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UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
69, monoclonal
Application:
ELISA
immunocytochemistry
immunoprecipitation (IP)
western blot
immunocytochemistry
immunoprecipitation (IP)
western blot
Species reactivity:
human
Citations:
6
Technique(s):
ELISA: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
Uniprot accession no.:
产品名称
Anti-Fibrillin-1 Antibody, CT, clone 69, clone 69, Chemicon®, from mouse
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
69, monoclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... FBN1(2200)
Application
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.
Immunofluorescence
Immunoprecipitation
ELISA
Optimal working dilutions must be determined by end user.
Research Category
Cell Structure
Cell Structure
Research Sub Category
ECM Proteins
ECM Proteins
Biochem/physiol Actions
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.
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.
Immunogen
Epitope: C-terminus
Human Fibrillin-1
Physical form
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.
Preparation Note
Maintain refrigerated at 2-8°C in undiluted aliquots for up to 12 months.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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存储类别
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Fan Chen et al.
Skin research and technology : official journal of International Society for Bioengineering and the Skin (ISBS) [and] International Society for Digital Imaging of Skin (ISDIS) [and] International Society for Skin Imaging (ISSI), 29(6), e13350-e13350 (2023-06-26)
Intrinsic skin aging is an inevitable process with reduced extracellular matrix deposition and impaired mechanical integrity in the dermal-epidermal junction (DEJ). Hyaluronan is one of the most promising natural ingredients. In this research, multiple mechanisms of a novel hyaluronan complex
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
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
Dipti Thakkar et al.
Connective tissue research, 55(5-6), 397-402 (2014-08-29)
There is increasing evidence for a progressive extracellular matrix change in rotator cuff disease progression. Directly surrounding the cell is the pericellular matrix, where assembly of matrix aggregates typically occurs making it critical in the response of tendon cells to
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