STS2 _ TULA (internal)
- Known as:
- STS2 _ TULA (middlesequence)
- Catalog number:
- Y213631
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- STS2 _ TULA (internal)
Ask about this productRelated genes to: STS2 _ TULA (internal)
- Gene:
- UBASH3A NIH gene
- Name:
- ubiquitin associated and SH3 domain containing A
- Previous symbol:
- -
- Synonyms:
- STS-2, TULA, CLIP4
- Chromosome:
- 21q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-05-02
- Date modifiied:
- 2015-08-13
- Gene:
- UBASH3B NIH gene
- Name:
- ubiquitin associated and SH3 domain containing B
- Previous symbol:
- -
- Synonyms:
- KIAA1959, STS-1, TULA2, TULA-2
- Chromosome:
- 11q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 2007-12-07
- Date modifiied:
- 2017-03-10
Related products to: STS2 _ TULA (internal)
(I) LightCycler 1. 0; (Internal Control can't be used for this system) ; (II) LightCycler2. 0; (III) PE5700, MJ_Opticon etc. single color systems; (IV) ABI7000, ABI7300, ABI7500, ABI7900, ABI StepO1.0ml Self-Standing Cryovial Internal Thread w/ O-Ring Seal1.2ml Cryogenic Vial,Self-Standing, Internal Thread1.2ml Self-Standing Cryovial Internal Thread w per O-Ring Seal1.2ml Self-Standing Cryovial Internal Thread w per Silicone Wa1.2ml Self-Standing Cryovial Internal Thread w per Washer Seal1.2ml Self-Standing Cryovial Internal Thread w/ O-Ring Seal1.2ml Self-Standing Cryovial Internal Thread w/ O-Ring Seal1.2ml Self-Standing Cryovial Internal Thread w/ Silicone Wa1.2ml Self-Standing Cryovial Internal Thread w/ Silicone Wa1.2ml Self-Standing Cryovial Internal Thread w/Washer Seal1.2ml Self-Standing Cryovial Internal Thread w/Washer Seal1.2ml Self-Standing Cryovial Internal Thread w_ O-Ring Seal1.2ml Self-Standing Cryovial Internal Thread w_ Silicone Wa1.5-times expansion model of ear dissection, external, middle & internal ear, 4 parts Related articles to: STS2 _ TULA (internal)
- The T cell Ubiquitin Ligand (TULA) protein family contains two members, UBASH3A and UBASH3B, that display similarities in protein sequence and domain structure. Both TULA proteins act to repress T cell activation via a combination of overlapping and nonredundant functions. UBASH3B acts mainly as a phosphatase that suppresses proximal T cell receptor (TCR) signaling. In contrast, UBASH3A acts primarily as an adaptor protein, interacting with other proteins (including UBASH3B) in T cells upon TCR stimulation and resulting in downregulation of TCR signaling and NF-κB signaling. Human genetic and functional studies have revealed another notable distinction between UBASH3A and UBASH3B: numerous genome-wide association studies have identified statistically significant associations between genetic variants in and around the UBASH3A gene and at least seven different autoimmune diseases, suggesting a key role of UBASH3A in autoimmunity. However, the evidence for an independent role of UBASH3B in autoimmune disease is limited. This review summarizes key findings regarding the roles of TULA proteins in T cell biology and autoimmunity, highlights the commonalities and differences between UBASH3A and UBASH3B, and speculates on the individual and joint effects of TULA proteins on T cell signaling. - Source: PubMed
Publication date: 2024/11/18
Wang HuaConcannon PatrickGe Yan - FLI1 is an oncogenic transcription factor that promotes diverse malignancies through mechanisms that are not fully understood. Herein, FLI1 is shown to regulate the expression of Ubiquitin Associated and SH3 Domain Containing A/B (UBASH3A/B) genes. UBASH3B and UBASH3A are found to act as an oncogene and tumor suppressor, respectively, and their combined effect determines erythroleukemia progression downstream of FLI1. - Source: PubMed
Publication date: 2024/03/09
Wang JieWang ChunlinHu AnlingYu KunlinKuang YiGajendran BabuZacksenhaus EldadSample Klarke MichaelXiao XiaoLiu WulingBen-David Yaacov - UBASH3A and UBASH3B are protein families of atypical protein tyrosine phosphatases that function as regulators of various cellular processes during mammalian development. As UBASH3A has only mild phosphatase activity, its regulatory effects are based on the phosphatase-independent mechanisms. On the contrary, UBASH3B has strong phosphatase activity, and the suppression of its receptor signalling is mediated by Syk and Zap-70 kinases. The regulatory functions of UBASH3A and UBASH3B are particularly evident in the lymphoid tissues and kidney development. These tyrosine phosphatases are also known to play key roles in autoimmunity and neoplasms. However, their involvement in mammalian development and its regulatory functions are largely unknown and are discussed in this review. - Source: PubMed
Publication date: 2024/02/05
Vukojević KatarinaŠoljić VioletaMartinović VlatkaRaguž FilaFilipović Natalija - The two members of the UBASH3/STS/TULA protein family have been shown to critically regulate key biological functions, including immunity and hemostasis, in mammalian biological systems. Negative regulation of signaling through immune receptor tyrosine-based activation motif (ITAM)- and hemITAM-bearing receptors mediated by Syk-family protein tyrosine kinases appears to be a major molecular mechanism of the down-regulatory effect of TULA-family proteins, which possess protein tyrosine phosphatase (PTP) activity. However, these proteins are likely to carry out some PTP-independent functions as well. Whereas the effects of TULA-family proteins overlap, their characteristics and their individual contributions to cellular regulation also demonstrate clearly distinct features. Protein structure, enzymatic activity, molecular mechanisms of regulation, and biological functions of TULA-family proteins are discussed in this review. In particular, the usefulness of the comparative analysis of TULA proteins in various metazoan taxa, for identifying potential roles of TULA-family proteins outside of their functions already established in mammalian systems, is examined. - Source: PubMed
Publication date: 2023/05/23
Tsygankov Alexander Y - Two members of the UBASH3/STS/TULA family exhibit a unique protein domain structure, which includes a histidine phosphatase domain, and play a key role in regulating cellular signaling. UBASH3A/STS-2/TULA is mostly a lymphoid protein, while UBASH3B/STS-1/TULA-2 is expressed ubiquitously. Dephosphorylation of tyrosine-phosphorylated proteins by TULA-2 and, probably to a lesser extent, by TULA critically contribute to the molecular basis of their regulatory effect. The notable differences between the effects of the two family members on cellular signaling and activation are likely to be linked to the difference between their specific enzymatic activities. However, these differences might also be related to the functions of their domains other than the phosphatase domain and independent of their phosphatase activity. The down-regulation of the Syk/Zap-70-mediated signaling, which to-date appears to be the best-studied regulatory effect of TULA family, is discussed in detail in this publication. - Source: PubMed
Publication date: 2019/10/19
Tsygankov Alexander Y