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Recombinant Human CALML5/CLSP Protein (His & GST Tag)
SKU: PKSH031003-100
Recombinant Human CALML5/CLSP Protein (His & GST Tag)
| SKU # | PKSH031003 |
| Expression Host | E.coli |
Description
| Synonyms | CLSP |
| Species | Human |
| Expression Host | E.coli |
| Sequence | Met 1-Glu 146 |
| Accession | AAH39172.1 |
| Calculated Molecular Weight | 44.2 kDa |
| Observed Molecular Weight | 43 kDa |
| Tag | N-His-GST |
| Bio-activity | Not validated for activity |
Properties
| Purity | > 92 % as determined by reducing SDS-PAGE. |
| Endotoxin | Please contact us for more information. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation | Lyophilized from sterile 20mM Tris, 150mM NaCl, 1mM DTT, 0.5mM GSH, 10% glycerol, pH 7.8 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
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.