Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized rmCL-P1 at 5 µg/mL (100 µL/well) can bind biotinylated advance glycation endproducts of bovine serum albumin (AGE-BSA) with a linear range of 3-200 ng/mL. |
Source | Mouse myeloma cell line, NS0-derived mouse CL-P1/COLEC12 protein Ala101-Leu742, with an N-terminal 6-His tag |
Accession # | |
N-terminal Sequence | His |
Protein/Peptide Type | Recombinant Proteins |
Gene | Colec12 |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 71 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 118-133 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
Collectins are a family of Ca++-dependent, C-type lectins that contain a collagenous domain and function as recognition molecules for molecular patterns found on pathogens (1 - 4). Collectin placenta 1 (CL-P1), also known as collectin sub-family member 12 and scavenger receptor with C-type lectin type I (SRCL), is a 140 kDa member of the collectin family of glycoproteins. With two exceptions, all collectins are secreted. CL-P1 is the only collectin known to be membrane bound, while CL-L1 (collectin liver-1) is the only known cytoplasmic collectin (1). Mouse CL-P1 is synthesized as a 742 amino acid (aa) type II transmembrane glycoprotein that includes an N-terminal 39 aa cytoplasmic domain, an 18 aa transmembrane segment, and a 685 aa C-terminal extracellular domain. The short cytoplasmic domain contains an internalization motif (Y-K-R-F), while the ECD is complex, demonstrating a coiled-coil segment, a Ser-Thr rich region, a collagen-like structure, and a C-type lectin/carbohydrate recognition domain (CRD) (5, 6). Unlike human CL-P1, no splice variants of mouse CL-P1 have been described (5, 7). Trimerization of CL-P1 is mediated by its collagen-like and coiled-coil helical domains (1, 6). Within the ECD, mouse CL-P1 shares 88%, 89%, 92%, and 98% aa sequence identity with bovine, canine, human, and rat CL-P1, respectively. The CRD shares 23 - 27% aa sequence identity with the CRD of collectins CL-L1, collectin sub-family member 11, MBL, SP-A1, and SP-D. Notably, this CRD recognizes galactose and fucose within the context of asialo-orosomucoids associated with the Lewisx epitope (8, 9). CL-P1 is expressed in vascular endothelial cells and may play a role in bacterial recognition or as a scavenger receptor for desialylated glycoproteins (6, 8).
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