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Anti-CALML5 Antibody, Rabbit Polyclonal
Anti-CALML5 Antibody, Rabbit Polyclonal
- 中文名称：
- Anti-CALML5 Antibody, Rabbit Polyclonal
- 英文名称：
- Anti-CALML5 Antibody, Rabbit Polyclonal
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA259460
- 规格：
- 0.1 mL|2x0.1 mL|3x0.1 mL|4x0.1 mL|5x0.1 mL
- 保存建议：
- This antibody can be stored at 2 degree C-8 degree C for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20 degree C to -80 degree C. Avoid repeated freeze-thaw cycles.
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
- 货期：
- 6-8周
- 来源宿主：
- Rabbit
- 反应种属：
- Human
- 应用：
- IHC (Immunohistochemistry)
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 其他：
克隆性:Polyclonal
同型:Rabbit IgG
克隆号:N/A
特异性:Human CALML5
纯度:Protein A & Antigen Affinity
形式：Liquid; PBS, pH7.0 with 0.03% Proclin300
浓度：N/A
- 说明书：
Calmodulin-like protein 5, also known as Calmodulin-like skin protein, CALML5 and CLSP, is a protein which contains fourEF-hand domains. CALML5/CLSP is particularly abundant in the epidermis where its expression is directly related to keratinocyte differentiation. The expression is very low in lung. CALML5/CLSP binds calcium. It may be involved in terminal differentiation of keratinocytes. Coxsackievirus and adenovirus receptor (CAR) is a member of the immunoglobulin (Ig) superfamily and a component of epithelial tight junction. CAR functions as a primary receptor for coxsackievirus B and adenovirus (Ad) infection. CALML5/CLSP is closely related to CAR. The structure and dynamics of human calmodulin-like skin protein CALML5/CLSP have been characterized by NMR spectroscopy. The mobility of CALML5/CLSP has been found to be different for the N-terminal and C-terminal domains. The N-terminal domain is characterized by four stable helices, which experience large fluctuations. This is shown to be due to mutations in the hydrophobic core. The overall N-terminal domain behavior is similar both in the full-length protein and in the isolated domain.
