Fibronectin Protein, Human, Recombinant (His Tag)
Product Specifications
Background
Fibronectin (FN) is a glycoprotein component of the extracellular matrix of the extracellular matrix (ECM) with roles in embryogenesis, development, and wound healing. More recently, FN has emerged as player in platelet thrombus formation and diseases associated with thrombosis including vascular remodeling, atherosclerosis, and cardiac repair following a myocardial infarct. Each monomer of FN consists of three types of homologous repeating units, that is 12 type I repeats, two type II repeats and 15-17 type III repeats. The occurrence of multiple isoforms results from alternative mRNA splicing of the ED-A, ED-B and III-CS regions, and subsequent post-translational modification. As an ECM component and one of the primary cell adhesion molecules, Fibronectin can be a ligand for fibrin, heparin, chondroitin sulfate, collagen/gelatin, as well as many integrin receptors through which FN mediates the variety of cellular signaling pathways. The study of solid human tumors showed among the early signs of malignant transformation the fragmentation of pericellular FN, concommitent with the increase of its production by the peritumoral stroma. These results should encourage further investigations concerning the potential importance of Fn production and breakdown during cancer progression. FN1 expression has been described to increase significantly from the morula towards the early blastocyst stage, suggesting that FN1 may also be involved in early blastocyst formation. The fragment 2 of FN comprises the first 7 FN type III repeats and is suggested to be important for self association during fibril growth via the key module III2.
Synonyms
CIG Protein, Human; ED-B Protein, Human; FINC Protein, Human; FN Protein, Human; FNZ Protein, Human; GFND Protein, Human; GFND2 Protein, Human; LETS Protein, Human; MSF Protein, Human
Gene Name
Fibronectin 1
Expression System
HEK293 Cells
Tag
C-His
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
Purity
> 95 % as determined by SDS-PAGE.
Activity
At Leading Biology, the biological activity of a recombinant protein is routinely measured using a bioassay, e.g. chemotaxis or cell proliferation assay, enzyme assay, or a functional ELISA. When a recombinant protein is an enzyme, specific activity is derived from an enzymatic assay. Each enzyme is tested for potency by cleavage of a substrate. We are in the process of updating the biological activity data. If you have any questions regarding this update, please feel free to contact our technical support team.
Form
Lyophilized
Buffer
Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Function
Biomarker Proteins
Molecular Weight
The recombinant human FN1 consists of 101 amino acids and predicts a molecular mass of 11.3 kDa.
Storage Conditions
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.
Product Datasheet
http://www.leading-biology.com/en/fastadmin/public/data/datasheet/S_Protein_datasheet/PH50629M2.pdf
Symbol
FN1
Species
Human
Protein ID
NP_997647.1
Overview
A DNA sequence encoding the human FN1 (NP_997647.1) (Asn1722-Thr1811) was expressed with a polyhistidine tag at the C-terminus.
AA Sequence
Asn1722-Thr1811
Protein ID Link
https://www.ncbi.nlm.nih.gov/protein/NP_997647.1
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