Fibronectin, Human

Fibronectin, Human

• UNSPSC Description: Fibronectin is a glycoprotein located in the extracellular matrix that can bind to collagen, fibrin, heparin, DNA, and actin. Fibronectin is involved in cell adhesion, movement, conditioning, wound healing, and maintaining cell shape. Additionally, by binding to the LILRB4 receptor, Fibronectin can inhibit monocyte activation mediated by FCGR1A/CD64, thereby exerting immune regulatory effects. Human Fibronectin is a recombinant protein dimer complex with a full length of 573 amino acids (P1270-S1546 & A1721-T2016), expressed in E. coli and is untagged[1][2][3][4][5][6][7][8][9][10][11][12].
• Type: Recombinant Proteins
• Assay Protocol: https://www.medchemexpress.com/cytokines/fibronectin-protein-human.html
• Purity: 98.0
• Smiles: PTDLRFTNIG PDTMRVTWAP PPSIDLTNFL VRYSPVKNEE DVAELSISPS DNAVVLTNLL PGTEYVVSVS SVYEQHESTP LRGRQKTGLD SPTGIDFSDI TANSFTVHWI APRATITGYR IRHHPEHFSG RPREDRVPHS RNSITLTNLT PGTEYVVSIV ALNGREESPL LIGQQSTVSD VPRDLEVVAA TPTSLLISWD APAVTVRYYR ITYGETGGNS PVQEFTVPGS KSTATISGLK PGVDYTITVY AVTGRGDSPA SSKPISINYR TEIDKPS&AI PAPTDLKFTQ VTPTSLSAQW TPPNVQLTGY RVRVTPKEKT GPMKEINLAP DSSSVVVSGL MVATKYEVSV YALKDTLTSR PAQGVVTTLE NVSPPRRARV TDATETTITI SWRTKTETIT GFQVDAVPAN GQTPIQRTIK PDVRSYTITG LQPGTDYKIY LYTLNDNARS SPVVIDASTA IDAPSNLRFL ATTPNSLLVS WQPPRARITG YIIKYEKPGS PPREVVPRPR PGVTEATITG LEPGTEYTIY VIALKNNQKS EPLIGRKKTD ELPQLVTLPH PNLHGPEILD VPST
• Molecular Weight: Approximately 56-76 kDa due to the glycosylation.
• References & Citations: [1]Patten J, Wang K. Fibronectin in development and wound healing. Adv Drug Deliv Rev. 2021 Mar;170:353-368.|[2]Lenselink EA. Role of fibronectin in normal wound healing. Int Wound J. 2015 Jun;12(3):313-6. doi: 10.1111/iwj.12109. Epub 2013 Jun 7.|[3]Bielefeld K A, et al. Fibronectin and β-catenin act in a regulatory loop in dermal fibroblasts to modulate cutaneous healing[J]. Journal of Biological Chemistry, 2011, 286(31): 27687-27697.|[4]Shi F, et al. MT1-MMP regulates the turnover and endocytosis of extracellular matrix fibronectin[J]. Journal of cell science, 2011, 124(23): 4039-4050.|[5]Lefcort F, et al. Regulation of expression of fibronectin and its receptor, α5β1, during development and regeneration of peripheral nerve[J]. Development, 1992, 116(3): 767-782.|[6]Clark RA, et al. Blood vessel fibronectin increases in conjunction with endothelial cell proliferation and capillary ingrowth during wound healing. J Invest Dermatol. 1982 Nov;79(5):269-76.|[7]Oyama F, et al. Deregulation of alternative splicing of fibronectin pre-mRNA in malignant human liver tumors. J Biol Chem. 1989 Jun 25;264(18):10331-4.|[8]Yi M, Ruoslahti E. A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis. Proc Natl Acad Sci U S A. 2001 Jan 16;98(2):620-4.|[9]Quirós J, et al. Beneficial effect of fibronectin administration on chronic nephritis in rats. Arthritis Rheum. 1990 May;33(5):685-92.|[10]Su MT, et al. Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronectin ameliorates autoimmune disease in BXSB/Yaa mice. Int Immunol. 2021 Jul 23;33(8):447-458.|[11]Sottile J, et al. Fibronectin matrix assembly enhances adhesion-dependent cell growth. J Cell Sci. 1998 Oct;111 ( Pt 19):2933-43.|[12]Su MT, et al. Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronectin ameliorates autoimmune disease in BXSB/Yaa mice. Int Immunol. 2021 Jul 23;33(8):447-458.
• Shipping Conditions: Blue Ice
• Storage Conditions: Stored at -20°C for 2 years