Reactivity | HuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized rhCL-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 human CL-P1/COLEC12 protein Leu57-Leu742, with an N-terminal 9-His tag |
Accession # | |
N-terminal Sequence | His |
Structure / Form | Disulfide-linked homodimer |
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 | 76 kDa (monomer). 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 | 125-130 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). Human collectin placenta 1 (CL-P1; also known as collectin sub-family member 12 and SRCL type I [scavenger receptor with C-type lectin type I]) is a 110 kDa member of the collectin family of glycoproteins (5, 6). 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). Human CL-P1 is synthesized as a 742 amino acid (aa) type II transmembrane glycoprotein that contains an N-terminal 39 aa cytoplasmic domain, a 17 aa transmembrane segment, and a 686 aa C-terminal extracellular region (6). The short cytoplasmic domain contains an internalization motif (Y-K-R-F) while the extracellular region 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). Notably, this CRD recognizes galactose (and fucose) within the context of asialo-orosomucoids associated with the Lewisx epitope (7, 8). CL-P1 has a 300 kDa trimeric form due to its collagen-like and coiled-coil helical domains (1, 5). There is a 97 kDa, alternate splice form of CL-P1 (SRCL type II) that shows a 120 aa truncation at the C-terminus. This effectively removes the entire CRD found on full-length CL-P1 (6). Human CL-P1 is 93% aa identical to mouse CL-P1 over the entire extracellular region, and 87% aa identical within each species CRD (5, 9). Human CL-P1 is known to be expressed in vascular endothelial cells (5). CL-P1 may play a role in bacterial recognition or as a scavenger receptor for desialylated.
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