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Product Name
Anti-CALML5 antibody
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Description
Rabbit monoclonal to CALML5
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Tested applications
IHC-P
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Species reactivity
Human CALML5
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Alternative names
CALML5 antibody; CLSP antibody
- Immunogen
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Isotype
Rabbit IgG
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Preparation
This antibody was obtained from a rabbit immunized with purified, recombinant Human CALML5 (rh CALML5; AAH39172.1; Met1-Glu146).
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Clonality
Monoclonal
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Formulation
0.2 μm filtered solution in PBS with 5% trehalose
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Storage instructions
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.
Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles. -
Applications
IHC-P: 0.5-5 μg/mL
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Validations
CALML5 Antibody, Rabbit MAb, Immunohistochemistry
Immunochemical staining of human CALML5 in human skin with rabbit monoclonal antibody (5 µg/mL, formalin-fixed paraffin embedded sections). Positive staining was localized to epithelium.
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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.
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References
- Mehul B., et al., 2000, J. Biol. Chem. 275:12841-12847.
- Babini E., et al., 2006, Structure 14:1029-1038.
- Kawabata,K. et al., 2007, Gene Ther. 14 (16):1199-207.
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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"