- 产品信息
商品描述
靶点-Target
JPH2
反应性
Human,Rat,Mouse,
应用
WB,ELISA
宿主物种-Host Species
Rabbit
同种型-Isotype
IgG
修饰-Modification
Unmodified
MW(Observed)
76kD
推荐稀释比
WB 1:500-2000;ELISA 1:5000-20000
组成
PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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
克隆性
Polyclonal
免疫原
Synthesized peptide derived from human protein . at AA range: 611-660
特异性
JPH2 Polyclonal Antibody detects endogenous levels of protein.
基因名称
JPH2 JP2
蛋白名称
Junctophilin-2 (JP-2) (Junctophilin type 2)
Organism-1
Human
基因ID-1
57158
SwissProt-1
Q9BR39
Organism-2
Mouse
SwissProt-2
Q9ET78
Organism-3
Rat
SwissProt-3
Q2PS20
背景
Junctional complexes between the plasma membrane and endoplasmic/sarcoplasmic reticulum are a common feature of all excitable cell types and mediate cross talk between cell surface and intracellular ion channels. The protein encoded by this gene is a component of junctional complexes and is composed of a C-terminal hydrophobic segment spanning the endoplasmic/sarcoplasmic reticulum membrane and a remaining cytoplasmic domain that shows specific affinity for the plasma membrane. This gene is a member of the junctophilin gene family. Alternative splicing has been observed at this locus and two variants encoding distinct isoforms are described. [provided by RefSeq, Jul 2008],
细胞定位
[Junctophilin-2]: Cell membrane ; Peripheral membrane protein . Sarcoplasmic reticulum membrane ; Single-pass type IV membrane protein . Endoplasmic reticulum membrane ; Single-pass type IV membrane protein . The transmembrane domain is anchored in sarcoplasmic reticulum membrane, while the N-terminal part associates with the plasma membrane. In heart cells, it predominantly associates along Z lines within myocytes. In skeletal muscle, it is specifically localized at the junction of A and I bands. .; [Junctophilin-2 N-terminal fragment]: Nucleus . Accumulates in the nucleus of stressed hearts. .





