Catalog: | C-EL-1721T |
Product Type: | Test kit |
Size: | 96 tests |
Principle: | Solid Phase Sandwich ELISA |
Conjugation: | HRP |
Species: | Human |
Detection range: | 23.44-1500 pg/mL |
Sensitivity: | 4.1 pg/mL |
Specificity: | Recognizes both recombinant and natural Human CALML5 |
Interference: | Preparations of PLK1 at 15 ng/mL in a mid-range recombinant human CALML5 control were assayed for interference. No significant interference was observed. |
Sample type: | Recombinant protein |
Test type: | Quantitative |
Analysis mode: | ELISA |
Shipping: | This ELISA Kit is shipped at ambient temperature. |
Storage: | 2-8℃ |
Full name: | calmodulin like 5 |
This CALML5 ELISA Kit, Human is an enzyme-linked immunosorbent assay for the quantitative measurement of Human CALML5 protein in Recombinant protein . It contains recombinant Human CALML5, and antibodies raised against the recombinant protein. This ELISA kit is complete and ready-to-use.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.
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