Description
Recombinant Human CALML5/CLSP Protein (His & GST Tag) | PKSH031003 | Gentaur US, UK & Europe Disrtribition
Synonyms: CLSP
Active Protein: N/A
Activity: A DNA sequence encoding the human CALML5 (AAH39172.1) (Met 1-Glu 146) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
Protein Construction: A DNA sequence encoding the human CALML5 (AAH39172.1) (Met 1-Glu 146) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
Fusion Tag: N-His & GST
Species: Human
Expressed Host: E.coli
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 92 % as determined by reducing SDS-PAGE.
Endotoxin: Please contact us for more information.
Stability and 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.
Molecular Mass: 44.2 kDa
Formulation: Lyophilized from sterile 20mM Tris, 150mM NaCl, 1mM DTT, 0.5mM GSH, 10% glycerol, pH 7.8
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 four EF-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.
Research Area: N/A
