Recombinant Human Fibronectin (FN1) Protein (His)

Name: Recombinant Human Fibronectin (FN1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01924P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Cytokines, Recombinant proteins

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Product Overview

Description	Recombinant Human Fibronectin (FN1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P02751
Target Symbol	FN1
Synonyms	Cold-insoluble globulin (CIG)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	His-tag
Target Protein Sequence	TASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPR
Expression Range	732-911aa
Protein Length	Partial of the full length of 723-911AA
Mol. Weight	23.6 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Fibronectins 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.; 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.
Subcellular Location	Secreted, extracellular space, extracellular matrix.
Database References	HGNC: 3778 OMIM: 135600 KEGG: hsa:2335 UniGene: Hs.203717
Associated Diseases	Glomerulopathy with fibronectin deposits 2 (GFND2)
Tissue Specificity	Expressed in the inner limiting membrane and around blood vessels in the retina (at protein level). Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and ot

Gene Functions References

Evidence has been presented for FN modification by inflammatory oxidants, and particularly myeloperoxidase (MPO)-derived species including hypochlorous acid (HOCl). Studies using primary human coronary artery smooth muscle cells show that exposure to HOCl-modified FN, results in decreased adherence, increased proliferation and altered expression of genes involved in extracellular matrix synthesis and remodelling. PMID: 30237127
Depletion of FN1 by siRNA knockdown markedly reduced the invasive capacity of prostate cancer cells in vitro. PMID: 29391407
Human IL-7 binds more strongly to stretched than to relaxed Fibronectin. PMID: 28845674
TGFB1-mediated PI3K/Akt and p38 MAP kinase dependent alternative splicing of fibronectin extra domain A in human podocyte culture has been reported. PMID: 29729706
The findings of this study provide evidence highlighting the prominent role played by FN1 in stimulating glioma growth, invasion, and survival through the activation of the PI3K/AKT signaling pathway. PMID: 30048971
The simultaneous delivery of multiple proinflammatory payloads to the cancer site conferred protective immunity against subsequent tumor challenges. A fully human homolog of IL2-F8-TNF(mut), which retained selectivity similar to its murine counterpart when tested on human material, may open new clinical applications for the immunotherapy of cancer. PMID: 28716814
Under the same condition, p53 protein expression, but not mRNA expression, was reversed by MG132. Taken together, our data demonstrate that the level of FN expression is associated with the status and expression of p53 in breast cancer cells PMID: 28765903
Our study thus demonstrates the dual roles of PTHrP on TGF-b1 signaling and FN up-regulation for the first time in glomerular mesangial cells . These data also provided new insights to guide development of therapy for diabetic kidney disease PMID: 28954822
data suggest that miR-200b regulates EMT of chemo-resistant breast cancer cells by targeting FN1. miR-200b-based therapy may be an effective strategy in treating advanced breast cancer patients. PMID: 28972876
Identification of novel integrin-binding domain mutations in FN1 in patients with glomerulopathy with fibronectin deposits. PMID: 27056061
Fibronectin fragments (FNFr) function as matrikines driving the chemotactic affinity of prostate cancer cells via the alpha5beta1 integrin. PMID: 27715399
Fn with its inactive compact structure requires unfolding to assemble into active fibrils. Shear stress could induce conformational changes of plasma Fn. PMID: 29470988
B. burgdorferi does not primarily target insoluble matrix Fn deposited on endothelial surfaces but, instead, recruits and induces polymerization of soluble plasma Fn (pFn), an abundant protein in blood plasma that is normally soluble and nonadhesive. PMID: 28396443
miR1271 inhibited glioma cell growth by targeting FN1, and a low level of miR1271 in glioma tumor tissues was associated with lower survival rates in patients with glioma. PMID: 28535003
There is a significant association between a positive fetal fibronectin result and underlying inflammatory pathology of the placenta, even more so than the recognized relationship with short cervical length. PMID: 28535404
The article focuses on summarizing the many binding partners for fibronectin such as extracellular matrix proteins, growth factors, and synthetic binding partners with a particular interest in binding partners whose adhesiveness is impacted by the molecular conformation of the fibronectin fibers. (Review) PMID: 27496349
FN1 fibrils regulate TGFB1-induced epithelial-mesenchymal transition. PMID: 28109697
Breast cancer cells alter the dynamics of stromal fibronectin-collagen interactions. PMID: 27503584
This study suggested that high a1-antitrypsin (AAT)expression might be a negative prognostic marker for lung adenocarcinoma. AAT promoted lung adenocarcinoma metastasis, whose functional target may be fibronectin . Our findings provide new insight into the mechanisms of lung adenocarcinoma metastasis PMID: 28440399
Data show the expression of ED-B fibronectin was much higher in mesenchymal than prostate cancer cells even after the epithelial to mesenchymal transition. Epithelial to mesenchymal transition is a key step for tumor progression contributing to the metastatic spread. Therefore, circulating cancer cells could seed into the metastatic niche taking advantage from the ED-B fibronectin that secrete their own. PMID: 27902486
Thrombomodulin (TM) promotes angiogenesis by enhancing cell adhesion, migration, and FAK activation through interaction with fibronectin. PMID: 27602495
