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Rhesus CLP1 / COLEC12 Protein (His Tag)

COLEC12

Catalog Number P90148-C07B
Organism Species Rhesus
Host Baculovirus-Insect Cells
Synonyms COLEC12
Molecular Weight The recombinant rhesus COLEC12 comprises 658 amino acids and has a calculated molecular mass of 72.3 KDa.
predicted N His
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the rhesus COLEC12 (F6RUR9) (Ala37-Leu678) was expressed with a polyhistide tag at the N-terminus.
Bio-activity
Research Area Cancer |Invasion microenvironment |Adhesion molecule |Cell adhesion |Lectin |C-tyep lectin |
Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 7.4.
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background CLP1, also known as COLEC12, is a scavenger receptor that displays several functions associated with host defense. It contains 1 C-type lectin domain and 3 collagen-like domains. CLP1 is strongly expressed in placenta and moderately expressed in heart, skeletal muscle, small intestine and lung. It promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. CLP1 mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. It binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells. It binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). CLP1 may also play a role in the clearance of amyloid beta in Alzheimer disease.
Reference
  • Ramirez A, et al. (2008) Human RNA 5'-kinase (hClp1) can function as a tRNA splicing enzyme in vivo. RNA. 14(9):1737-45.
  • Danielsen JM, et al.. (2011) Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level. Mol Cell Proteomics. 10(3):M110.003590.
  • Kim W, et al. (2011) Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 44(2):325-40.
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