Cosmo Bio抗体,CAC-TNL-002-SH2

Cosmo Bio抗体,CAC-TNL-002-SH2,蛋白质酪氨酸磷酸酶是一组酶,从蛋白质上磷酸化的酪氨酸残基中去除磷酸基。蛋白酪氨酸(pTyr)磷酸化是一种常见的翻译后修饰,可以为蛋白质相互作用和细胞定位创造新的识别基元,影响蛋白质稳定性,并调节酶活性。

蛋白质酪氨酸磷酸酶是一组酶,从蛋白质上磷酸化的酪氨酸残基中去除磷酸基。蛋白酪氨酸(pTyr)磷酸化是一种常见的翻译后修饰,可以为蛋白质相互作用和细胞定位创造新的识别基元,影响蛋白质稳定性,并调节酶活性。因此,维持适当水平的蛋白质酪氨酸磷酸化是许多细胞功能所必需的。酪氨酸特异性蛋白磷酸酶(PTPase;EC 3.1.3.48)使用半胱氨酸-磷酸酶中间体催化去除附着在酪氨酸残基上的磷酸基。这些酶是信号转导通路(如MAP激酶通路)和细胞周期控制的关键调控成分,在控制细胞生长、增殖、分化、转化和突触可塑性方面具有重要意义。

Cosmo Bio抗体,Anti Tyrosine-Protein Phosphatase Non-Receptor Type 6 (SHP-1/PTPN6) Phospho-Tyr536 pAb (Rabbit, Antiserum),CAC-TNL-002-SH2

Application: IP, IHC, WB

Clonality: Polyclonal

Host: Rabbit

Purification: Serum

Reactivity: Rat

Protein tyrosine phosphatases are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Protein tyrosine (pTyr) phosphorylation is a common post-translational modification that can create novel recognition motifs for protein interactions and cellular localization, affect protein stability, and regulate enzyme activity. As a consequence, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; EC 3.1.3.48) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation, transformation, and synaptic plasticity.

SHP1 belongs to the family of protein tyrosine phosphatases (PTPs), which dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases. PTPs and protein tyrosine kinases function in a variety of cellular processes, from cell survival to proliferation, differentiation, migration, and immune responses. SHP1 (PTPN6) and SHP2 (PTPN11) are closely related non–receptor-type PTPs, each having two Src homology 2 domains N-terminal to the phosphatase catalytic domain (5–7). Although SHP2 is expressed ubiquitously, SHP1 is predominantly expressed in hematopoietic cell lineages, and it has been implicated in the regulation of a diverse range of cytokine receptors, growth factor receptors, and immunoreceptors (5, 6, 8). SHP1 has been shown to associate with ITIMs in these receptors (5, 6) and has been proposed to bind to ITIM-like motifs in various kinases, including IL-1R–associated kinase 1, ERK1/2, p38, JNK, JAK2, JAK3, TAK1, IκB kinase α, and LYN (9, 10).