Recombinant Human CD302/CLEC13A Fc Chimera Protein, CF Summary
Details of Functionality |
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. |
Source |
Human embryonic kidney cell, HEK293-derived human CD302/CLEC13A protein Human CD302/CLEC13A (Asp23-Asn167) Accession # Q8IX05-1 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Asp23 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
43 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
51-59 kDa, under reducing conditions |
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.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CD302/CLEC13A Fc Chimera Protein, CF
Background
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).
- Kato, M. et al. (2007) J. Immunol. 179:6052.
- Lo, T-H. et al. (2016) J. Immunol. 197:885.
- Pospisilova, E. et al. (2016) Biomol. NMR. Assign. 10:189.
- Kato, M. et al. (2003) J Biol Chem. 278:34035.
- Butler, M. et al. (2017) J. Immunol. 120:362.
- Lo, T-H. et al. (2019) PLoS One. 14:e0216368.
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