Measured by its binding ability in a functional ELISA. When Recombinant Human LRRC32/GARP is immobilized at 5 μg/mL (100 μL/well) Recombinant Human Latent TGF‑ beta 1 (Catalog # 299-LT) binds with an apparent Kd <30 nM.
Source
Chinese Hamster Ovary cell line, CHO-derived human LRRC32/GARP protein Met1-Asn627, with a C-terminal 6-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
67.0 kDa (monomer). 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
70-80 kDa, reducing conditions
Publications
Read Publications using 6055-LR 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 with trehalose..
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 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 LRRC32/GARP Protein, CF
D11S833E
D11S833Eleucine-rich repeat-containing protein 32
GARP
GARPGarpin
Garpin
Glycoprotein A repetitions predominantgarpin
leucine rich repeat containing 32
LRRC32
Background
Leucine-rich repeat protein 32 (LRRC32), also known as GARP (glycoprotein A repetitions predominant), is an 80 kDa type I transmembrane glycoprotein (1). Mature human LRRC32 consists of a 608 amino acid (aa) extracellular domain (ECD) that contains 22 leucine‑rich repeats, a 21 aa transmembrane segment, and a 14 aa cytoplasmic domain (2, 3). Within the ECD, human LRRC32 shares approximately 80% aa sequence identity with mouse and rat LRRC32. LRRC32 is widely expressed during embryogenesis and on adult platelets (4, 5). Human LRRC32 is identified as a lineage specific key receptor for human T cells. It is selectively expressed on activated FOXP3+ regulatory T cells (Treg) (6-10). LRRC32 expression promotes the acquisition of a Treg phenotype including reduced cellular proliferation, reduced cytokine secretion, and the capacity to suppress the proliferation of naïve T cells (6 ‑ 8). LRRC32 binds directly to the TGF-beta latency associated peptide (LAP) and tethers latent TGF-beta on the surface of activated Treg cells (9, 10). The presentation of TGF-beta on Tregs contributes to their ability to suppress naïve T cell proliferation (11).
Battaglia, M. and M.G. Roncarolo (2009) Eur. J. Immunol. 39:3296.
Ollendorff, V. et al. (1994) Cell Growth Differ. 5:213.
Bella, J. et al. (2008) Cell Mol Life Sci. 65:2307.
Roubin, R. et al. (1996) Int. J. Dev. Biol. 40:545.
Macaulay, I.C. et al. (2007) Blood 109:3260.
Wang, R. et al. (2008) PloS ONE 3:e2705.
Wang, R. et al. (2009) Proc. Natl. Acad. Sci. 106:13439.
Probst-Kepper, M. et al. (2009) J. Cell. Mol. Med. 13:3343.
Tran, D.Q. et al. (2009) Proc. Natl. Acad. Sci. 106:13445.
Stockis, J. et al. (2009) Eur. J. Immunol. 39:3315.
Vignali, D.A. et al. (2008) Nat. Rev. Immunol. 8:523.
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