癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
Anti-Emerin Picoband Antibody
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | P50402 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for Emerin(EMD) detection. Tested with WB, IHC-P in Human;Mouse;Rat. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 2010 |
|---|---|
| Other Names | Emerin, EMD, EDMD, STA |
| Calculated MW | 28994 Da |
| Application Details | Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, By Heat Western blot, 0.1-0.5 µg/ml, Human, Mouse, Rat |
| Subcellular Localization | Nucleus inner membrane ; Single-pass membrane protein; Nucleoplasmic side . Nucleus outer membrane. Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non- farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus. |
| Tissue Specificity | Skeletal muscle, heart, colon, testis, ovary and pancreas. |
| Source | Eukaryota |
| Protein Name | Emerin |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | A synthetic peptide corresponding to a sequence at the N-terminus of human Emerin (1-48aa MDNYADLSDTELTTLLRRYNIPHGPVVGSTRRLYEKKIFEYETQRRRL), different from the related mouse sequence by eight amino acids, and from the related rat sequence by nine amino ac |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | EMD (HGNC:3331) |
|---|---|
| Function | Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments (PubMed:15328537). Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway (PubMed:16858403). Links centrosomes to the nuclear envelope via a microtubule association (PubMed:17785515). Required for proper localization of non-farnesylated prelamin-A/C (PubMed:19323649). Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. |
| Cellular Location | Nucleus inner membrane; Single-pass membrane protein; Nucleoplasmic side. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus |
| Tissue Location | Skeletal muscle, heart, colon, testis, ovary and pancreas |
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Emerin is a serine-rich nuclear membrane protein that in humans is encoded by the EMD gene. And this gene is mapped to Xq28. Emerin is a member of the nuclear lamina-associated protein family. It mediates membrane anchorage to the cytoskeleton. Emery–Dreifuss muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the EMD (also known clinically as STA) gene. Emerin appears to be involved in mechanotransduction, as emerin-deficient mouse fibroblasts failed to transduce normal mechanosensitive gene expression responses to strain stimuli. In cardiac muscle, emerin is also found complexed to beta-catenin at adherens junctions of intercalated discs, and cardiomyocytes from hearts lacking emerin showed beta-catenin redistribution as well as perturbed intercalated disc architecture and myocyte shape. This interaction appears to be regulated by glycogen synthase kinase 3 beta.
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