J774A.1 mouse reticulum cell sarcoma macrophage cell line was stained with Goat Anti-Mouse CL‑P1/COLEC12 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3130, filled histogram) or isotype control antibody ...read more
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 6 months, -20 to -70 degreesC 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 [Unconjugated]
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). 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).
van de Wetering, J.K. et al. (2004) Eur. J. Biochem. 271:1229.
Holmskov, U. et al. (2003) Annu. Rev. Immunol. 21:547.
Hoppe, H-J. and K. Reid (1994) Protein Sci. 3:1143.
Hickling, T.P. et al. (2004) J. Leukoc. Biol. 75:27.
Nakamura, K. et al. (2001) Biochim. Biophys. Acta 1522:53.
Ohtani, K. et al. (2001) J. Biol. Chem. 276:44222.
Nakamura, K. et al. (2001) Biochem. Biophys. Res. Commun. 280:1028.
Coombs, P.J. et al. (2005) J. Biol. Chem. 280:22993.
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.
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