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GITR (mouse):Fc (human), (recombinant)

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Alternative Name	AITR, TNFRSF 18, Glucocorticoid-induced TNFR-related protein, Activation-inducible TNFR family receptor
Concentration	1mg/ml after reconstitution.
Endotoxin Content	<0.1EU/µg purified protein (LAL test; Bio Whittaker).
Formulation	Lyophilized. Contains PBS.
MW	~45kDa (SDS-PAGE).
Purity	≥95% (SDS-PAGE)
Reconstitution	Reconstitute with 50µl sterile water. Further dilutions should be made with medium containing 5% fetal calf serum or a carrier protein.
Source	Produced in HEK 293 cells. The cysteine-rich region of mouse GITR (aa 20-152) is fused to the Fc portion of human IgG1.
Specificity	Binds mouse GITRL.
UniProt ID	O35714

Use/Stability	Stable for at least 6 months after receipt when stored at -20°C.
Handling	Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -20°C.
Long Term Storage	-20°C
Shipping	Blue Ice

Regulatory Status	RUO – Research Use Only

Identification of glucocorticoid-induced TNF receptor-related protein ligand on keratinocytes: ligation by GITR induces keratinocyte chemokine production and augments T-cell proliferation: A.M. Byrne, et al.; J. Invest. Dermatol. 129, 2784 (2009), Abstract — Full Text
Proinflammatory role of glucocorticoid-induced TNF receptor-related gene in acute lung inflammation: S. Cuzzocrea, et al.; J. Immunol. 177, 631 (2006), Abstract
Soluble glucocorticoid-induced tumor necrosis factor receptor (sGITR) stimulates osteoclast differentiation in response to receptor activator of NF-kappaB ligand (RANKL) in osteoclast cells: H.H. Shin, et al.; Bone 36, 832 (2005), Abstract
Soluble glucocorticoid-induced TNF receptor (sGITR) induces inflammation in mice: H. H. Shin, et al.; Exp. Mol. Med. 35, 358 (2003), Abstract — Full Text
Mouse glucocorticoid-induced tumor necrosis factor receptor ligand is costimulatory for T cells: M. Tone, et al.; PNAS 100, 15059 (2003), Abstract

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Negative control for Fc chimeric proteins

Alternative Name	Thy-1 (RLE mutant)
Purity	≥90% (SDS-PAGE)
Source	Produced in HEK 293 cells. The extracellular domain of mutated hThy-1, hThy-1 (RLE) (aa 20-130), is fused to the Fc portion of human IgG1. The integrin binding sequence RLD of hThy-1 has been changed to RLE abolishing the binding of integrins.

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