CL-P1/COLEC12 Antibody [Biotin]

• Applications: WB
• Clonality: Polyclonal
• Host: Goat
• Conjugate: Biotin
• Concentration: LYOPH

CL-P1/COLEC12 Antibody [Biotin] Summary

• Immunogen: Mouse myeloma cell line NS0-derived recombinant mouse CL‑P1/COLEC12
  Ala101-Leu742
  Accession # Q8K4Q8
• Specificity: Detects mouse CL‑P1/COLEC12 in Western blots.
• Source: N/A
• Isotype: IgG
• Clonality: Polyclonal
• Host: Goat
• Gene: Colec12
• Purity Statement: Antigen Affinity-purified

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.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
• Preservative: No Preservative
• Concentration: LYOPH
• Reconstitution Instructions: Reconstitute at 0.2 mg/mL in sterile PBS.

Notes

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

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 Lewis^x 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.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Bioinformatics

• Gene Symbol: Colec12