Product Details
| Alternative Name: | Leucine-rich repeat-containing protein 32, GARP, Garpin, Glycoprotein A repetitions predominant |
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| MW: | 104kDa (observed) |
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| Source: | Produced in CHO cells. Human LRRC32 (aa 20-627) is fused to the Fc portion of human IgG1. |
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| UniProt ID: | Q14392 |
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| Concentration: | 1mg/ml (after reconstitution). |
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| Formulation: | Lyophilized. Contains PBS. |
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| Purity: | ≥90% (SDS-PAGE) |
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| Endotoxin Content: | <0.1EU/µg purified protein (LAL test; Cape Cod Associates). |
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| Reconstitution: | Reconstitute with 50µl sterile water. Further dilutions should be made with medium containing 5% fetal calf serum or a carrier protein. |
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| Shipping: | Blue Ice |
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| Long Term Storage: | -20°C |
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| Use/Stability: | Stable for at least 6 months after receipt when stored at -20°C. |
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| Handling: | Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -20°C. |
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| Scientific Background: | LRRC32 (leucine rich repeat containing 32; also known as GARP or Garpin; Glycoprotein A repetitions predominant) is a glycoprotein expressed on the cell surface of megakaryocytes, platelets and activated regulatory T (Treg) cells. |
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| Regulatory Status: | RUO - Research Use Only |
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Western Blot analysis: Lane 1: MW Marker, Lane 2: 100ng LRRC32 (human):Fc (human), (recombinant) probed with LRRC32 mAb (Prod. no. ALX-804-867).
SDS-PAGE analysis: Lane 1: MW Marker, Lane 2: 2µg LRRC32 (human):Fc (human), (recombinant).
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General Literature References
GARP (LRRC32) is essential for the surface expression of latent TGF-beta on platelets and activated FOXP3+ regulatory T cells: D.Q. Tran et al.; PNAS
106, 13445 (2009),
Abstract;
Membrane protein GARP is a receptor for latent TGF-beta on the surface of activated human Treg: J. Stock et al.; Eur. J. Immunol.
39, 3315 (2009),
Abstract;
Identification of a regulatory T cell specific cell surface molecule that mediates suppressive signals and induces Foxp3 expression: R. Wang, et al.; PLoS ONE
3, e2705 (2008),
Abstract;
Full Text
Comparative gene expression profiling of in vitro differentiated megakaryocytes and erythroblasts identifies novel activatory and inhibitory platelet membrane proteins: I.C. Macaulay, et al.; Blood
109, 3260 (2007),
Abstract;
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