TRIM32, Polyclonal Antibody

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit

Purified by antigen-affinity chromatography.

Supplied in 0.1M Tris-buffered saline with 20% Glycerol (pH7.0). 0.01% Thimerosal was added as a preservative.

Store at -20 degree C for long term preservation (recommended). Store at 4 degree C for short term use.

Small volumes of anti-TRIM32 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

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. [provided by RefSeq]

Total protein Ab

Western Blot (WB), Immunohistochemistry (IHC), Immunofluorescence (IF)

Western blotting: 1:500-1:3000
Immunohistochemistry: 1:100-1:250
Immunofluorescence: 1:100-1:200

Sample (30 ug of whole cell lysate) A: 293T 7.5% SDS PAGE Primary antibody diluted at 1: 1000

Immunohistochemical analysis of paraffin-embedded H441 Xenograft, using TRIM32 antibody at 1: 100 dilution.

Immunofluorescence analysis of paraformaldehyde-fixed A431, using TRIM32 antibody at 1: 500 dilution.

71,989 Da

tripartite motif containing 32

E3 ubiquitin-protein ligase TRIM32

E3 ubiquitin-protein ligase TRIM32

HT2A  [Similar Products]

TRI32_HUMAN

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. [provided by RefSeq, Jul 2008]

TRIM32: Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Defects in TRIM32 are the cause of limb-girdle muscular dystrophy type 2H (LGMD2H); also known as muscular dystrophy Hutterite type. LGMD2H is an autosomal recessive degenerative myopathy characterized by pelvic girdle, shoulder girdle and quadriceps muscle weakness. Clinical phenotype and severity are highly variable. Disease progression is slow and most patients remain ambulatory into the sixth decade of life. Defects in TRIM32 are the cause of Bardet-Biedl syndrome type 11 (BBS11). Bardet-Biedl syndrome (BBS) is a genetically heterogeneous, autosomal recessive disorder characterized by usually severe pigmentary retinopathy, early onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. A relatively high incidence of BBS is found in the mixed Arab populations of Kuwait and in Bedouin tribes throughout the Middle East, most likely due to the high rate of consaguinity in these populations and a founder effect. Belongs to the TRIM/RBCC family.

Protein type: Ligase; Ubiquitin ligase; Ubiquitin conjugating system; EC 6.3.2.19; EC 6.3.2.-

Chromosomal Location of Human Ortholog: 9q33.1

Cellular Component: cytoplasm; cytosol; nucleus; striated muscle thick filament

Molecular Function: ligase activity; myosin binding; protein binding; protein self-association; RNA binding; Tat protein binding; transcription coactivator activity; translation initiation factor binding; ubiquitin binding; ubiquitin-protein ligase activity; zinc ion binding

Biological Process: activation of NF-kappaB transcription factor; fat cell differentiation; indirect flight muscle actin ubiquitination; innate immune response; negative regulation of fibroblast proliferation; negative regulation of viral transcription; positive regulation of cell cycle; positive regulation of cell growth; positive regulation of cell migration; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of interferon type I production; positive regulation of neurogenesis; positive regulation of neuron differentiation; positive regulation of protein catabolic process; positive regulation of proteolysis; positive regulation of transcription factor activity; protein polyubiquitination; protein ubiquitination; protein ubiquitination during ubiquitin-dependent protein catabolic process; regulation of interferon type I production; response to UV; tissue homeostasis

Disease: Bardet-biedl Syndrome 11; Muscular Dystrophy, Limb-girdle, Type 2h

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