Recombinant Mouse CD302/CLEC13A Protein (Fc Tag) | PKSM040534

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SKU:
575-PKSM040534
Weight:
1.00 KGS
€1,120.00
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Description

Recombinant Mouse CD302/CLEC13A Protein (Fc Tag) | PKSM040534 | Gentaur US, UK & Europe Disrtribition

Synonyms: 1110055L24Rik;AI159627

Active Protein: N/A

Activity: A DNA sequence encoding the extracellular domain of mouse CD302 isoform 2 (Q9DCG2-2) (Met 1-His 156) was fused with the Fc region of human IgG1 at the C-terminus.

Protein Construction: A DNA sequence encoding the extracellular domain of mouse CD302 isoform 2 (Q9DCG2-2) (Met 1-His 156) was fused with the Fc region of human IgG1 at the C-terminus.

Fusion Tag: C-Fc

Species: Mouse

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 93 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 42.6 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: CD302/CLEC13A (C-type lectin domain family 13 member A), also known as C-type lectin receptor DCL-1, is a type I transmembrane C-type lectin DCL-1/CD302. DCL-1 protein was highly conserved among the human, mouse, and rat orthologs. DCL-1 ectodomain contains only one CRD, whereas other type I transmembrane C-type lectins contain more than one domain (e.g. selectins and MMR). DCL-1 CP contains several putative motifs, including a Tyr-based internalization, a cluster of acidic amino acids, and Ser and Tyr phosphorylation motifs, suggesting that DCL-1 CP mediates not only endocytosis and late endosome targeting but also signaling. DCL-1 may be another cell/matrix adhesion receptor integrated in cell adhesion complexes and that DCL-1 dysfunction may affect APC adhesion and migration, causing suppression of APC function.

Research Area: N/A

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