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Recombinant Human FAP protein (His Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

His Tag

Activity

not tested

Cat no : Eg0821


Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity
Not tested
Expression HEK293-derived Human FAP protein Leu26-Asp760 (Accession# Q12884-1) with a His tag at the N-terminus.
GeneID 2191
Accession Q12884-1
PredictedSize 86.1 kDa
SDS-PAGE 80-95 kDa, reducing (R) conditions
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

FAP, also known as fibroblast activation protein-alpha (FAP-alpha) is a cell surface glycoprotein serine protease, which can participate in extracellular matrix degradation and is involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. FAP is a single transmembrane protein that locates the cytoplasm and plasma membrane. Immunohistochemical studies have shown that FAP is transiently expressed in certain normal fetal mesenchymal tissues but that normal adult tissues as well as malignant epithelial, neural, and hematopoietic cells are generally FAP-negative. However, most of the common types of epithelial cancers contain abundant FAP-reactive stromal fibroblasts.

References:

1. Lee, Kyung N et al. Blood vol. 103,10 (2004): 3783-8. 2. Lee, Kyung N et al. Blood vol. 107,4 (2006): 1397-404. 3. Scanlan, M J et al. Proceedings of the National Academy of Sciences of the United States of America vol. 91,12 (1994): 5657-61.


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