HPA023122
Anti-TRIM72 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
别名:
Anti-Tripartite motif-containing protein 72
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关于此项目
Conjugate:
unconjugated
Clone:
polyclonal
Application:
immunofluorescence
immunohistochemistry (formalin-fixed, paraffin-embedded sections)
western blot
immunohistochemistry (formalin-fixed, paraffin-embedded sections)
western blot
Species reactivity:
human
Citations:
5
Technique(s):
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
western blot: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
western blot: suitable
Uniprot accession no.:
产品名称
Anti-TRIM72 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
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)
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
western blot: suitable
immunogen sequence
LKTQLPQQKLQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRVFLAALEGSLDREAERVRGE
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... TRIM72(493829)
Other Notes
Corresponding Antigen APREST76053
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
Application
Anti-TRIM72 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.
Biochem/physiol Actions
TRIM72 (tripartite motif containing 72) protein is involved in wound healing and scarring by regulating cell migration and modulating myofibroblast differentiation. The muscle TRIM72 is an E3 ligase and is responsible for the ubiquitination of insulin receptor substrate 1 (IRS-1) during skeletal myogenesis.
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.
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.
General description
The gene TRIM72 (tripartite motif containing 72) is mapped to human chromosome 16p11. It belongs to the TRIM (tripartite motif) family of proteins. The protein has two Zn2+ binding motifs.
Immunogen
Tripartite motif-containing protein 72 recombinant protein epitope signature tag (PrEST)
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存储类别
10 - Combustible liquids
wgk
WGK 1
法规信息
常规特殊物品
此项目有
Haichang Li et al.
The Journal of biological chemistry, 290(40), 24592-24603 (2015-08-26)
Cell membrane repair is an important aspect of physiology, and disruption of this process can result in pathophysiology in a number of different tissues, including wound healing, chronic ulcer and scarring. We have previously identified a novel tripartite motif family
Nga Nguyen et al.
The Journal of biological chemistry, 289(6), 3209-3216 (2013-12-18)
The striated muscle-specific mitsugumin 53 (MG53) is a novel E3 ligase that induces the ubiquitination of insulin receptor substrate 1 (IRS-1) during skeletal myogenesis, negatively regulating insulin-like growth factor and insulin signaling. Here we show that focal adhesion kinase (FAK)
Frances A Lemckert et al.
Cardiovascular research, 110(2), 178-187 (2016-01-23)
Mitsugumin-53 (MG53/TRIM72) is an E3-ubiquitin ligase that rapidly accumulates at sites of membrane injury and plays an important role in membrane repair of skeletal and cardiac muscle. MG53 has been implicated in cardiac ischaemia-reperfusion injury, and serum MG53 provides a
Leigh B Waddell et al.
Journal of neuropathology and experimental neurology, 70(4), 302-313 (2011-03-18)
Mutations in dysferlin cause an inherited muscular dystrophy because of defective membrane repair. Three interacting partners of dysferlin are also implicated in membrane resealing: caveolin-3 (in limb girdle muscular dystrophy type 1C), annexin A1, and the newly identified protein mitsugumin
Chuanxi Cai et al.
The Journal of biological chemistry, 290(22), 13830-13839 (2015-04-15)
Zinc is an essential trace element that participates in a wide range of biological functions, including wound healing. Although Zn(2+) deficiency has been linked to compromised wound healing and tissue repair in human diseases, the molecular mechanisms underlying Zn(2+)-mediated tissue
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