Recombinant Human CL-P1/COLEC12 Protein, CF Summary
Leu57-Leu742, with an N-terminal 9-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in sterile PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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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- Holmskov, U. et al. (2003) Annu. Rev. Immunol. 21:547.
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- Hickling, T.P. et al. (2004) J. Leukoc. Biol. 75:27.
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- Nakamura,K. et al. (2001) Biochem. Biophys. Res. Commun. 280:1028.
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- Yoshida, T. et al. (2003) J. Biochem. 133:271.
- Nakamura, K. et al. (2001) Biochim. Biophys. Acta 1522:53.
Citations for Recombinant Human CL-P1/COLEC12 Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Rapid and Efficient Purification of Functional Collectin-12 and Its Opsonic Activity against Fungal Pathogens
Authors: J Zhang, A Li, CQ Yang, P Garred, YJ Ma
J Immunol Res, 2019;2019(0):9164202.
Sample Types: Recombinant Protein
Applications: ELISA Standard
Soluble Collectin-12 (CL-12) Is a Pattern Recognition Molecule Initiating Complement Activation via the Alternative Pathway.
Authors: Ma Y, Hein E, Munthe-Fog L, Skjoedt M, Bayarri-Olmos R, Romani L, Garred P
J Immunol, 2015;195(7):3365-73.
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