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一抗
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中文名称

hDAPK1-T1316 一抗

英文名字
hDAPK1-T1316 Primary antibody
供应商
Promab
产品货号
PMB-P34859
产品报价
¥询价/100ul
产品说明书
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购买方式
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产品新闻
背景资料
Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Phosphorylates PIN1 resulting in inhibition of its catalytic activity, nuclear localization, and cellular function. Phosphorylates TPM1, enhancing stress fiber formation in endothelial cells. Phosphorylates STX1A and significantly decreases its binding to STXBP1. Phosphorylates PRKD1 and regulates JNK signaling by binding and activating PRKD1 under oxidative stress. Phosphorylates BECN1, reducing its interaction with BCL2 and BCL2L1 and promoting the induction of autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating mTORC1 activity in a growth factor-dependent pathway. Phosphorylates RPS6, MYL9 and DAPK3. Acts as a signaling amplifier of NMDA receptors at extrasynaptic sites for mediating brain damage in stroke. Cerebral ischemia recruits DAPK1 into the NMDA receptor complex and it phosphorylates GRINB at Ser-1303 inducing injurious Ca(2+) influx through NMDA receptor channels, resulting in an irreversible neuronal death. Required together with DAPK3 for phosphorylation of RPL13A upon interferon-gamma activation which is causing RPL13A involvement in transcript-selective translation inhibition.
应用类型
WB
免疫原
This antibody is generated from a mouse immunized with a KLH conjugated synthetic peptide between amino acids from human.
来源宿主
Mouse
反应性
Human, Mouse
保存建议
4℃短期保存;-20℃长期保存。避免冻融循环。
其他
ProMab 生物技术公司通过整合生物信息学、分子生物学、蛋白质表达、纯化技术、基因克隆、微生物学和免疫学,利用新型高通量技术开发重组蛋白、抗体和工程细胞系并将其商业化。专注于免疫治疗领域,特别是 CAR-T/NK 细胞技术。ProMab 还开发了一种新型的 mRNA 脂质纳米颗粒(mRNA-LNP)平台,用于即用型试剂和定制研究服务,以推进现有产品并扩展到更多的研究领域。
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