货号 |
bsm-33089M-1 |
品牌 |
|
浓度 |
|
货期 |
现货 |
英文名称 |
Mouse Anti-IDE antibody |
中文名称 |
Mouse Anti-IDE antibody |
研究领域 |
肿瘤,心血管,细胞生物,免疫学,信号转导,生长因子和激素,糖尿病, |
英文别名 |
BC2; Insulin degrading enzyme; FLJ35968; insulin protease; insulinase; insulysin; Abeta-degrading protease; FLJ35968; Ide; IDE_HUMAN; Insulin-degrading enzyme; OTTHUMP00000020097. |
反应物种(已验证) |
Human |
产品应用(已验证) |
WB |
产品应用(可推荐) |
IHC,ICC,IF |
推荐稀释比例 |
WB=1:500-1000,IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500,ICC=1:100-500, |
克隆类型 |
单克隆 |
克隆号 |
5H4 |
抗体来源 |
Mouse |
理论分子量 |
117 |
细胞定位 |
细胞浆,细胞膜,细胞外基质 |
性状 |
Liquid |
免疫原 |
KLH conjugated synthetic peptide derived from human IDE |
亚型 |
IgG |
纯化方法 |
affinity purified by Protein G |
SUBCELLULAR |
Cytoplasm. Cell surface. Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosolic isoform. |
SIMILARITY |
Belongs to the peptidase M16 family. |
SUBUNIT |
Homodimer. Can form higher oligomers. Interacts (via N-terminus) with varicella-zoster virus (VZV) envelope glycoprotein E (via N-terminus); the membrane-associated isoform may function as an entry receptor for this virus. |
Function |
Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and cleara |
Post-translational |
The N-terminus is blocked. |
SWISS |
P14735 |
Gene ID |
3416 |
保存条件 |
Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. |
Important Note |
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
英文介绍 |
Insulysin was identified nearly a century ago as an enzyme responsible for the degradation of insulin in cells, although the precise interactions between insulin and insulysin remain elusive. Human insulysin was cloned in 1988, and shown to be a 118 kDa protein that exists primarily as a homodimer, and perhaps also complexed with other molecules. The sequence is well conserved between humans, rats and mice, and the antibody recognizes these species. Insulysin is a metalloproteinase of the clan ME, family M16, which contains an active site HxxEH, a reversal of the canonical HExxH zinc binding motif. Considered a zinc metalloproteinase, the activity of insulysin can be blocked with EDTA or 1-10 phenanthroline. In addition to the active metalloproteinase domain, insulysin contains a second metalloproteinase site which is considered catalytically inactive, and is thought to assist in substrate binding. Insulysin is most closely related to the bacterial proteinase pitrilysin, (the human orthologue of which appears to be MPRP1) and the mammalian proteinsae nardilysin. Generally thought to be a cytoplasmic protein, insulysin has been isolated from many different tissues and cell lines, and can degrade intact insulin, insulin B chain, glucagon, denatured hemoglobin, alpha amyloid protein, TGF alpha and amylin. Recent work implicates insulysin in clearing beta amyloid plaques from the brain, and has generated much interest in Alzheimer’s disease research. The pH optimum for insulysin is basic, pH 8.5, which also distinguishes it from other metalloproteinases.
Insulin degrading enzyme (IDE) has a preferential affinity for insulin such that the presence of insulin will inhibit IDE mediated degradation of other substrates. IDE degrades a variety of other peptides including atrial natriuretic peptide and amylin. IDE catabolizes A beta and has been implicated as a candidate enzyme responsible for the degradation and clearance of A beta in the brain. IDE has also been shown to degrade the APP intracellular domain (AICD), a product of gamma secretase cleaved APP that may function in nuclear signaling. |