|Catalog||Size (Price)||Quantity||In Stock||Operation||Other Information|
Parvin, alpha Protein Datasheet
PARVA / Actopaxin Protein Price Inquiry ( Available Sizes )
PARVA / Actopaxin Protein Product Information
|Synonym :||PARVA, MXRA2|
A DNA sequence encoding the mature form of human PARVA(Q9NVD7-1) (Met1-Glu372) was fused with the GST tag at the N-terminus.
PARVA / Actopaxin Protein QC Testing
|Purity:||> 60 % as determined by SDS-PAGE||SDS-PAGE:
PARVA / Actopaxin protein
|Endotoxin:||Please contact us for more information.|
|Stability:||Samples are stable for up to twelve months from date of receipt at -70℃|
|Predicted N terminal:||Met|
The recombinant human PARVA /GST chimera consists of 606 amino acids and has a predicted molecular mass of 69.4 kDa. It migrates as an approximately 69 KDa band in SDS-PAGE under reducing conditions.
|Formulation:||Lyophilized from sterile PBS, pH7.4.
PARVA / Actopaxin Protein Usage Guide
|Storage:||Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|Reconstitution:||A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
PARVA / Actopaxin Protein Related Products & Topics
PARVA / Actopaxin Protein Description
Actopaxin, also known as alpha-parvin, is a member of the parvin family. It contains 2 CH (calponin-homology) domains and is widely expressed, with highest levels in heart, skeletal muscle, kidney and liver. It interacts with integrin-linked protein kinase and probably with actin and the LD1 and LD4 motifs of PXN. Actopaxin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Actopaxin binds directly to both F-actin and paxillin LD1 and LD4 motifs. Actopaxin binds directly to both F-actin and paxillin LD1 and LD4 motifs. Actopaxin also exhibits robust focal adhesion localization in several cultured cell types but is not found along the length of the associated actin-rich stress fibers. It is absent from actin-rich cell-cell adherens junctions.
- Korenbaum E. et al., 2002, Gene. 279 (1): 69-79.
- Nikolopoulos SN. et al., 2002, J Biol Chem. 277 (2): 1568-75.
- Tu Y. et al., 2001, J Cell Biol. 153 (3): 585-98.