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Key Documents

MAB2499

Sigma-Aldrich

Anti-Fibrillin-1 Antibody, CT, clone 69

clone 69, Chemicon®, from mouse

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About This Item

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

fonte biológica

mouse

Nível de qualidade

forma do anticorpo

purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

69, monoclonal

reatividade de espécies

human

fabricante/nome comercial

Chemicon®

técnica(s)

ELISA: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

Isotipo

IgG1

nº de adesão NCBI

nº de adesão UniProt

Condições de expedição

wet ice

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... FBN1(2200)

Especificidade

Monoclonal antibody MAB2499 recognizes human Fibrillin-1. Epitope mapping studies identify the binding site of this antibody to the C-terminal end of the molecule, between amino acid residues 2093 and 2871. The antibody is reactive with human, chicken, and bovine Fibrillin-1.

Imunogênio

Epitope: C-terminus
Human Fibrillin-1

Aplicação

Detect Fibrillin-1 using this Anti-Fibrillin-1 Antibody, C-terminus, clone 69 validated for use in ELISA, IP, WB & IC.
Immunoblotting

Immunofluorescence

Immunoprecipitation

ELISA

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

forma física

Format: Purified
Purified immunoglobulin. Liquid at 1 mg/mL in 20 mM phosphate buffer, 250 mM NaCl, pH 7.6, containing 0.1% sodium azide.Note: Sodium azide is toxic. MSDS available upon request.

Armazenamento e estabilidade

Maintain refrigerated at 2-8°C in undiluted aliquots for up to 12 months.

Informações legais

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

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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Fibrillin-1 staining anomalies are associated with increased staining for TGF-beta and elastic fibre degradation; new clues to the pathogenesis of emphysema.
Mieke M J F Koenders,Ronnie G Wismans,Barry Starcher,Ben C J Hamel,Richard P N Dekhuijzen et al.
The Journal of Pathology null
Ko Tsutsui et al.
The Journal of biological chemistry, 285(7), 4870-4882 (2009-11-27)
ADAMTS (A disintegrin and metalloproteinase with thrombospondin motifs)-like (ADAMTSL) proteins, a subgroup of the ADAMTS superfamily, share several domains with ADAMTS proteinases, including thrombospondin type I repeats, a cysteine-rich domain, and an ADAMTS spacer, but lack a catalytic domain. We
Enrico Almici et al.
Frontiers in bioengineering and biotechnology, 10, 851825-851825 (2022-05-14)
Collagen VI-related dystrophies (COL6-RDs) are a group of rare congenital neuromuscular dystrophies that represent a continuum of overlapping clinical phenotypes that go from the milder Bethlem myopathy (BM) to the severe Ullrich congenital muscular dystrophy, for which there is no
Fibrillin-1 in human cartilage: developmental expression and formation of special banded fibers.
Keene, D R, et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 45, 1069-1082 (1997)
Expression of latent TGF-beta binding proteins and association with TGF-beta 1 and fibrillin-1 following arterial injury.
Sanjay Sinha, Anthony M Heagerty, C Adrian Shuttleworth, Cay M Kielty
Cardiovascular Research null

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