Calpain 1 Large Subunit (Mu-type)抗体可以识别内源性总的calpain1(大亚基)蛋白。抗体可以识别全长的钙蛋白酶1和在28位亮氨酸处自发进行了蛋白裂解的钙蛋白酶1。合成对应人钙蛋白酶1(大亚基)的多肽序列免疫动物获得多克隆抗体。抗体由肽亲和层析纯化。钙蛋白酶是钙依赖的硫醇蛋白酶,功能活化形式是一个由小调节亚基和两个大催化亚基(钙蛋白酶1或钙蛋白酶2)的其中之一组成的异二聚体。在体外,钙蛋白酶1(mu-钙蛋白酶)和钙蛋白酶2(M-钙蛋白酶)分别需要微摩尔水平和毫克分子水平的钙进行激活。体内钙蛋白酶激活目前是多种研究的主题,提示蛋白水解受到多种翻译后调控例如钙离子,异二聚体的亚细胞定位,EGFR-Erk信号通路的磷酸化调控,内源性抑制因子(钙蛋白酶抑素)和自发性蛋白水解(1)。钙蛋白酶抑素负向调控钙蛋白酶27位甘氨酸和29位亮氨酸间的自发水解(2)。钙蛋白酶影响细胞迁移是通过修饰而非降解它的底物进行的,这些底物负责细胞黏附和细胞骨架重排。操控钙蛋白酶活性引发了人们新药开发的兴趣,因为限制钙蛋白酶的活性将削弱肿瘤的侵润能力或慢性炎症(1)。
Species predicted to react based on 100% sequence homology:Rat
Specificity / Sensitivity
Calpain 1 Large Subunit (Mu-type) Antibody detects endogenous levels of total calpain 1 (large subunit) protein. The antibody detects full-length calpain 1 as well as calpain 1 autoproteolytically cleaved at leucine 28.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the human sequence of calpain 1 (large subunit). Antibodies are purified by protein A and peptide affinity chromatography.
Background
Calpain is a calcium-dependent thiol proteinase that is functionally active as a heterodimer composed of a small regulatory subunit and one of at least two large catalytic subunits (calpain 1 or calpain 2). In vitro, calpain 1 (mu-calpain) requires micromolar levels of calcium, while calpain 2 (M-calpain) requires millimolar levels of calcium for activation. The regulation of calpain in vivo is the subject of many current studies, which suggest that proteolytic activity is regulated post-transcriptionally by mechanisms such as calcium requirements, subcellular localization of the heterodimer, phosphorylation via the EGFR-Erk signaling cascade, endogenous inhibitors (calpastatin) and autoproteolytic cleavage (1). Calpastatin negatively regulates autoproteolytic cleavage of calpain 1 between Gly27 and Leu28 (2). Calpain influences cell migration by modifying rather than degrading its substrates responsible for cell adhesion and cytoskeletal arrangement. Control of calpain activity has caught the attention of drug development since limiting its activity could mute invasiveness of tumors or chronic inflammation (1).