Product: Fibrillin 1 Antibody
Catalog: AF0429
Description: Rabbit polyclonal antibody to Fibrillin 1
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit
Mol.Wt.: 312kDa; 312kD(Calculated).
Uniprot: P35555
RRID: AB_2834136

View similar products>>

   Size Price Inventory
 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors

Product Info

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

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.

Pig(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%)
Fibrillin 1 Antibody detects endogenous levels of total Fibrillin 1.
Cite Format: Affinity Biosciences Cat# AF0429, RRID:AB_2834136.
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
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.


350 kDa glycoprotein component extracellular microfibril; ACMICD; FBN 1; FBN; FBN1; FBN1_HUMAN; Fibrillin 15; Fibrillin-1; Fibrillin1; Fibrillin15; GPHYSD2; Marfan syndrome; MASS; MFS 1; MFS1; OCTD; SGS; SSKS; Weill Marchesani syndrome; WMS; WMS2;


FBN1 Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-1- containing microfibrils provide long-term force bearing structural support. Belongs to the fibrillin family. Interacts with COL16A1. Note: This description may include information from UniProtKB.



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.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P35555 As Substrate

Site PTM Type Enzyme
K54 Sumoylation
S115 Phosphorylation
R232 Methylation
K278 Sumoylation
S346 Phosphorylation
S352 Phosphorylation
N448 N-Glycosylation
K568 Sumoylation
K599 Sumoylation
K612 Sumoylation
K666 Acetylation
K666 Sumoylation
K666 Ubiquitination
K672 Acetylation
K672 Ubiquitination
K747 Ubiquitination
K799 Sumoylation
K799 Ubiquitination
K904 Sumoylation
K904 Ubiquitination
Y962 Phosphorylation
K1017 Sumoylation
K1023 Sumoylation
K1027 Sumoylation
K1033 Sumoylation
S1037 Phosphorylation
K1043 Sumoylation
K1043 Ubiquitination
N1067 N-Glycosylation
K1317 Sumoylation
N1484 N-Glycosylation
Y1535 Phosphorylation
N1581 N-Glycosylation
K1836 Sumoylation
S2047 Phosphorylation
S2048 Phosphorylation
S2049 Phosphorylation
K2064 Sumoylation
K2069 Sumoylation
K2246 Sumoylation
T2297 Phosphorylation
K2298 Sumoylation
K2387 Acetylation
K2388 Acetylation
K2388 Sumoylation
K2388 Ubiquitination
K2407 Sumoylation
S2702 Phosphorylation
S2709 Phosphorylation
T2788 Phosphorylation
K2805 Sumoylation
K2809 Sumoylation
S2813 Phosphorylation
K2821 Sumoylation
T2826 Phosphorylation
Y2827 Phosphorylation
S2832 Phosphorylation
T2834 Phosphorylation
Y2837 Phosphorylation
K2848 Sumoylation
Y2849 Phosphorylation
K2851 Sumoylation
K2863 Sumoylation
K2865 Sumoylation

Research Backgrounds


Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function. Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1. Binds heparin and this interaction has an important role in the assembly of microfibrils.

Hormone that targets the liver to increase plasma glucose levels. Secreted by white adipose tissue and circulates in the plasma. Acts in response to fasting and promotes blood glucose elevation by binding to the surface of hepatocytes. Promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation.


Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils. The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide. Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils.

Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils.

Subcellular Location:

Note: Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166).

Note: Secreted into the plasma.

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
Subunit Structure:

Interacts with COL16A1. Interacts with integrin alpha-V/beta-3. Interacts with ADAMTS10; this interaction promotes microfibril assembly. Interacts with THSD4; this interaction promotes fibril formation (By similarity). Interacts (via N-terminal domain) with FBLN2, FBLN4 and FBLN5. Interacts with ELN. Forms a ternary complex with ELN and FBLN2 or FBLN5 and a significant interaction with ELN seen only in the presence of FBLN2 or FBLN5. Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner. Interacts (via N-terminal domain) with LTBP1 (via C-terminal domain). Interacts with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6. Interacts (via N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5. Interacts (via N-terminal domain) with MFAP2 and MFAP5. Interacts with ADAMTSL5. Interacts with MFAP4. Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent manner.


Belongs to the fibrillin family.


1). Chakraborty M 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

2). Chakraborthy M et al. A Feedback Loop between TGF-β1 and ATG5 Mediated by miR-122-5p Regulates Fibrosis and EMT in Human Trabecular Meshwork Cells. Current Issues in Molecular Biology 2023 Mar 13;45(2381-2392) (PubMed: 36975524) [IF=3.1]

Application: WB    Species: Human    Sample: HTM Cells

Figure 2. TGF-induced fibrosis and EMT is regulated by ATG5. (A) The protein levels of ATG-5, LC3-I, LC3-II, SMA, vimentin, fibronectin, and fibrillin in whole-cell lysates of siRNA-mediated knockdown HTM cells with (10 ng/mL) and without TGF-β1. (B–G), relative quantification of the proteins obtained using densitometry analysis of the bands. The error bars represent the standard deviation

3). Zhao S et al. Sudden death due to a novel nonsense mutation in Marfan syndrome. Legal Medicine 2021 Sep 24;53:101967 (PubMed: 34598112) [IF=1.5]

Restrictive clause


Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.