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Key Documents

MAB1919

Sigma-Aldrich

Anti-Fibrillin Antibody, clone 11C1.3

clone 11C1.3, Chemicon®, from mouse

Synonym(s):

Anti-ACMICD, Anti-FBN, Anti-GPHYSD2, Anti-MASS, Anti-MFLS, Anti-MFS1, Anti-OCTD, Anti-SGS, Anti-SSKS, Anti-WMS, Anti-WMS2

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

11C1.3, monoclonal

species reactivity

bovine, pig, human

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
immunofluorescence: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... FBN1(2200)

Specificity

Bovine zonular fibrils. Reacts well with human elastin microfibrils and can be used to investigate the presence and organization of these fibrils either in Marfan patients or in fibroblasts obtained from these patients.

Immunogen

Bovine zonular fibrils

Application

Anti-Fibrillin Antibody, clone 11C1.3 is an antibody against Fibrillin for use in ELISA, IF, IP, WB, IH(P).
Immunoblot: antibody reacts with 350,000 Da protein released from bovine aortic smooth muscle cells, which is identical to that of fibrillin.

Immunohistochemistry: fresh frozen tissue: 1:200-1:500. Paraffin sections reactive after microwave citrate buffer antigen retrieval.

Immunoprecipitation: 5 microliters of antibody diluted in no more than 400 microliters of concentrated supernatants from bovine smooth muscle cells. We recommend either an anti-mouse IgG bead or a rabbit anti-mouse capture antibody followed by protein A.

ELISA

Optimal dilutions must be determined by the end user.
Research Category
Cell Structure
Research Sub Category
ECM Proteins

Physical form

Format: Purified
Liquid

Storage and Stability

Maintain at -20°C in undiluted aliquots for up to 12 months. Avoid repeated freeze/thaw cycles.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A common variant rs2054564 in ADAMST17 is associated with susceptibility to lumbar spondylosis.
Taniguchi, et al.
Scientific Reports, 13, 4900-4900 (2023)
ADAMTS10 protein interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts.
Kutz, WE; Wang, LW; Bader, HL; Majors, AK; Iwata, K; Traboulsi, EI; Sakai, LY; Keene, DR; Apte, SS
The Journal of Biological Chemistry null
Hannah L Bader et al.
Matrix biology : journal of the International Society for Matrix Biology, 31(7-8), 398-411 (2012-09-27)
ADAMTS-like proteins are related to ADAMTS metalloproteases by their similarity to ADAMTS ancillary domains. Here, we have characterized ADAMTSL5, a novel member of the superfamily with a unique modular organization that includes a single C-terminal netrin-like (NTR) module. Alternative splicing
Mohamed A Sideek et al.
Matrix biology : journal of the International Society for Matrix Biology, 34, 114-123 (2013-10-24)
Latent transforming growth factor-beta-1 binding protein-2 (LTBP-2) is a protein of ill-defined function associated with elastic fibers during elastinogenesis. Although LTBP-2 binds fibrillin-1, fibulin-5, and heparin/heparan sulfate, molecules critical for normal elastic fiber assembly, it does not interact directly with
Eric Hanssen et al.
The Journal of biological chemistry, 279(28), 29185-29194 (2004-05-08)
The interactions of microfibril-associated glycoprotein (MAGP)-2 have been investigated with fibrillins and fibrillin-containing microfibrils. Solid phase binding assays were conducted with recombinant fragments covering fibrillin-1 and most of fibrillin-2. MAGP-2, and its structure relative MAGP-1, were found to bind two

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