Western blot analysis of extracts from various human primary cells and cell lines using GARP/LRRC32 (E2L6B) Rabbit mAb (upper) and β-Actin (D6A8) Rabbit mAb #8457 (lower).
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
For western blots, incubate membrane with diluted primary antibody in 5% w/v BSA, 1X TBS, 0.1% Tween® 20 at 4°C with gentle shaking, overnight.
NOTE: Please refer to primary antibody product webpage for recommended antibody dilution.
From sample preparation to detection, the reagents you need for your Western Blot are now in one convenient kit: #12957 Western Blotting Application Solutions Kit
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
Load 20 µl onto SDS-PAGE gel (10 cm x 10 cm).
NOTE: Volumes are for 10 cm x 10 cm (100 cm2) of membrane; for different sized membranes, adjust volumes accordingly.
* Avoid repeated exposure to skin.
posted June 2005
revised June 2020
Protocol Id: 10
GARP/LRRC32 (E2L6B) Rabbit mAb recognizes endogenous levels of total GARP/LRRC32 protein. This antibody cross-reacts with an unidentified protein of 32 kDa in some cell extracts.
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala292 of human GARP/LRRC32 protein.
Leucine-rich repeat containing 32 (LRRC32), also known as glycoprotein A repetitions predominant (GARP), is a key regulator of the TGF-beta family (TGF-β1, TGF-β2, and TGF-β3), and is primarily expressed on the surface of mesenchymal stromal cells, hepatic stellate cells, platelets, and regulatory T cells (Tregs) (1). GARP/LRRC32 enhances the suppressive function of Tregs and decreases the expression of inflammatory cytokines, IL-2, and IFNγ (2,3). GARP/LRRC32 associates via disulfide bonds with the latency-associated peptide (LAP), the regulatory chain of TGF-β, to induce integrin-dependent activation of TGF-β and secretion (1, 3-5), thereby promoting Treg function and homeostasis. As a result, targeting GARP/LRRC32 in combination with other molecules for depleting Tregs or attenuating their suppressive activity represents an opportunity for cancer immunotherapy (6,7).
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