In stock
SERCA2 belongs to the P-type family of ATPases (Xu et al., 1993; Toyofuku et al., 1994; Hawkins et al., 1994; Osada et al., 1998; Netticadan et al., 1999; Netticadan et al., 2000). Controversy still surrounds the phosphorylation status of Ser-38 and its physiological implication. Some groups have reported that Ser-38 of SERCA2 is phosphorylated by CaMKII, which apparently leads to a substantial increase in ATPase activity (Xu et al., 1993; Hawkins et al., 1994). However, the control of Ca2+ pump function by direct phosphorylation has not been observed by all investigators (Odermatt et al., 1996; Reddy et al., 1996; Rodriguez et al., 2004). Independent attempts to confirm SERCA2 phosphorylation at Ser-38 have failed to confirm the stimulation of Ca2+ pump function upon treatment with CaMKII, which suggests that Ser-38 phosphorylation of SERCA2 is not a significant regulatory feature of cardiac Ca2+ homeostasis. This antibody, described by Rodriguez et al. (2004), may help to resolve the controversy, as it recognises the Ser-38 phospho-epitope
Tested applications: Western Blot (1:1000 dilution). Species recognition: Epitope sequence exists in SERCA2 from all mammalian species.
BIOLEAF热搜 BIOLEAF试剂盒 BIOLEAF ELISA BIOLEAF试剂 BIOLEAF品牌 BIOLEAF抗体 BIOLEAF耗材 BIOLEAF小仪器
sitemap 细胞库查询 危险品图标 本公司网站所展示销售的产品仅供科研!
沪公网安备 31011202007338号