AV31692
Anti-TRIM32 antibody produced in rabbit
affinity isolated antibody
Synonym(s):
Anti-Tripartite motif-containing 32
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
Pricing and availability is not currently available.
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
72 kDa
species reactivity
rat, human, dog, guinea pig, rabbit, mouse, horse, bovine
concentration
0.5 mg - 1 mg/mL
technique(s)
immunohistochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... TRIM32(22954)
General description
TRIM32 is an E3 ubiquitin ligase that activates miRNAs. this ligase inhibits self-renewal in mouse neural progenitor cells. TRIM32 mutations have been linked to Bardet-Biedl syndrome .
Rabbit Anti-TRIM32 antibody recognizes canine, bovine, human, mouse, rat, and zebrafish TRIM32.
Rabbit Anti-TRIM32 antibody recognizes canine, bovine, human, mouse, rat, and zebrafish TRIM32.
Immunogen
Synthetic peptide directed towards the C terminal region of human TRIM32
Application
Rabbit Anti-TRIM32 antibody can be used for western blot applications at 1μg/ml.
Biochem/physiol Actions
TRIM32 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM32 localizes to cytoplasmic bodies. The protein has also been localized to the nucleus, where it interacts with the activation domain of the HIV-1 Tat protein. The Tat protein activates transcription of HIV-1 genes.The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. The protein has also been localized to the nucleus, where it interacts with the activation domain of the HIV-1 Tat protein. The Tat protein activates transcription of HIV-1 genes.The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. The protein has also been localized to the nucleus, where it interacts with the activation domain of the HIV-1 Tat protein. The Tat protein activates transcription of HIV-1 genes.
Sequence
Synthetic peptide located within the following region: GFSIGSVGPDGQLGRQISHFFSENEDFRCIAGMCVDARGDLIVADSSRKE
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
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 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Annie P Chiang et al.
Proceedings of the National Academy of Sciences of the United States of America, 103(16), 6287-6292 (2006-04-12)
The identification of mutations in genes that cause human diseases has largely been accomplished through the use of positional cloning, which relies on linkage mapping. In studies of rare diseases, the resolution of linkage mapping is limited by the number
Jens C Schwamborn et al.
Cell, 136(5), 913-925 (2009-03-10)
In the mouse neocortex, neural progenitor cells generate both differentiating neurons and daughter cells that maintain progenitor fate. Here, we show that the TRIM-NHL protein TRIM32 regulates protein degradation and microRNA activity to control the balance between those two daughter
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