Human LRRC32&TGF-beta 1 Heterotrimer protein, His Tag&Tag Free, low endotoxin (MALS verified)

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Cat. No. / Size
Price
Qty
GA1-H52W9-100ug
$360.00
GA1-H52W9-1mg (500ug X 2)
$2615.00
ETA of in-stock products:2 business days

Product Details

  • Synonyms

    LRRC32 & TGF-beta 1, LRRC32&TGFB1

  • Source

    Human LRRC32&TGFB1 Heterotrimer protein, His Tag&Tag Free (GA1-H52W9) is expressed from human 293 cells (HEK293). It contains AA His 20 - Asn 627 (LRRC32) & Leu 30 - Ser 390 (TGF-beta 1) (Accession # Q14392-1 (LRRC32) & P01137-1 (TGF-beta1)).

    Predicted N-terminus: Leu 30

    Request for sequence
  • Molecular Characterization

    Human 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 68.0 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), 38-45 kDa (LAP) and 14 kDa (mature TGF-beta 1) when calibrated against Star Ribbon Pre-stained Protein Marker due to glycosylation respectively.

  • Endotoxin

    Less than 0.01 EU per μg by the LAL method / rFC method.

  • Purity

    >90% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

    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.
  • ACRO Quality Management System

    1. QMS(ISO, GMP)
    2. Quality Advantages
    3. Quality Control Process

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Performance Data

  • SDS-PAGE

    LRRC32 & TGF-beta 1 SDS-PAGE

    Human LRRC32&TGFB1 Heterotrimer protein, His Tag&Tag Free on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90% (With Star Ribbon Pre-stained Protein Marker).

  • SEC-MALS

    LRRC32 & TGF-beta 1 SEC-MALS

    The purity of Human LRRC32&TGFB1 Heterotrimer protein, His Tag&Tag Free (Cat. No. GA1-H52W9) is more than 85% and the molecular weight of this protein is around 135-180 kDa verified by SEC-MALS.

    Report
  • Bioactivity-ELISA

     LRRC32 & TGF-beta 1 ELISA

    Immobilized Human LRRC32&TGFB1 Heterotrimer protein, His Tag&Tag Free (Cat. No. GA1-H52W9) 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 2-39 ng/mL (Routinely tested).

    Protocol
  •  LRRC32 & TGF-beta 1 ELISA

    Immobilized Human LRRC32&TGFB1 Heterotrimer protein, His Tag&Tag Free (Cat. No. GA1-H52W9) at 1 μg/mL (100 μL/well) can bind Biotinylated Human ITGAV&ITGB8 Heterodimer Protein, His,Avitag&Tag Free (Cat. No. IT8-H82W5) with a linear range of 0.002-0.313 μg/mL (Routinely tested).

    Protocol

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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.

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