Name :
Recombinant Human FAP Protein (ECD, His & AVI Tag), Biotinylated, HPLC-verified
Biological Activity :
Background :
Seprase, also known as 17 kDa melanoma membrane-bound gelatinase , Fibroblast activation protein alpha, Integral membrane serine protease and FAP, is a single-pass type II membrane protein which belongs to thepeptidase S9B family. Seprase / FAP is found in cell surface lamellipodia, invadopodia and on shed vesicles. Seprase / FAP appears to act as a proteolytically active 17-kDa dimer, consisting of two 97-kDa subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. Seprase / FAP colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Seprase / FAP colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. In association with DPP4, Seprase / FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. Seprase / FAP has a dual function in tumour progression. The proteolytic activity of Seprase has been shown to promote cell invasiveness towards the ECM and also to support tumour growth and proliferation. Seprase / FAP may have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers. Cancer Immunotherapy Immune Checkpoint Immunotherapy Targeted Therapy
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
HEK293 Cells
Tag :
Protein Accession No. :
Q12884-1
NCBI Gene ID :
Synonyms :
Synonyms :
fibroblast activation protein, alpha
Amino Acid Sequence :
Molecular Weight :
The recombinant Human FAP consists of 760 amino acids and predicts a molecular mass of 88.23 kDa. It migrates as an approximately 102.0 kDa band in SDS-PAGE under reducing conditions.
Purity :
≥ 95 % as determined by SDS-PAGE. ≥ 90 % as determined by SEC-HPLC.
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg protein as determined by the LAL method.
Protein Construction :
A DNA sequence encoding the Human FAP (Q12884-1) (Leu26-Asp760) was expressed with a N-terminal polyhistidine tag followed by an AVI tag.The expressed protein was biotinylated in vivo by the Biotin-Protein ligase (BirA enzyme) which is co-expressed.
Buffer Solution :
Supplied as sterile 25mM Tris, 250mM NaCl, 10% Glycerol, pH 8.2.Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
Liquid. It is shipped out with blue ice.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
DPPIV Protein, Human; DPPIVA Protein, Human; FAPA Protein, Human; Fapalpha Protein, Human; Fibroblast Activation Protein alpha Protein, Human; SIMP Protein, Human FAP 背景信息 Seprase, also known as 17 kDa melanoma membrane-bound gelatinase , Fibroblast activation protein alpha, Integral membrane serine protease and FAP, is a single-pass type II membrane protein which belongs to thepeptidase S9B family. Seprase / FAP is found in cell surface lamellipodia, invadopodia and on shed vesicles. Seprase / FAP appears to act as a proteolytically active 17-kDa dimer, consisting of two 97-kDa subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. Seprase / FAP colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Seprase / FAP colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. In association with DPP4, Seprase / FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. Seprase / FAP has a dual function in tumour progression. The proteolytic activity of Seprase has been shown to promote cell invasiveness towards the ECM and also to support tumour growth and proliferation. Seprase / FAP may have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers. Cancer Immunotherapy Immune Checkpoint Immunotherapy Targeted Therapy
References & Citations :
Mori,Y. et al., 2004, Oncology. 67 (5-6):411-9. Aertgeerts K., et al., 2005, J. Biol. Chem. 280:19441-19444. Liu T., et al., 2005, J. Proteome Res. 4:2070-2080. Ghersi G., et al., 2006, Cancer Res. 66:4652-4661. O’Brien,P. et al., 2008, Biochim Biophys Acta. 1784 (9):1130-45.
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