SREBF chaperone Protein (SCAP) (DYKDDDDK Tag)
Quick Overview for SREBF chaperone Protein (SCAP) (DYKDDDDK Tag) (ABIN7596504)
Target
See all SREBF chaperone (SCAP) ProteinsProtein Type
Origin
Source
Application
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Purification tag / Conjugate
- This SREBF chaperone protein is labelled with DYKDDDDK Tag.
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Purpose
- Human SCAP full length protein-synthetic nanodisc
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Comment
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Advantages:
- Highly purified membrane proteins
- High solubility in aqueous solutions
- High stability
- Proteins are in a native membrane environment and remain biologically active
- No detergent and can be used for cell-based assays
- No MSP backbone proteins
- Mammalian cell expression system ensures post- translational modifications
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Restrictions
- For Research Use only
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Format
- Lyophilized
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Buffer
- Solubilization buffer (20 mM Tris-HCl, 150 mM NaCl, pH 8.0). Normally 5% – 8% trehalose is added as protectants before lyophilization.
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Storage
- -20 °C,-80 °C
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Storage Comment
- Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing). Lyophilized proteins are shipped at ambient temperature.
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Expiry Date
- 12 months
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- SREBF chaperone (SCAP)
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Alternative Name
- SCAP
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Background
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N/A
A protein with a sterol sensing domain (SSD) and seven WD domains. In the presence of cholesterol, this protein binds to sterol regulatory element binding proteins (SREBPs) and mediates their transport from the ER to the Golgi. The SREBPs are then proteolytically cleaved and regulate sterol biosynthesis. -
Molecular Weight
- The human full length SCAP protein has a MW of 139.7 kDa
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UniProt
- Q12770
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Pathways
- SARS-CoV-2 Protein Interactome
Target
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