Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Tags: His-T7 tag N-Terminus
- Suitable for: SDS-PAGE, Functional Studies
Product nameRecombinant Human Fibronectin type III EDB protein
See all Fibronectin proteins and peptides
Purity> 90 % SDS-PAGE.
ab209886 was sterile-filtered.
Expression systemEscherichia coli
Protein lengthProtein fragment
SequenceMASMTGGQQMGRGHHHHHHGNLYFQGGEFNVSVYTVKDDKESVPISDTII PEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFED FVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDL RFTNIGPDTMRVT
Predicted molecular weight18 kDa including tags
Amino acids1244 to 1377
TagsHis-T7 tag N-Terminus
Additional sequence informationFN-III EDB domain constructed by fully synthetic gene synthesis with codon optimization and expressed with an N-terminal 29aa T7-His-TEV cleavage site.
DescriptionRecombinant Human Fibronectin protein
Our Abpromise guarantee covers the use of ab209886 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ab209886 was expressed in E.coli as inclusion bodies. The final product was refolded using a unique “temperature shift inclusion body refolding” technology and chromatographically purified.
Extracellular matrix protein fibronectin (FN) plays an important role in cell adhesion. FN contains FN type I, II and III domains. The FN III repeat is generally about 90 amino acid long and to be composed of seven b-strands, forming two antiparallel b-sheets. In the C-terminal of human fibronectin region, there are 16 FN-III repeat domains. FN III domain derived proteins have been demonstrated to bind various proteins with high affinity. The alternatively-spliced extra-domain B (EDB) of fibronectin represents one of the best characterized markers of angiogenesis. This domain of 91-aminoacids is completely identical between mouse and man, is virtually absent in normal adult tissues (exception made for the endometrium in the proliferative phase and some vessels of the ovaries), but is strongly expressed in most aggressive solid cancer types, with a prominent vascular and/or stromal pattern of expression.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at -80°C.
Constituent: 0.32% Tris HCl
Proprietary formulation of NaCl, KCl, EDTA, Arginine, DTT and Glycerol.
- Cold insoluble globulin
- Cold-insoluble globulin
FunctionFibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts.
Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.
Tissue specificityPlasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine.
Involvement in diseaseGlomerulopathy with fibronectin deposits 2
Sequence similaritiesContains 12 fibronectin type-I domains.
Contains 2 fibronectin type-II domains.
Contains 16 fibronectin type-III domains.
Developmental stageUgl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age.
It is not known whether both or only one of Thr-2064 and Thr-2065 are/is glycosylated.
Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers).
Phosphorylated by FAM20C in the extracellular medium.
Proteolytic processing produces the C-terminal NC1 peptide, anastellin.
Cellular localizationSecreted, extracellular space, extracellular matrix.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab209886 has not yet been referenced specifically in any publications.