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-Calnexin (N-terminal region) Antibody
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, ICC |
|---|---|
| Primary Accession | P27824 |
| Host | Mouse |
| Clonality | Mouse Monoclonal |
| Isotype | IgG1 |
| Clone Names | M437 |
| Calculated MW | 67568 Da |
| Gene ID | 821 |
|---|---|
| Other Names | IP90, P90 |
| Target/Specificity | Calnexin is a 90 kDa integral membrane protein located primarily in the endoplasmic reticulum (ER). The structure of calnexin includes a long N-terminal calcium-binding domain that extends into the lumen of the ER and a short, acidic cytosolic domain. Calnexin associates with several cell surface proteins as they pass through the ER, and may be involved in the Ca2+-dependent retention of proteins in the ER. The amino acid sequence of calnexin is highly conserved among various species and is similar in sequence to calreticulin, another Ca2+-binding protein found in the ER. Phosphorylation may regulate the activity of the C-terminal region of Calnexin. Both proline-dependent kinase and casein kinase sites have been identified, and the phosphorylation of these sites may regulate calnexin functions involved with detection of ER protein quality control and transport. |
| Dilution | WB~~1:1000 ICC~~N/A |
| Format | Protein A Purified |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Anti-Calnexin (N-terminal region) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Calnexin is a 90 kDa integral membrane protein located primarily in the endoplasmic reticulum (ER). The structure of calnexin includes a long N-terminal calcium-binding domain that extends into the lumen of the ER and a short, acidic cytosolic domain. Calnexin associates with several cell surface proteins as they pass through the ER, and may be involved in the Ca2+-dependent retention of proteins in the ER. The amino acid sequence of calnexin is highly conserved among various species and is similar in sequence to calreticulin, another Ca2+-binding protein found in the ER. Phosphorylation may regulate the activity of the C-terminal region of Calnexin. Both proline-dependent kinase and casein kinase sites have been identified, and the phosphorylation of these sites may regulate calnexin functions involved with detection of ER protein quality control and transport.
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