CL-P1/COLEC12 Antibody

HUVEC human umbilical vein endothelial cells were stained with Goat Anti-Human CL‑P1/COLEC12 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2690, filled histogram) or isotype control antibody (Catalog # AB-108-C, open histogram), followed by Allophycocyanin-conjugated Anti-Goat IgG Secondary Antibody (Catalog # F0108).

MCAM and COLEC12 are novel BEC- and LEC- specific markers.Two new endothelial markers MCAM and COLEC12 (selected from our analysis of Dataset B) were used to stain (A) normal human lymph nodes together with two established vascular markers PV-1 (for BEC) and CLEVER-1 (for LEC). In addition, (B) chronically inflamed tonsils and (C) specimens from bladder cancer and colorectal cancer were stained with the antibodies against the indicated proteins. LYVE-1 and COLEC12 co-staining was done on colorectal cancer specimens, whereas the other stainings represent bladder cancer. MCAM staining colocalized very well with the established BEC marker PV-1 whereas no colocalization could be detected between MCAM and the established LEC markers LYVE-1 and podoplanin. COLEC12-staining on the other hand showed colocalization with LYVE-1 but not PV-1. White arrows point to areas of colocalization. Nuclear counterstaining was performed with DAPI. Scale bars represent 100 µm. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24058540), licensed under a CC-BY license. Not internally tested by R&D Systems.

MCAM and COLEC12 are novel BEC- and LEC- specific markers.Two new endothelial markers MCAM and COLEC12 (selected from our analysis of Dataset B) were used to stain (A) normal human lymph nodes together with two established vascular markers PV-1 (for BEC) and CLEVER-1 (for LEC). In addition, (B) chronically inflamed tonsils and (C) specimens from bladder cancer and colorectal cancer were stained with the antibodies against the indicated proteins. LYVE-1 and COLEC12 co-staining was done on colorectal cancer specimens, whereas the other stainings represent bladder cancer. MCAM staining colocalized very well with the established BEC marker PV-1 whereas no colocalization could be detected between MCAM and the established LEC markers LYVE-1 and podoplanin. COLEC12-staining on the other hand showed colocalization with LYVE-1 but not PV-1. White arrows point to areas of colocalization. Nuclear counterstaining was performed with DAPI. Scale bars represent 100 µm. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24058540), licensed under a CC-BY license. Not internally tested by R&D Systems.

MCAM and COLEC12 are novel BEC- and LEC- specific markers.Two new endothelial markers MCAM and COLEC12 (selected from our analysis of Dataset B) were used to stain (A) normal human lymph nodes together with two established vascular markers PV-1 (for BEC) and CLEVER-1 (for LEC). In addition, (B) chronically inflamed tonsils and (C) specimens from bladder cancer and colorectal cancer were stained with the antibodies against the indicated proteins. LYVE-1 and COLEC12 co-staining was done on colorectal cancer specimens, whereas the other stainings represent bladder cancer. MCAM staining colocalized very well with the established BEC marker PV-1 whereas no colocalization could be detected between MCAM and the established LEC markers LYVE-1 and podoplanin. COLEC12-staining on the other hand showed colocalization with LYVE-1 but not PV-1. White arrows point to areas of colocalization. Nuclear counterstaining was performed with DAPI. Scale bars represent 100 µm. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24058540), licensed under a CC-BY license. Not internally tested by R&D Systems.

• Reactivity: Hu
• Applications: WB, Flow, B/N, CyTOF-ready, ICC/IF
• Clonality: Polyclonal
• Host: Goat
• Conjugate: Unconjugated
• Concentration: LYOPH

CL-P1/COLEC12 Antibody Summary

• Immunogen: Mouse myeloma cell line NS0-derived recombinant human CL‑P1/COLEC12 isoform 1
  Leu57-Leu742
  Accession # Q5KU26
• Specificity: Detects CL‑P1/COLEC12 in direct ELISAs and Western blots. In direct ELISAs, approximately 45% cross‑reactivity with recombinant mouse CL-P1 is observed.
• Source: N/A
• Isotype: IgG
• Clonality: Polyclonal
• Host: Goat
• Gene: COLEC12
• Purity Statement: Antigen Affinity-purified

Applications/Dilutions

• Dilutions:
  • Blockade of Receptor-ligand Interaction
  • CyTOF-ready
  • Flow Cytometry 2.5 ug/10^6 cells
  • Immunocytochemistry 5-15 ug/mL
  • Western Blot 0.1 ug/mL

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 Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
• 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.

Alternate Names for CL-P1/COLEC12 Antibody

• CL-P1
• CLP1hCL-P1
• COLEC12
• collectin placenta 1
• Collectin placenta protein 1
• collectin sub-family member 12
• collectin-12
• NSR2
• Nurse cell scavenger receptor 2
• SCARA4
• SCARA4NSR2
• Scavenger receptor class A member 4
• scavenger receptor class A, member 4
• SRCL Type I
• SRCLScavenger receptor with C-type lectin

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). 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). 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 Lewis^x 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 over the CRD region (5, 9). Human CL-P1 is known to be expressed in vascular endothelial cells (5).

1. van de Wetering, JK. 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. Ohtani, K. et al. (2001) J. Biol. Chem. 276:44222.
6. Nakamura,K. et al. (2001) Biochem. Biophys. Res. Commun. 280:1028.
7. Coombs, P.J. et al. (2005) J. Biol. Chem. 280:22993.
8. Yoshida, T. et al. (2003) J. Biochem. 133:271.
9. Nakamura, K. et al. (2001) Biochim. Biophys. Acta 1522:53.

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.

Publications for CL-P1/COLEC12 Antibody (AF2690)(4)

Publications using AF2690

• J Zhang, A Li, CQ Yang, P Garred, YJ Ma Rapid and Efficient Purification of Functional Collectin-12 and Its Opsonic Activity against Fungal Pathogens J Immunol Res, 2019-07-29;2019(0):9164202. 2019-07-29 [PMID: 31482100] (ELISA Capture, Western Blot, Human)
• JF Bogie, J Mailleux, E Wouters, W Jorissen, E Grajchen, J Vanmol, K Wouters, N Hellings, J Van Horsen, T Vanmierlo, JJ Hendriks Scavenger receptor collectin placenta 1 is a novel receptor involved in the uptake of myelin by phagocytes Sci Rep, 2017-03-20;7(0):44794. 2017-03-20 [PMID: 28317919] (Flow Cytometry, IHC, Western Blot, Human)
• Ma Y, Hein E, Munthe-Fog L, Skjoedt M, Bayarri-Olmos R, Romani L, Garred P Soluble Collectin-12 (CL-12) Is a Pattern Recognition Molecule Initiating Complement Activation via the Alternative Pathway. J Immunol, 2015-08-19;195(7):3365-73. 2015-08-19 [PMID: 26290605] (Flow Cytometry)
• Keuschnigg , Johannes, Karinen , Sirkku, Auvinen , Kaisa, Irjala , Heikki, Mpindi , John-Pat, Kallioniemi , Olli, Hautaniemi , Sampsa, Jalkanen , Sirpa, Salmi , Marko Plasticity of blood- and lymphatic endothelial cells and marker identification. PLoS ONE, 2013-09-10;8(9):e74293. 2013-09-10 [PMID: 24058540] (IHC-Fr, Human)

Bioinformatics

• Gene Symbol: COLEC12
• Uniprot:
  • Q5KU26()