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Your Position: Home > All Other Proteins > LRRC32 & TGF-beta 1 > GA1-C52W7

Cynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag Free

  • Synonym
    LRRC32 & TGF-beta 1,LRRC32&TGFB1
  • Source
    Cynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag Free (GA1-C52W7) is expressed from human 293 cells (HEK293). It contains AA Ala 18 -Asn 627 (LRRC32) & Leu 30 - Ser 390 (TGF-beta 1) (Accession # A0A2K5X2X9-1(LRRC32) & A0A2K5TJB2-1(TGF-beta 1)).
    Predicted N-terminus: Ala 18 (LRRC32) & Leu 30 (TGF-beta 1)
  • Molecular Characterization
    Online(Ala 18 -Asn 627 (LRRC32) & Leu 30 - Ser 390 (TGF-beta 1)) A0A2K5X2X9-1 (LRRC32) & A0A2K5TJB2-1 (TGF-beta 1)

    Cynomolgus LRRC32&TGFB1 Heterotrimer protein, His Tag&Tag Free (the molar ratio of LRRC32 & TGF-beta 1 equals 1:2) is produced by co-expression of LRRC32 and TGF-beta 1, which has a calculated MW of 68.1 kDa (LRRC32), 28.5 (LAP) and 12.8 kDa (mature TGF-beta 1) respectively. LRRC32 is fused with a polyhistidine tag at the C-terminus and TGF-beta 1 contains no tag. The reducing (R) Heterotrimer protein migrates as 70 kDa (LRRC32), 37-43 kDa (LAP) and 13 kDa (mature TGF-beta 1) due to glycosylation respectively.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >90% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
Cynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag Free (Cat. No. GA1-C52W7) SDS-PAGE gel

Cynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag Free on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.

Bioactivity-ELISA
Cynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag FreeCynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag Free (Cat. No. GA1-C52W7) ELISA bioactivity

Immobilized Cynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag Free (Cat. No. GA1-C52W7) at 1 μg/mL (100 μL/well) can bind Biotinylated Human ITGAV&ITGB6 Heterodimer Protein, His,Avitag&Tag Free (Cat. No. IT6-H82E4) with a linear range of 1-39 ng/mL (QC tested).

Cynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag FreeCynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag Free (Cat. No. GA1-C52W7) ELISA bioactivity

Immobilized Cynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag Free (Cat. No. GA1-C52W7) at 1 μg/mL (100 μL/well) can bind Mouse IgG1:Purified anti-human LAP(TGF-β1) (Cat. No. GA1-C52W7) with a linear range of 0.5-8 ng/mL (Routinely tested).

Bioactivity-SPR
Human_FcRn_Heterodimer_Protein_SPR

Anti-LRRC32 antibody captured on Protein A Chip can bind Cynomolgus LRRC32&TGF-beta 1 Heterotrimer Protein, His Tag&Tag Free (Cat. No. GA1-C52W7) with an affinity constant of 51.9 pM as determined in SPR assay (Biacore 8K) (Routinely tested).

  • Background
    GARP (LRRC32) is a transmembrane protein that binds latent-TGF-β1 and tethers it on the Treg surface. and has been proved to promote the activation and secretion of transforming growth factor β (TGF-β). The expression of GARP is highly on the surface activated Tregs and increases the suppressive function of Tregs. Additionally, GARP can bind to latent transforming growth factor β (TGF-β), thus promoting secretion and activation of TGF-β. TGF-β plays a critical rule for homeostasis and function of Tregs. Notably, it has been also observed that fibroblasts and endothelial cell lines that express GARP/latent TGF-β1 complexes do not activate TGF-β1. However, it cannot be excluded that specific stimuli are required to trigger TGF-β1 activation from complexes on the surface of these cell types.
  • Clinical and Translational Updates
      
  • Please contact us via TechSupport@acrobiosystems.com if you have any question on this product.

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