Recombinant Human CD302/CLEC13A Fc Chimera Protein, CF

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Recombinant Human CD302/CLEC13A Fc Chimera Protein SDS-PAGE
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Product Details

Recombinant Human CD302/CLEC13A Fc Chimera Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Recombinant Human CD302/CLEC13A Fc Chimer (Catalog # 10203-CL) is immobilized at 5 μg/mL, 100 μL/well, the concentration of Recombinant Human DEC-205/CD205 Fc Chimera (Catalog # 10205-DE) that produces 50% of the optimal binding response is 4-24 μg/mL.
Human embryonic kidney cell, HEK293-derived human CD302/CLEC13A protein
Human CD302/CLEC13A
Accession # Q8IX05-1
N-terminus C-terminus

Accession #
N-terminal Sequence
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
43 kDa
51-59 kDa, under reducing conditions

Product Datasheets

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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 500 μg/mL in 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.
  • 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.

Data Image

SDS-PAGE Recombinant Human CD302/CLEC13A Fc Chimera Protein SDS-PAGE View Larger

2 μg/lane of Recombinant Human CD302/CLEC13A Fc Chimera was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 51-59 kDa and 100-120 kDa, respectively.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.


Background: CD302/CLEC13A

CD302, also known as CLEC13A and DCL1, is a type I transmembrane C-type lectin receptor.  It was identified while cloning human DEC-205 and was termed DCL1 (DEC-205-associated C-type lectin-1) (1). In humans, the highest expression of CD302 transcripts was observed in the liver, followed by lungs, spleen, and myeloid PBMC populations including monocytes, granulocytes, and dendritic cells (DC) (2). Human CD302 is synthesized as a 232 amino acid (aa) protein that includes 22 aa signal peptide, a 146 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 43 aa cytoplasmic region. The extracellular domain is predicted to contain eight beta strands and two ɑ helices using NMR (3).  Within the ECD, human CD302 shares 82% aa sequence identity with mouse and rat CD302. Unlike other classical C-type lectin receptors, CD302 is missing the known amino acid residues essential for calcium-dependent sugar binding, suggesting that CD302 may not have classic sugar binding capacity. However, CD302 did have the ability to behave as an endocytosis/phagocytosis receptor (1). In addition, CD302 was shown to colocalize with F-actin rich migratory structures, including filopodia, lamellipodia, and podosomes in macrophages, where CD302 may bind yet to be determined endothelial ligands involved in DC adhesion or migration (1, 2). Further evidence that CD302 is involved in regulating DC migration, includes that CD302 knockout mice had reduced frequency and numbers of migratory DC within the lymph nodes (LN) and reduced in vivo capacity to reach draining LN (2). CD302 was also found to exist as an intergenic splice variant able to form a fusion protein with DEC-205/CD205 in Hodgkin's lymphoma cell lines (4). The CD302/DEC-205 fusion protein was also found to be expressed by mature dendritic cells which altered endocytic capacity of DEC-205, although the wild-type single gene transcripts were the dominant isoforms expressed (5). Due to its selective expression in myeloid immune populations, CD302 has become a potential therapeutic target for acute myeloid leukemia (AML) (6).

  1. Kato, M. et al. (2007) J. Immunol. 179:6052.
  2. Lo, T-H. et al. (2016) J. Immunol. 197:885.
  3. Pospisilova, E. et al. (2016) Biomol. NMR. Assign. 10:189.
  4. Kato, M. et al. (2003) J Biol Chem. 278:34035.
  5. Butler, M. et al. (2017) J. Immunol. 120:362.
  6. Lo, T-H. et al. (2019) PLoS One. 14:e0216368.
Entrez Gene IDs
9936 (Human); 66205 (Mouse); 295629 (Rat)
Alternate Names
BIMLEC; CD302 antigenC-type lectin domain family 13, member A; CD302 molecule; CD302; CLEC13A; CLEC13AMGC22301; C-type lectin domain family 13 member A; DCL1; DCL-1; DCL1C-type lectin BIMLEC; KIAA0022FLJ43091; Type I transmembrane C-type lectin receptor DCL-1


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