Recombinant Mouse CL-P1/COLEC12 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Mouse CL-P1/COLEC12 Protein, CF Summary

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.

Applications/Dilutions

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.
SDS-PAGE
118-133 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse CL-P1/COLEC12 Protein, CF

  • CL-P1
  • CLP1, cleavage and polyadenylation factor I subunit, homolog (S. cerevisiae)
  • COLEC12
  • EC 2.7.1.78
  • hClp1
  • HEABATP/GTP-binding protein
  • homolog of yeast CFIA subunit Clp1p
  • NSR2
  • Polynucleotide kinase Clp1
  • polyribonucleotide 5'-hydroxyl-kinase Clp1
  • Pre-mRNA cleavage complex II protein Clp1
  • SCARA4
  • SRCL Type I

Background

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).

  1. van de Wetering, J.K. et al. (2004) Eur. J. Biochem. 271:1229.
  2. Holmskov, U. et al. (2003) Annu. Rev. Immunol. 21:547.
  3. Hoppe, H-J. and K. Reid (1994) Protein Sci. 3:1143.
  4. Hickling, T.P. et al. (2004) J. Leukoc. Biol. 75:27.
  5. Nakamura, K. et al. (2001) Biochim. Biophys. Acta 1522:53.
  6. Ohtani, K. et al. (2001) J. Biol. Chem. 276:44222.
  7. Nakamura, K. et al. (2001) Biochem. Biophys. Res. Commun. 280:1028.
  8. Coombs, P.J. et al. (2005) J. Biol. Chem. 280:22993.
  9. Yoshida, T. et al. (2003) J. Biochem. 133:271.

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Bioinformatics

Gene Symbol Colec12
Entrez
Uniprot