HPA022817
Anti-MKLN1 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
别名:
Anti-Muskelin
biological source
rabbit
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)
immunohistochemistry: 1:20- 1:50
immunogen sequence
QAAKDNPTKSLQEEEPCPRFAHQLVYDELHKVHYLFGGNPGKSCSPKMRLDDFWSLKLCRPSKDYLLRHCKYLIRKHRFEEKAQVDPLSALKYLQNDLYITVDHSDP
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... MKLN1(4289)
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General description
MKLN1 (Muskelin 1, intracellular mediator containing kelch motifs) is a primarily cytoplasmic protein consisting of mainly two domains, N- and C-terminal domains. Specifically, it is composed of a discoidin-like domain and a LiSH/CTLH domain. The C-terminal domain consists of a kelch motif with 6 kelch repeats followed by a C-terminal tail.
Immunogen
Muskelin recombinant protein epitope signature tag (PrEST)
Application
All Prestige Antibodies®Powered by Atlas Antibodies 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. We also provide Prestige Antibodies® protocols and other useful information.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Immunohistochemistry (1 paper)
Biochem/physiol Actions
MKLN1 (Muskelin 1, intracellular mediator containing kelch motifs) is mainly involved in different intracellular signaling pathways for scaffolding and nucleocytoplasmic protein shuttling. Its kelch repeats domain directly binds to the T-box DNA-binding domain of TBX20b isoform. It has been suggested that TBX20b and MKLN1 may be involved in novel regulatory mechanisms within heart development.
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.
Physical form
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Other Notes
Corresponding Antigen APREST74968
Legal Information
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
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存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Paige Debenedittis et al.
Biochemical and biophysical research communications, 409(2), 338-343 (2011-05-19)
The genetic regulation necessary for the formation of a four-chambered heart is tightly regulated by transcription factors such as TBX20, a member of the T-box (TBX) transcription factor family. TBX20 is critical for proper cardiogenesis and is expressed in the
J C Adams et al.
The EMBO journal, 17(17), 4964-4974 (1998-09-02)
We have used an expression cloning strategy based on a cell-attachment assay screen to seek identification of molecules required in cellular responses to thrombospondin-1, a regulated macromolecular component of extracellular matrix. We report the identification and functional characterization of a
Karsten Boldt et al.
Nature communications, 7, 11491-11491 (2016-05-14)
Cellular organelles provide opportunities to relate biological mechanisms to disease. Here we use affinity proteomics, genetics and cell biology to interrogate cilia: poorly understood organelles, where defects cause genetic diseases. Two hundred and seventeen tagged human ciliary proteins create a
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