Call Now

Rat CLP1 / COLEC12 Protein (His Tag)

Clp1, Nsr2, COLEC12

Catalog Number P80394-R07B
Organism Species Rat
Host Baculovirus-Insect Cells
Synonyms Clp1, Nsr2, COLEC12
Molecular Weight The recombinant ratCOLEC12 consists of 658 amino acids and predicts a molecular mass of 72.4 KDa. It migrates as an approximately 90 KDa band in SDS-PAGE under reducing conditions.
predicted N His
SDS-PAGE
Purity > 99 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mature form of rat COLEC12 (Q4V885) (Ala101-Leu742) 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, pH 8.0
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 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.
  •