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Mouse Anti-FN1 Antibody (HFN 7.1) (CBMAB-1241CQ)

This product is a mouse antibody that recognizes FN1. The antibody HFN 7.1 can be used for immunoassay techniques such as: ELISA, Blocking, IF, WB.
See all FN1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
HFN 7.1
Antibody Isotype
IgG1
Application
ELISA, Blocking, IF, WB

Basic Information

Immunogen
Human fibronectin Purified from serum
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Supernatant
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
Between the PHSRN synergy and RGD sites (spans the connection between type III repeats 9 and 10)

Target

Full Name
Fibronectin 1
Introduction
This gene encodes fibronectin, a glycoprotein present in a soluble dimeric form in plasma, and in a dimeric or multimeric form at the cell surface and in extracellular matrix. The encoded preproprotein is proteolytically processed to generate the mature protein. Fibronectin is involved in cell adhesion and migration processes including embryogenesis, wound healing, blood coagulation, host defense, and metastasis. Diseases associated with FN1 include Glomerulopathy With Fibronectin Deposits 2 and Plasma Fibronectin Deficiency. Among its related pathways are Response to elevated platelet cytosolic Ca2+ and RET signaling.
Entrez Gene ID
2335
UniProt ID
P02751
Alternative Names
Fibronectin 1; Cold-Insoluble Globulin; Migration-Stimulating Factor; CIG; FN; GFND2; ED-B; FINC; GFND; LETS; FNZ; MSF
Function
Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (PubMed:3024962, PubMed:3900070, PubMed:3593230, PubMed:7989369).

Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (PubMed:3024962, PubMed:3900070, PubMed:3593230, PubMed:7989369).

Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity).

Participates in the regulation of type I collagen deposition by osteoblasts (By similarity).

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.
Biological Process
Acute-phase response Source: UniProtKB-KW
Angiogenesis Source: UniProtKB-KW
Biological process involved in interaction with symbiont Source: CAFA
Blood coagulation, fibrin clot formation Source: GO_Central
Calcium-independent cell-matrix adhesion Source: Ensembl
Cell adhesion Source: UniProtKB
Cell-matrix adhesion Source: GO_Central
Cell-substrate junction assembly Source: GO_Central
Endodermal cell differentiation Source: UniProtKB
Heart development Source: GO_Central
Integrin activation Source: UniProtKB
Integrin-mediated signaling pathway Source: BHF-UCL
Negative regulation of transforming growth factor beta production Source: UniProtKB
Nervous system development Source: GO_Central
Neural crest cell migration involved in autonomic nervous system development Source: MGI
Peptide cross-linking Source: BHF-UCL
Platelet aggregation Source: GO_Central
Positive regulation of axon extension Source: Ensembl
Positive regulation of cell population proliferation Source: UniProtKB
Positive regulation of fibroblast proliferation Source: UniProtKB
Positive regulation of gene expression Source: UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
Positive regulation of substrate-dependent cell migration, cell attachment to substrate Source: UniProtKB
Regulation of cell shape Source: UniProtKB-KW
Regulation of ERK1 and ERK2 cascade Source: UniProtKB
Regulation of protein phosphorylation Source: UniProtKB
Response to wounding Source: UniProtKB
Substrate adhesion-dependent cell spreading Source: BHF-UCL
Cellular Location
Extracellular matrix
Involvement in disease
Glomerulopathy with fibronectin deposits 2 (GFND2):
Genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.
Spondylometaphyseal dysplasia, corner fracture type (SMDCF):
An autosomal dominant form of spondylometaphyseal dysplasia, a group of short stature disorders distinguished by abnormalities in the vertebrae and the metaphyses of the tubular bones. SMDCF is characterized by flake-like, triangular, or curvilinear ossification centers at the edges of irregular metaphyses that simulate fractures. These corner fractures involve the distal tibia, the ulnar aspect of the distal radius, the proximal humerus, and the proximal femur. They represent irregular ossification at the growth plates and secondary ossification centers.
PTM
Sulfated.
It is not known whether both or only one of Thr-2155 and Thr-2156 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.
Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation.
Serotonylated on Gln residues by TGM2 in response to hypoxia.

Zhou, W. H., Du, W. D., Li, Y. F., Al-Aroomi, M. A., Yan, C., Wang, Y., ... & Sun, C. F. (2022). The overexpression of fibronectin 1 promotes cancer progression and associated with M2 macrophages polarization in head and neck squamous cell carcinoma patients. International Journal of General Medicine, 5027-5042.

Aladal, M., You, W., Huang, R., Huang, J., Deng, Z., Duan, L., ... & Sun, W. (2022). Insights into the implementation of Fibronectin 1 in the cartilage tissue engineering. Biomedicine & Pharmacotherapy, 148, 112782.

Bouvier, C., Nihous, H., & Macagno, N. (2022, February). Soft tissue tumours with FN1 (Fibronectin 1) fusion gene. In Annales de Pathologie.

Wang, Y., Zhao, M., & Zhang, Y. (2021). Identification of fibronectin 1 (FN1) and complement component 3 (C3) as immune infiltration-related biomarkers for diabetic nephropathy using integrated bioinformatic analysis. Bioengineered, 12(1), 5386-5401.

Bao, H., Huo, Q., Yuan, Q., & Xu, C. (2021). Fibronectin 1: a potential biomarker for ovarian cancer. Disease Markers, 2021, 1-11.

Sun, Y., Zhao, C., Ye, Y., Wang, Z., He, Y., Li, Y., & Mao, H. (2020). High expression of fibronectin 1 indicates poor prognosis in gastric cancer. Oncology Letters, 19(1), 93-102.

Ji, J., Chen, L., Zhuang, Y., Han, Y., Tang, W., & Xia, F. (2020). Fibronectin 1 inhibits the apoptosis of human trophoblasts by activating the PI3K/Akt signaling pathway. International Journal of Molecular Medicine, 46(5), 1908-1922.

Li, B., Shen, W., Peng, H., Li, Y., Chen, F., Zheng, L., ... & Jia, L. (2019). Fibronectin 1 promotes melanoma proliferation and metastasis by inhibiting apoptosis and regulating EMT. OncoTargets and therapy, 12, 3207.

Kun‐Peng, Z., Chun‐Lin, Z., Xiao‐Long, M., & Lei, Z. (2019). Fibronectin‐1 modulated by the long noncoding RNA OIP5‐AS1/miR‐200b‐3p axis contributes to doxorubicin resistance of osteosarcoma cells. Journal of Cellular Physiology, 234(5), 6927-6939.

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For research use only. Not intended for any clinical use.

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