thyroid nodule stiffness is correlated with fibrosis and expression of Gal-3 and FN-1 PMID: 27809694
EGF and TNFalpha cooperatively promoted the motility of HCC cells mainly through NF-kappaB/p65 mediated synergistic induction of FN in vitro. These findings highlight the crosstalk between EGF and TNFalpha in promoting HCC, and provide potential targets for HCC prevention and treatment. PMID: 28844984
analysis of FN in breast cancer reveals its role and diagnostic potential PMID: 27250024
RT-PCR together with Sanger sequencing verified the presence of the FN1-ALK fusion transcripts PMID: 27469327
Fibronectin is readily modified by ONOOH at low (physiologically-relevant) molar ratios of oxidant to protein. PMID: 27396946
The 45 kDa gelatin-binding domain of fibronectin is responsible for the binding to TGM2. PMID: 27394141
Proteomics study showed a strong association of FN1, A2M, C4BPA and CFB in molecular subtypes of breast cancer. The findings also revealed the altered level expressions of these selected proteins could classify BC subtypes through plasma and tissue based expression analysis PMID: 27498393
FN1/CCL2 levels are elevated in the bronchoalveolar lavage fluid from pulmonary sarcoidosis patients. PMID: 27259755
Cancer-associated fibroblasts organize the fibronectin matrix and promote directional prostate cancer cell migration. PMID: 29021221
FN1 mutations that cause defective fibronectin secretion are found in SMD. PMID: 29100092
FN1 overexpression is an important determinant of thyroid cancer aggressiveness. PMID: 27173027
Thyroid hormone T3 induces fibronectin and HIF-1alpha synthesis via PI3K/AKT signaling pathway. PMID: 28974422
Mutations in FN are associated with glomerulopathy, but when we studied mutant proteins, the single-nucleotide mutations had only minor effects on conformation and matrix assembly. The mutations may destabilize their FNIII domains or generate dimers of dimers by disulfide cross-linking. PMID: 28745050
Fibronectin and Hepatocyte Growth Factor were shown to be produced by lung fibroblasts and, furthermore, to enhance malignant pleural mesothelioma cell migration and invasion PMID: 28476806
Study identifies four likely Tourette disorder risk genes with multiple de novo damaging variants in unrelated probands: WWC1 (WW and C2 domain containing 1), CELSR3 (Cadherin EGF LAG seven-pass G-type receptor 3), NIPBL (Nipped-B-like), and FN1 (fibronectin 1). PMID: 28472652
fibrillar fibronectin on this polymer, but not a globular conformation obtained on control polymers, promotes synergistic presentation of integrin-binding sites and bound bone morphogenetic protein 2 (BMP-2), which enhances mesenchymal stem cell osteogenesis in vitro and drives full regeneration of a nonhealing bone defect in vivo at low GF concentrations. PMID: 27574702
Fn plays a critical role in inflammasome-activated cells by amplifying caspase-1 activation and inducing inflammatory cell death. PMID: 27870323
If the expression of Capon is decreased, myeloma cells are adhered to fibronectin or bone marrow stromal cells (bone marrow mesenchymal stem cells). In addition, the sensitivity of the cell line to chemotherapeutic agents was reduced after silencing Capon in the myeloma cell line which was adhered to bone marrow mesenchymal stem cells. PMID: 28671047
Protease sensitivity resulting from mutations in the Fn-binding sequence could lead to degradation of type I collagen, early embryonic lethality PMID: 27799304
C-terminal truncation of transglutaminase 2 (TG2) reduces binding to the small intestinal extracellular matrix (ECM) despite retained fibronectin (FN)-binding capacity. PMID: 27685605
analysis of novel functions for two fibronectin isoforms and the mediating receptors in osteoblast differentiation PMID: 28325836
In vitro binding assays with purified components reveal that Tie-integrin recognition is direct, and further demonstrate that the receptor binding domain of the Tie2 ligand Ang-1, but not the receptor binding domain of Ang-2, can independently associate with a5b1 or aVb3. cooperative Tie/integrin interactions selectively stimulate ERK/MAPK signaling in the presence of both Ang-1 and fibronectin PMID: 27695111
Results directly implicate the heparin-binding sequence of the first type III repeat of fibrillar fibronectin (FNIII1) in realignment of stress fibers in HUVECs and, importantly, show that the matricryptic heparin-binding RWRPK sequence located in FNIII1 is required for the response. PMID: 27521419
TGFbeta elevated the expression of CamK IIbeta and CamK IIdelta, while siRNA silencing of those two subtypes significantly reduced TGFbeta-mediated expression of collagen A1 and fibronectin 1. PMID: 28130256
Findings suggest that the up-regulated level of EDA+ FN is associated with liver damage in nonalcoholic fatty liver disease. PMID: 28397039
In vitro binding studies support a previously unreported two-state "catch-clamp" mechanism of Fn binding by CshA, in which the disordered N-terminal domain of CshA acts to "catch" Fn, via formation of a rapidly assembled but also readily dissociable pre-complex, enabling its neighboring ligand binding domain to tightly clamp the two polypeptides together. PMID: 27920201
These data add new evidence that thermodynamic stability correlates primarily with unfolding rate rather than folding rate. The study also has implications for the question of whether opening of FNIII domains contributes to the stretching of fibronectin matrix fibrils. PMID: 27909052
A positive fFN was associate with preterm birth <32 weeks (15.6% versus 4.2%, p = 0.043), <35 weeks (37.5% versus 11.1%, p = 0.002), <37 weeks (65.6% versus 20.8%, p < 0.001), and earlier gestational ages at delivery (35.2 +/- 3.9 versus 37.4 +/- 2.9, p = 0.001). PMID: 26782923
FN1 plays a role in the development of cisplatin resistance in non-small cell lung cancer (NSCLC), possibly by modulation of beta-catenin signaling through interaction with integrin-beta1 in NSCLC. PMID: 27207836

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.