Product: Fibronectin Antibody
Catalog: AF5335
Description: Rabbit polyclonal antibody to Fibronectin
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Sheep, Rabbit
Mol.Wt.: 263 kDa, 200 kDa; 272kD(Calculated).
Uniprot: P02751
RRID: AB_2837820

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(92%), Bovine(100%), Sheep(92%), Rabbit(100%)
Clonality:
Polyclonal
Specificity:
Fibronectin Antibody detects endogenous levels of total Fibronectin.
RRID:
AB_2837820
Cite Format: Affinity Biosciences Cat# AF5335, RRID:AB_2837820.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

CIG; Cold insoluble globulin; Cold-insoluble globulin; DKFZp686F10164; DKFZp686H0342; DKFZp686I1370; DKFZp686O13149; ED B; Fibronectin 1; FINC; FINC_HUMAN; FN; FN1; FNZ; GFND; GFND2; LETS; Migration stimulating factor; MSF; Ugl-Y3;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P02751 FINC_HUMAN:

Expressed in the inner limiting membrane and around blood vessels in the retina (at protein level) (PubMed:29777959). Plasma 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 (PubMed:17614963).

Description:
Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization
Sequence:
MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHPQPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTRGGNSNGALCHFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDMGHMMRCTCVGNGRGEWTCIAYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDSWEKYVHGVRYQCYCYGRGIGEWHCQPLQTYPSSSGPVEVFITETPSQPNSHPIQWNAPQPSHISKYILRWRPKNSVGRWKEATIPGHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTSTPVTSNTVTGETTPFSPLVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDTTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPRDLQFVEVTDVKVTIMWTPPESAVTGYRVDVIPVNLPGEHGQRLPISRNTFAEVTGLSPGVTYYFKVFAVSHGRESKPLTAQQTTKLDAPTNLQFVNETDSTVLVRWTPPRAQITGYRLTVGLTRRGQPRQYNVGPSVSKYPLRNLQPASEYTVSLVAIKGNQESPKATGVFTTLQPGSSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYVYTIQVLRDGQERDAPIVNKVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGNSLEEVVHADQSSCTFDNLSPGLEYNVSVYTVKDDKESVPISDTIIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYVVSVSSVYEQHESTPLRGRQKTGLDSPTGIDFSDITANSFTVHWIAPRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTNLTPGTEYVVSIVALNGREESPLLIGQQSTVSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIDKPSQMQVTDVQDNSISVKWLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGEEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAIPAPTDLKFTQVTPTSLSAQWTPPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAVPANGQTPIQRTIKPDVRSYTITGLQPGTDYKIYLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLLVSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTSGQQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYPHGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLTGLTRGATYNVIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDEWERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGGEPSPEGTTGQSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Rabbit
100
Bovine
100
Pig
92
Sheep
92
Xenopus
50
Horse
0
Dog
0
Zebrafish
0
Chicken
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P02751 As Substrate

Site PTM Type Enzyme
S41 Phosphorylation
Y101 Phosphorylation
Y106 Phosphorylation
Y112 Phosphorylation
T136 Phosphorylation
T278 O-Glycosylation
T279 O-Glycosylation
S280 O-Glycosylation
S281 O-Glycosylation
S283 O-Glycosylation
T287 O-Glycosylation
Y372 Phosphorylation
N430 N-Glycosylation
K486 Methylation
N528 N-Glycosylation
N542 N-Glycosylation
Y588 Phosphorylation
Y641 Phosphorylation
T715 Phosphorylation
N877 N-Glycosylation
S904 Phosphorylation
S909 Phosphorylation
Y937 Phosphorylation
T960 Phosphorylation
S968 Phosphorylation
T972 Phosphorylation
K987 Acetylation
N1007 N-Glycosylation
Y1042 Phosphorylation
K1050 Ubiquitination
Y1206 Phosphorylation
N1244 N-Glycosylation
T1271 Phosphorylation
T1276 O-Glycosylation
S1565 O-Glycosylation
S1566 O-Glycosylation
S1567 O-Glycosylation
T1570 O-Glycosylation
T1641 O-Glycosylation
T1743 Phosphorylation
T1762 Phosphorylation
T1786 Phosphorylation
S1833 Phosphorylation
K1837 Ubiquitination
T1840 Phosphorylation
T1842 Phosphorylation
T1855 Phosphorylation
T1860 Phosphorylation
Y1879 Phosphorylation
K1880 Acetylation
Y1884 Phosphorylation
S1982 Phosphorylation
T1999 O-Glycosylation
T2060 O-Glycosylation
T2061 O-Glycosylation
T2064 O-Glycosylation
T2065 O-Glycosylation
T2067 O-Glycosylation
N2108 N-Glycosylation
Y2258 Phosphorylation
Y2312 Phosphorylation
S2318 Phosphorylation
S2341 O-Glycosylation
S2341 Phosphorylation
T2345 O-Glycosylation
T2346 O-Glycosylation
S2349 O-Glycosylation
S2349 Phosphorylation
Y2350 Phosphorylation
Y2353 Phosphorylation
S2354 Phosphorylation
T2363 Phosphorylation
S2384 Phosphorylation

