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产品名称:EpidermalFattyAcidBindingProtein5(AA2-135)(Active)protein(Histag)
产品型号:
产品厂商:ACROBiosystems
产品文档:
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简单介绍:
EpidermalFattyAcidBindingProtein5(AA2-135)(Active)protein(Histag)
详情介绍:
Product details
Product details
Characteristics
This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 16 kDa. The protein migrates as 16 kDa under reducing (R) condition (SDS-PAGE).
Purity
>95 % as determined by SDS-PAGE.
Sterility
0.22 μm filtered
Endotoxin Level
Less than 1.0 EU per μg by the LAL method.
Target details
Target details
Background
Fatty acid-binding protein 5 (FABP5), is also known as Fatty acid-binding protein, epidermal (E-FABP), Psoriasis-associated fatty acid-binding protein homolog (PA-FABP). FABP5 / E-FABP belongs to the calycin superfamily and fatty-acid binding protein (FABP) family. FABP5 / E-FABP is highly expressed in psoriatic skin. FABP5 / E-FABP has high specificity for fatty acids and has highest affinity for C18 chain length. FABP5 may be involved in keratinocyte differentiation.
Molecular Weight
16 kDa
UniProt
Q01469
Application Details
Application Details
Restrictions
For Research Use only
Handling
Handling
Format
Lyophilized
Reconstitution
Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer
PBS, pH 7.4
Handling Advice
Avoid repeated freeze-thaw cycles.
Storage
-20 °C
Storage Comment
No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Images
Images
Supplier Images
Human FABP5, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained ov...
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Human FABP5, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Human FABP5, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
References
References
Background publications
Gevaert, Goethals, Martens, Van Damme, Staes, Thomas, Vandekerckhove: "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
in:
Nature biotechnology
, Vol. 21, Issue 5, pp. 566-9, 2003 (PubMed).