When Recombinant Human CD69 is coated at 5 µg/mL (100 µL/well), the concentration of Recombinant Human Galectin-1 Recombinant Human Galectin‑1 (Catalog # 1152-GA) that produces a 50% optimal binding response ...read more
1 μg/lane of Recombinant Human CD69 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing R bands at 22.0, 27.9 kDa and NR bands at 39.3, 42.1, 47.2 ...read more
Measured by its binding ability in a functional ELISA. When Recombinant Human CD69 is coated at 5 µg/mL (100 µL/well), the concentration of Recombinant Human Galectin-1 (Catalog # 1152‑GA) that produces a 50% optimal binding response is 0.4-2 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human CD69 protein Gly64-Lys199 with an N-terminal 9-His tag
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
17 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
20-30 kDa, reducing conditions
Publications
Read Publication using 8468-CD in the following applications:
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
>95%, by SDS-PAGE with silver staining
Reconstitution Instructions
Reconstitute at 250 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 CD69 Protein, CF
activation inducer molecule (AIM/CD69)
Activation inducer molecule
AIM
BL-AC/P26
CD69 antigen (p60, early T-cell activation antigen)
CD69 antigen
CD69 molecule
CD69
CLEC2CC-type lectin domain family 2 member C
C-type lectin domain family 2, member C
EA1
EA-1
early activation antigen CD69
early lymphocyte activation antigen
Early T-cell activation antigen p60
GP32/28
Leu23
Leukocyte surface antigen Leu-23
MLR-3
p60
Background
CD69, also known as CLEC2C, is a type 2 transmembrane glycoprotein in the C-type lectin family. It plays roles in immune cell trafficking, inflammation, T cell memory, and humoral immune responses (1). Mature human CD69 consists of a 40 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 138 aa extracellular domain with one C-type lectin domain (CTL) (2-4). Within the ECD, human CD69 shares 57% aa sequence identity with mouse and rat CD69. CD69 is expressed on the cell surface as an approximately 60 kDa disulfide-linked homodimer (3-5). It is found on CD4+ T cells, CD8+ T cells, NK cells, NKT cells, gamma delta cells dendritic cells (DC) and is up-regulated on activated T cells and DC (6-8). Ligation of CD69 on DC induces IL-2 production, leading to T cell proliferation (6). CD69 is important for the homing of CD4+ T cells and plasmablasts to the bone marrow but inhibits the migration of dermal DC to draining lymph nodes (7, 9). It supports the expression of multiple chemokines and chemokine receptors but suppresses the expression of others (10, 11). It associates with and negatively regulates S1P1 expression on DC and CD4+ T cells, resulting in a decreased chemotactic response to S1P (7, 12, 13). S1P1 similarly inhibits the cell surface expression of CD69 (12). The direct interaction of CD69 with Galectin-1 contributes to the ability of CD69 to limit Th17 mediated inflamamtion while supporting the differentiation of regulatory T cells (8, 10, 13-16). In various disease models, CD69 has been shown to have both enhancing and inhibitory effects on Th17 and Th2 cell mediated inflammation (8, 10, 11, 13, 16, 17).
Gonzalez-Amaro, R. et al. (2013) Trends Mol. Med. 19:625.
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Hamann, J. et al. (1993) J. Immunol. 150:4920.
Lopez-Cabrera, M. et al. (1993) J. Exp. Med. 178:537.
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Alari-Pahissa, E. et al. (2012) J. Leukoc. Biol. 92:145.
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Radulovic, K. et al. (2012) J. Immunol. 188:2001.
Shinoda, K. et al. (2012) Proc. Natl. Acad. Sci. USA 109:7409.
Radulovic, K. et al. (2013) PLoS ONE 8:e65413.
Hasegawa, A. et al. (2013) PLoS ONE 8:e65494.
Shiow, L.R. et al. (2006) Nature 440:540.
Martin, P. et al. (2010) J. Allergy Clin. Immunol. 126:355.
Martin, P. et al. (2010) Mol. Cell. Biol. 30:4877.
de la Fuente, H. et al. (2014) Mol. Cell. Biol. 34:2479.
Cruz-Adalia, A. et al. (2010) Circulation 122:1396.
Miki-Hosokawa, T. et al. (2009) J. Immunol. 183:8203.
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