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Recombinant Human GFAP Protein (His Tag)– MSE Supplies LLC

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Recombinant Human GFAP Protein (His Tag)

SKU: PKSH032490-50

  • $ 47095



Recombinant Human GFAP Protein (His Tag)

 

SKU # PKSH032490
Expression Host E.coli

 

 

Description

Synonyms GFAP, Glial Fibrillary Acidic Protein
Species Human
Expression Host E.coli
Sequence Leu292-Met432
Accession P14136
Calculated Molecular Weight 18.7 kDa
Observed Molecular Weight 17 kDa
Tag N-His
Bio-activity Not validated for activity
  

 

Properties

Purity > 95 % as determined by reducing SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method.
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 a 0.2 μm filtered solution of 20mM Tris-HCl, 10% Trehalose, 0.05% Tween 80, pH 8.5.
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

Glial Fibrillary Acidic Protein (GFAP) is an intermediate filament (IF) protein which belongs to the intermediate filament family. GFAP is expressed in numerous cell types of the central nervous system (CNS), ependymal cells and phosphorylated by PKN1. GFAP, a class-III intermediate filament, is a cell-specific marker during the development of the central nervous system and distinguishes astrocytes from other glial cells. It is closely related to its non-epithelial family members, vimentin, desmin, and peripherin, which are all involved in the structure and function of the cell’s cytoskeleton. GFAP is thought to help to maintain astrocyte mechanical strength, as well as the shape of cells but its exact function remains poorly understood.