Mouse Siglec-2 / CD22 Protein, His Tag (MALS verified)

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SI2-M52Ha-100ug
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SI2-M52Ha-1mg (200ug X 5)
$2,245.00
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SI2-M52Ha
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Synonyms

CD22, SIGLEC2, BL-CAM, SIGLEC-2, Siglec2, SIGLEC2FLJ22814

Source

Mouse Siglec-2, His Tag (SI2-M52Ha) is expressed from human 293 cells (HEK293). It contains AA Ser 22 - Arg 702 (Accession # P35329-1).

Predicted N-terminus: Ser 22

Molecular Characterization

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

The protein has a calculated MW of 78.3 kDa. The protein migrates as 100 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.

>95% as determined by SEC-MALS.

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

B-cell receptor CD22 is also known as Sialic acid-binding Ig-like lectin 2 (Siglec-2), B-lymphocyte cell adhesion molecule (BL-CAM), T-cell surface antigen Leu-14, which belongs to the immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. CD22 mediates B-cell B-cell interactions, and may be involved in the localization of B-cells in lymphoid tissues. Siglec-2 / CD22 binds sialylated glycoproteins, one of which is CD45. Siglec2 / CD22 plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.