Research Backgrounds

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.

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.

PTMs:

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.

Subcellular Location:

Secreted>Extracellular space>Extracellular matrix.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
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 other cell types, is deposited as fibrils in the extracellular matrix. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine.

Subunit Structure:

Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP. Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity). Interacts with FST3 and MYOC.

(Microbial infection) Interacts with S.aureus FnbA.

(Microbial infection) Interacts with M.bovis FbpB via the collagen-binding region.

(Microbial infection) Interacts with recombinant S.pneumoniae PavA (rqcH).

(Microbial infection) Interacts with recombinant S.suis FbpS (rqcH) via fibronectin's N-terminal 30 kDa region.

(Microbial infection) Interacts with fibronectin-binding proteins from other Mycobacteria.

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.   (View pathway)

· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.   (View pathway)

· Environmental Information Processing > Signaling molecules and interaction > ECM-receptor interaction.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Bacterial invasion of epithelial cells.

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Cancers: Specific types > Small cell lung cancer.   (View pathway)

References

1). Xiong J et al. Genomic and Transcriptomic Characterization of Natural Killer T Cell Lymphoma. CANCER CELL 2020 Mar 16;37(3):403-419 (PubMed: 32183952) [IF=50.3]

Application: IF/ICC    Species: human    Sample: NK-92 cells

Figure 6. Biological Function of MGA and BRDT. (D) Immunofluorescence images of E-cadherin (green), fibronectin (red), or vimentin (red) in NK-92 cells transfected with MGA shRNAs or scramble. Cells were counterstained with DAPI (blue). (G) Immunofluorescence images of E-cadherin (green), fibronectin (red), or vimentin (red) in NK-92 cells transfected with pCMV6-BRDT (upper panel) or vector control (lower panel). Cells were counterstained with DAPI (blue).

2). Li X et al. Betulinic acid Attenuated Bleomycin-induced Pulmonary Fibrosis by Effectively Intervening Wnt/β-catenin Signaling. PHYTOMEDICINE 2021 Jan;81:153428. (PubMed: 33341025) [IF=7.9]

3). Tian Y et al. Huaier polysaccharides suppress triple-negative breast cancer metastasis and epithelial-mesenchymal transition by inducing autophagic degradation of Snail. Cell and Bioscience 2021 Sep 4;11(1):170. (PubMed: 34481526) [IF=7.5]

Application: WB    Species: human    Sample: breast cancer cells

Fig. 1| PS-T inhibits invasion, migration and EMT in breast cancer cells in vitro and in vivo. d 4 T-1 and MDA-MB-231 cells are treated with 5 μg/mL PS-T for 24 h. The levels of each EMT marker are quantifed using the NIH ImageJ software. (mean ± SD, *P < 0.05 and **P < 0.01)

Application: WB    Species: Human    Sample: breast cancer cells

Fig. 1 PS-T inhibits invasion, migration and EMT in breast cancer cells in vitro and in vivo. a The invasiveness of 4 T-1 and MDA-MB-231 cells after treatment with PS-T at 5 μg/mL for 12 h is evaluated using Transwell invasion assays at 24 h (mean  ±  SD, ***P  <  0.001). b Migratory ability of 4 T-1 and MDA-MB-231 cells after treatment with PS-T at different concentrations is evaluated using scratch assays at different time points (mean  ±  SD, **P  <  0.01, ***P  <  0.001). c Mice are treated with normal saline (control), 25 μg/g or 100 μg/g PS-T by oral gavage every other day for 21 days (mean  ±  SD, *P  <  0.05, **P  <  0.01, scale bars: 100 μm). d 4 T-1 and MDA-MB-231 cells are treated with 5 μg/mL PS-T for 24 h. The levels of each EMT marker are quantified using the NIH ImageJ software. (mean  ±  SD, *P  <  0.05 and **P  <  0.01)

