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Your Position: Home > Protein > Fibronectin > FIN-H5113

Recombinant Fibronectin fragment, premium grade

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  • Synonym
    Fibronectin,FN1,CIG,ED-B,FINC,FN,FNZ,GFND,GFND2,LETS,MSF
  • Source
    Fibronectin fragment, premium grade(FIN-H5113) is expressed from E. coli cells. It contains AA Pro 1361 - Ser 1637 & Ala 1812 - Thr 2107 (Accession # P02751-15).
    Predicted N-terminus: Met
    It is produced under our rigorous quality control system that incorporates a comprehensive set of tests including sterility and endotoxin tests. Product performance is carefully validated and tested for compatibility for cell culture use or any other applications in the early preclinical stage. When ready to transition into later clinical phases, we also offer a custom GMP protein service that tailors to your needs. We will work with you to customize and develop a GMP-grade product in accordance with your requests that also meets the requirements for raw and ancillary materials use in cell manufacturing of cell-based therapies.
  • Molecular Characterization
    Fibronectin Structure

    This protein carries no "tag".

    The protein has a calculated MW of 62.6 kDa . The protein migrates as 55-60 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

  • Endotoxin
    Less than 0.01 EU per μg by the LAL method.
  • Sterility
    Negative
  • Mycoplasma
    Negative.
  • Purity

    >90% as determined by SDS-PAGE.

    >95% as determined by SEC-MALS.

  • Formulation

    Supplied as 0.2 μm filtered solution in 12.5 mM Sodium citrate, pH6.2 with Sucrose as protectant.

    Contact us for customized product form or formulation.

  • Shipping

    This product is supplied and shipped with dry ice, please inquire the shipping cost.

  • Storage

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. The product MUST be stored at -70°C or lower upon receipt;
    2. -70°C for 24 months under sterile conditions.
SDS-PAGE
Fibronectin SDS-PAGE

Fibronectin fragment, premium grade 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
Fibronectin MALS images

The purity of Fibronectin fragment, premium grade (Cat. No. FIN-H5113) is more than 95% and the molecular weight of this protein is around 55-70 kDa verified by SEC-MALS.

Bioactivity-FACS
 Fibronectin FACS

2e5 of Jurkat cells were transfected with pLenti-CMV-EGFP-puro-Amp for 48hrs in the presence or absence of Fibronectin fragment, premium grade (Cat. No. FIN-H5113)-Coated. The fluorescence of GFP were detected with FACS, Alexa Fluor 488 signal was used to evaluate the expression of GFP+ Jurkat cells (Routinely tested). Please click the button for more detailed protocols.

Bioactivity-ELISA
 Fibronectin ELISA

Immobilized Fibronectin fragment, premium grade (Cat. No. FIN-H5113) at 5 μg/mL (100 μL/well) can bind Biotinylated Human ITGA4&ITGB1 Heterodimer Protein, His,Avitag&Tag Free (Cat. No. IT1-H82W1) with a linear range of 2-78 ng/mL (QC tested).

  • Background
    Fibronectin (Fn) is a glycoprotein whose size ranges from 230 to 270 kDa and usually exists as a dimer, covalently linked by a pair of disulfide bonds at the C-termini. Each monomer consists of three repeating units: 12 Type I, 2 Type II, and 15–17 Type III domains which combined account for 90% of the FN sequence. The extracellular matrix (ECM) plays a key role as both structural scaffold and regulator of cell signal transduction in tissues. Fibronectin is one of the major ECM proteins in the trabecular meshwork (TM). It is found in the sheath material surrounding the elastin tendons that enter the TM from the ciliary muscle within the ciliary body. In times of ECM assembly and turnover, cells upregulate assembly of the ECM protein, FN. FN is assembled by cells into viscoelastic fibrils that can bind upward of 40 distinct growth factors and cytokines. These fibrils play a key role in assembling a provisional ECM during embryonic development and wound healing. Fibril assembly is also often upregulated during disease states, including cancer and fibrotic diseases.
  • Clinical and Translational Updates

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