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-L1CAM (Extracellular) Antibody
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, ICC, IP |
|---|---|
| Primary Accession | P32004 |
| Host | Mouse |
| Clonality | Mouse Monoclonal |
| Isotype | IgG1 |
| Clone Names | M023 |
| Calculated MW | 140003 Da |
| Gene ID | 3897 |
|---|---|
| Other Names | Neural cell adhesion molecule L1, N-CAM-L1, CD171, L1CAM, CAML1, MIC5 |
| Target/Specificity | The basal lamina contains Collagen Type IV, proteoglycans, and glycoproteins. Laminin is a high molecular weight (850 kDa) oligomer, consisting of three different chains (α, β, and γ) joined by disulfide bonds. The structure of laminins include two helical domains (I & II) at the COOH-terminal, a laminin IV domain, multiple EGF-like repeats, and a laminin globular domain (G), as well as an N-terminal domain VI. Domains IV and VI are the binding sites for collagen and heparan sulfate, respectively. Several isoforms have been identified for the genes of each chain. Laminin γ1 (laminin B2) contains 14 glycosylation sites and 12 cysteine repeat domains. The expression of the Laminin subunits is found in the basal lamina of tissues. Here, the protein interacts with other extracellular matrix components to mediate cell attachment, migration and organization during embryonic development. |
| Dilution | WB~~1:1000 ICC~~N/A IP~~N/A |
| 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-L1CAM (Extracellular) 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
The basal lamina contains Collagen Type IV, proteoglycans, and glycoproteins. Laminin is a high molecular weight (850 kDa) oligomer, consisting of three different chains (α, β, and γ) joined by disulfide bonds. The structure of laminins include two helical domains (I & II) at the COOH-terminal, a laminin IV domain, multiple EGF-like repeats, and a laminin globular domain (G), as well as an N-terminal domain VI. Domains IV and VI are the binding sites for collagen and heparan sulfate, respectively. Several isoforms have been identified for the genes of each chain. Laminin γ1 (laminin B2) contains 14 glycosylation sites and 12 cysteine repeat domains. The expression of the Laminin subunits is found in the basal lamina of tissues. Here, the protein interacts with other extracellular matrix components to mediate cell attachment, migration and organization during embryonic development.
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