular region of Siglec‐7 is characterized by an N‐terminal V‐set Ig domain that can bind sialic acid and two C2‐set Ig domains. The cytoplasmic tail of Siglec‐7 has one immune‐receptor tyrosine‐based inhibitory motif (ITIM) and one ITIM‐like motif. Siglec-7 is considered as a sialic acid-dependent immunoreceptor with inhibitory potential and expressed predominantly on human NK cells, monocytes and a small subset of CD8+ T cells.