4). Li X et al. Bergenin attenuates bleomycin‐induced pulmonary fibrosis in mice via inhibiting TGF‐β1 signaling pathway. PHYTOTHERAPY RESEARCH 2021 Aug 10. (PubMed: 34375009) [IF=7.2]

5). Li X et al. Synthesis and discovery of a drug candidate for treatment of idiopathic pulmonary fibrosis through inhibition of TGF-β1 pathway. EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY 2018 Aug 3;157:229-247 (PubMed: 30096654) [IF=6.7]

6). Huang X et al. CD39+ Fibroblasts Enhance Myofibroblast Activation by Promoting IL-11 Secretion in Hypertrophic Scars. Journal of Investigative Dermatology 2021 Sep 17;S0022-202X(21)02210-7. (PubMed: 34537192) [IF=6.5]

7). Chakraborty et al. Primary Human Trabecular Meshwork Model for Pseudoexfoliation. Cells 2021 Dec 07;10(12) (PubMed: 34943956) [IF=6.0]

Application: WB    Species: Human    Sample:

Figure 3. TGF-β1 induces expression of pro-fibrotic molecules. Relative mRNA expression of (a) α-SMA (b) COL6A2 (c) Fibrillin (d) Fibronectin (e) PAI-1 (f) UPR genes XBP1 and CCT4 (g) Protein expression of pro-fibrotic molecules after TGF-β1 treatment with densitometry analysis using ImageJ (h). (i) Vimentin expression after 10 ng/mL TGF-β1 treatment and densitometry analysis (j). The error bars represent standard deviation

8). Li X et al. Myricetin ameliorates bleomycin-induced pulmonary fibrosis in mice by inhibiting TGF-β signaling via targeting HSP90β. BIOCHEMICAL PHARMACOLOGY 2020 Jun 11;114097. (PubMed: 32535102) [IF=5.8]

9). Song X et al. Recombinant truncated latency-associated peptide alleviates liver fibrosis in vitro and in vivo via inhibition of TGF-β/Smad pathway. MOLECULAR MEDICINE 2022 Jul 16;28(1):80. (PubMed: 35842576) [IF=5.7]

Application: WB    Species: Rat    Sample: HSC-T6 cells

Fig. 4Detection of the effect of LAP and tLAP on liver fibrosis in HSC-T6 cells. A Detection of the effect of LAP and tLAP on cell proliferation by MTT. B Detection of the effect of LAP and tLAP on cell index by RTCA. C Detection of the mRNA expression α-SMA, Collagen I, Collagen IV, and Fibronectin in HSC-T6 cells. D Detection of the expression of α-SMA, Collagen I and Fibronectin in HSC-T6 cells. **P < 0.01 vs control group; ***P < 0.001 vs control group; #P < 0.05 vs TGF-β1 group; ##P < 0.01 vs TGF-β1 group; ###P < 0.001 vs TGF-β1 group; △P < 0.05, TGF-β1 + tLAP group vs TGF-β1 + LAP group; △△P < 0.01, TGF-β1 + tLAP group vs TGF-β1 + LAP group

Application: IF/ICC    Species: Rat    Sample: HSC-T6 cells

Fig. 5Detection of fibrosis-related proteins expression in HSC-T6 cells by Immunofluorescence. A Immunofluorescence detection of α‑SMA. B Immunofluorescence detection of collagen I. C Immunofluorescence detection of Fibronectin. DAPI (blue, nuclear stain) and antibodies to α‑SMA, Collagen I and Fibronectin (red), immunofluorescence staining (magnification × 200), Scale bars = 40 μm. **P < 0.01 vs control group; ***P < 0.001 vs control group; #P < 0.05 vs TGF-β1 group; ##P < 0.01 vs TGF-β1 group

10). Li X et al. Antifibrotic Mechanism of Cinobufagin in Bleomycin-Induced Pulmonary Fibrosis in Mice. Frontiers in Pharmacology 2019 Sep 13;10:1021 (PubMed: 31572194) [IF=5.6]

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