Human SIRP beta / CD172b Protein, Fc Tag (MALS verified)

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SIA-H5257-100ug
$360.00
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SIA-H5257-1mg (500ug X 2)
$2,615.00
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SIA-H5257
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Synonyms

CD172b antigen, CD172b, DKFZp686A05192, FLJ26614, SIRP beta 1, SIRPB1, SIRP-BETA-1, 9930027N05Rik, SIRP-beta

Source

Human SIRP beta, Fc Tag (SIA-H5257) is expressed from human 293 cells (HEK293). It contains AA Glu 30 - Leu 371 (Accession # O00241-1).

Predicted N-terminus: Glu 30

Molecular Characterization

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

The protein has a calculated MW of 63.7 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

>90% as determined by SDS-PAGE.

>95% as determined by SEC-MALS.

Formulation

Lyophilized from 0.22 μm filtered solution in Tris with Glycine, Arginine and NaCl, pH7.5 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.

Background

Signal-regulatory protein beta-1 (SIRP beta 1) also known as SIRPβ1, belongs to signal-regulatory-protein (SIRP) family, and immunoglobulin superfamily. SIRPβ1 is a transmembrane protein that has three Ig-like domains in its extracellular region and a short cytoplasmic tail. Human SIRPβ1 is expressed on monocytes and granulocytes but not on lymphocytes. SIRP beta 1 contains short cytoplasmic domains that lack cytoplasmic sequence motifs capable of recruiting SHP-2 and SHP-1. In addition, they contain a single basic lysine residue within the hydrophobic transmembrane domain.