Recombinant CALML5 Monoclonal Antibody (AN300242P)
For research use only.
| Verified Samples |
Verified Samples in IF: A431 Verified Samples in FCM: A431 |
| Dilution | ICC/IF 1:20-1:100, FCM 1:25-1:100, |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human |
| Applications | FCM, ICC/IF |
| Clonality | Rabbit Monoclonal |
| Immunogen | Recombinant Human CALML5 protein |
| Abbre | CALML5 |
| Synonyms | Calmodulin like, Calmodulin-like protein, CALML, CALL5_HUMAN, Calmodulin like 5, Calmodulin-like protein 5, Calmodulin-like skin protein, CLSP, CALML5 |
| Swissprot | |
| Concentration | 1 mg/mL |
| Buffer | 0.2 μm filtered solution in PBS |
| Purification Method | Protein A |
| Research Areas | Signal Transduction, Cell Biology |
| Clone No. | 5F5 |
| Conjugation | Unconjugated |
| Storage | This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles. |
| Shipping | Ice bag |
| background | 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. |
Other Clones
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Unconjugated
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