HPA002822
Anti-EMILIN1 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-EMILIN-1 precursor antibody produced in rabbit, Anti-Elastin microfibril interface-located protein 1 antibody produced in rabbit, Anti-Elastin microfibril interfacer 1 antibody produced in rabbit
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All Photos(5)
About This Item
Recommended Products
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
product line
Prestige Antibodies® Powered by Atlas Antibodies
form
buffered aqueous glycerol solution
species reactivity
human
technique(s)
immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:200-1:500
immunogen sequence
PQSIMYRRFLRPRYRVAYKTVTDMEWRCCQGYGGDDCAESPAPALGPASSTPRPLARPARPNLSGSSAGSPLSGLGGEGPGESEKVQQLEEQVQSLTKELQGLRGVLQGLSGRLAEDVQRAVETAFNGRQQPADAAARPGVHETLNE
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... EMILIN1(11117)
Immunogen
EMILIN-1 precursor recombinant protein epitope signature tag (PrEST)
Application
Anti-EMILIN1 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Immunofluorescence (1 paper)
Biochem/physiol Actions
The gene EMILIN1 encodes elastin microfibril interfacer-1 protein that contributes to the pathogenesis of essential hypertension (EH) in humans. It maintains elastic fibres in vessel walls and peripheral arterial compliance. It is considered as a candidate gene for human EH. It may regulate the formation of oxytalan fibers and play a role in their homeostasis. It acts as a negative regulator of the transforming growth factor-beta (TGF-β) signaling, which is involved in blood pressure (BP) homeostasis. The gene participates in the transcription of elastogenesis of elastic extracellular matrix (ECM′s) formation.
Features and Benefits
Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.
Every Prestige Antibody is tested in the following ways:
Every Prestige Antibody is tested in the following ways:
- IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
- Protein array of 364 human recombinant protein fragments.
Linkage
Corresponding Antigen APREST85200
Physical form
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Legal Information
Prestige Antibodies 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
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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Masanori Shimodaira et al.
American journal of hypertension, 23(5), 547-555 (2010-02-27)
Elastin microfibril interfacer 1 (EMILIN-1) is a negative regulator of the transforming growth factor-beta (TGF-beta) signaling, which is involved in blood pressure (BP) homeostasis. Emilin1 knockout mice display elevated BP. The aim of the present study was to assess the
V M S Oh et al.
Journal of human hypertension, 26(9), 553-561 (2011-07-15)
Studies in mice suggest that the elastin microfibril interfacer-1 gene (EMILIN1), the gene encoding elastin microfibril interfacer-1 protein, contributes to the pathogenesis of essential hypertension (EH) in humans. EMILIN1 in part maintains elastic fibres in vessel walls, and hence peripheral
Yuka Nakatomi et al.
Connective tissue research, 52(1), 30-35 (2010-08-13)
The elastic system fibers comprise oxytalan, elaunin, and elastic fibers, differing in their relative microfibril and elastin contents. Among them, human periodontal ligament (PDL) contains only oxytalan fibers (pure microfibrils). Elastin microfibril interface-located protein-1 (EMILIN-1) is localized at the interface
Chong Shen et al.
BMC medical genetics, 10, 118-118 (2009-11-20)
Elastogenesis of elastic extracellular matrix (ECM) which was recognized as a major component of blood vessels has been believed for a long time to play only a passive role in the dynamic vascular changes of typical hypertension. Emilin1 gene participated
Shinya Kondo et al.
Journal of cosmetic dermatology, 21(10), 4796-4804 (2022-01-23)
The elastic fiber structure becomes shorter, thicker, and curved with age. Nonetheless, the proteins and catabolic enzymes influencing the maintenance of and change in the three-dimensional (3D) structure of elastic fibers remain unknown. This study aimed to identify the proteins
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