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AV31692

Sigma-Aldrich

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

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.

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


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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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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