SAB1306751
ANTI-TRIM6 (N-TERMINAL) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
RING finger protein 89, RNF89, TRIM6, Tripartite motif-containing protein 6
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
rabbit
Quality Level
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
56400 Da
species reactivity
human
technique(s)
western blot: 1:1000
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... TRIM6(117854)
Physical form
Supplied in PBS with 0.09% (W/V) sodium azide
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
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Yifeng Zhang et al.
Turkish journal of medical sciences, 53(5), 1032-1044 (2023-02-28)
Hepatocellular carcinoma (HCC) ranks among the most prevalent malignancies worldwide and the third leading cause of cancer-related death. The TRIM (tripartite motif-containing) protein family members had been reported to be involved in carcinogenesis and tumor progression. Here we aimed to
Guangwei Zeng et al.
Aging, 11(11), 3536-3550 (2019-06-07)
Cardiomyocyte apoptosis is a major cause of myocardial ischemia/reperfusion (MI/R) injury, in which the activation of the signal transducer and activator of transcription 1 (STAT1) plays an important role. The E3-ubiquitin ligase TRIM6 has been implicated in regulating STAT1 activity
Adam Hage et al.
Cell reports, 38(10), 110434-110434 (2022-03-10)
Type I interferons (IFN-I) are essential to establish antiviral innate immunity. Unanchored (or free) polyubiquitin (poly-Ub) has been shown to regulate IFN-I responses. However, few unanchored poly-Ub interactors are known. To identify factors regulated by unanchored poly-Ub in a physiological
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