Anti-Polyubiquitylated conjugates monoclonal antibody (CABT-BL6370)

Mouse Anti-Polyubiquitylated conjugates monoclonal antibody for WB

Specifications


Host Species
Mouse
Antibody Isotype
IgM
Clone
GL2
Species Reactivity
Human
Immunogen
Crude preparation of polyubiquitylated lysozyme
Conjugate
Unconjugated

Target


Alternative Names
FLJ25987; MGC8385; Polyubiquitin B; RPS 27A; RPS27A; UBA 52

Citations


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References


The Roles of SPOP in DNA Damage Response and DNA Replication

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

Authors: Maekawa, Masashi; Higashiyama, Shigeki

Speckle-type BTB/POZ protein (SPOP) is a substrate recognition receptor of the cullin-3 (CUL3)/RING type ubiquitin E3 complex. To date, approximately 30 proteins have been identified as ubiquitinated substrates of the CUL3/SPOP complex. Pathologically, missense mutations in the substrate-binding domain of SPOP have been found in prostate and endometrial cancers. Prostate and endometrial cancer-associated SPOP mutations lose and increase substrate-binding ability, respectively. Expression of these SPOP mutants, thus, causes aberrant turnovers of the substrate proteins, leading to tumor formation. Although the molecular properties of SPOP and its cancer-associated mutants have been intensively elucidated, their cellular functions remain unclear. Recently, a number of studies have uncovered the critical role of SPOP and its mutants in DNA damage response and DNA replication. In this review article, we summarize the physiological functions of SPOP as a "gatekeeper" of genome stability.

CD4(+)T Cell Defects in a Mulibrey Patient With SpecificTRIM37Mutations

FRONTIERS IN IMMUNOLOGY

Authors: Bruzzaniti, Sara; Cirillo, Emilia; Prencipe, Rosaria; Giardino, Giuliana; Lepore, Maria Teresa; Garziano, Federica; Perna, Francesco; Procaccini, Claudio; Mascolo, Luigi; Pagano, Cristina; Fattorusso, Valentina; Mozzillo, Enza; Bifulco, Maurizio; Matarese, Giuseppe; Franzese, Adriana; Pignata, Claudio; Galgani, Mario

Mulibrey (muscle-liver-brain-eye) syndrome (MUL) is an autosomal recessive disorder caused by mutations in theTRIpartite motif(TRIM)37gene, encoding for TRIM37 a member of the TRIM E3 ubiquitin ligase protein family. MUL patients are characterized by growth retardation, dysmorphic features, and a wide range of abnormalities affecting different organs. However, T-cell abnormalities have not been observed in MUL subjects, to date. Here we described the immunological features of a MUL child carrying recently identifiedTRIM37mutations, a 17q22 deletion of maternal origin combined with aTRIM37variant of paternal origin. Here we found quantitative and functional defects in CD4(+)T cells from this MUL case. Low levels of TRIM37 protein were specifically detected in CD4(+)T cells of MUL patient and associated with their altered proliferation and cytokine production. Of note, both CD4(+)and CD8(+)T lymphocytes of MUL child displayed an effector memory phenotype compared with healthy children. This clinical case research highlighted the possible role of TRIM37 in the control of immune cell number and function, especially in CD4(+)T cells. Finally, this study may contribute to the novel mechanistic studies aim of identifying, in depth, the role of the TRIM37 protein in the immune system.

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