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Caspase-1 (phospho Ser376) Polyclonal Antibody
货 号:
YM-A15697
规 格:
50μL;100μL
种属反应:
Human,Mouse,Rat
实验应用:
WB,IHC,IF,ELISA
产品详情
产品名称
Caspase-1 (phospho Ser376) Polyclonal Antibody
产品货号
YM-A15697
规格
50μL;100μL
种属反应
Human,Mouse,Rat
实验应用
WB,IHC,IF,ELISA
分子量
45kD
宿主
Rabbit
同种型
IgG
修饰
Phospho
推荐稀释比
WB 1:500-1:2000;IHC 1:100-1:300;ELISA 1:20000;IF 1:50-200
组成
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
纯化工艺
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
储存
-15°C to -25°C/1 year(Do not lower than -25°C)
浓度
1 mg/ml
克降性
Polyclonal
克隆号
免疫原
The antiserum was produced against synthesized peptide derived from human Caspase 1 around the phosphorylation site of Ser376. AA range:342-391
特异性
Phospho-Caspase-1 (S376) Polyclonal Antibody detects endogenous levels of Caspase-1 protein only when phosphorylated at S376.
基因名称
CASP1
蛋白名称
Caspase1
别名
CASP1;IL1BC;IL1BCE;Caspase-1;CASP-1;Interleukin-1 beta convertase;IL-1BC;Interleukin-1 beta-converting enzyme;ICE;IL-1 beta-converting enzyme;p45
基因ID-1
834
SwissProt
P29466
背景
This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This gene was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. This gene has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing results in transcript variants encoding distinct isoforms. [provided by RefSeq, Mar 2012],
细胞定位
Cytoplasm . Cell membrane .
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