Key features and details
- Expression system: Native
Product nameNative Human Fibronectin protein
See all Fibronectin proteins and peptides
Protein lengthFull length protein
Additional sequence informationPrepared from frozen human plasma by immunodepletion with immobilized affinity purified antibodies to human fibronectin.
Our Abpromise guarantee covers the use of ab229795 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Store at -80°C.
- 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.
ab229795 has not yet been referenced specifically in any publications.