Factor VIIa Active Protein
Factor VIIa, Human
Purity
Affinity PurifiedPurified by immunoaffinity chromotography of Factor VII. Followed by by Ion Exchange chromatography. Purified Factor VII is activated to Factor VIIa. The purity is determined by SDS-PAGE analysis.
Synonyms
Factor VIIa; Human; Factor VIIa active protein
Host
Human plasma
Purity/Purification
Affinity Purified
Purified by immunoaffinity chromotography of Factor VII. Followed by by Ion Exchange chromatography. Purified Factor VII is activated to Factor VIIa. The purity is determined by SDS-PAGE analysis.
Purified by immunoaffinity chromotography of Factor VII. Followed by by Ion Exchange chromatography. Purified Factor VII is activated to Factor VIIa. The purity is determined by SDS-PAGE analysis.
Form/Format
Supplied as a liquid in 50% glycerol, H2O
Specific Activity
~16,000 units/mg, Determined from single stage clotting assay
Mode of Action
Enzyme component of the extrinsic factor X activating complex; also activates factor IX, thus by-passing the contact activation system.
Structure
Two subunits; NH2-terminal derived light chain (Mr=20,000), COOH-terminal derived heavy chain (Mr=30,000), NH2-terminal gla-domain, two EGF domains
Percent Carbohydrate
~13%
Post-translational Modifications
One b-hydroxyaspartate (11), ten gla residues (12)
Preparation and Storage
May be stored at 4 degree C for short-term only. For long-term storage, store at -20 degree C. Aliquots are stable for at least 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Related Product Information for Factor VIIa active protein
Participation of Factor VIIa in the Extrinsic Factor Xase Complex: Factor VIIa and its cofactor tissue factor (TF) assemble on a negatively charged membrane surface in a calcium dependent manner to form an enzyme complex which proteolytically converts factor X to factor Xa. The complex is referred to as the extrinsic factor Xase complex, because the tissue factor component is presumably derived from a source "extrinsic" to the plasma environment, which is accessible following vascular injury.
The conversion of factor VII to factor VIIa is catalyzed by a number of proteases including thrombin, factor IXa, factor Xa, factor XIa, and factor XIIa. Rapid activation also takes place when factor VII is combined with tissue factor in the presence of calcium (5-9). This latter event is consistent with autocatalysis, and is likely initiated by a small amount of pre-existing factor VIIa. The activation reaction results in cleavage of the peptide bond between arginine 152 and isoleucine 153.
The resulting factor VIIa consists of an NH2-derived light chain (Mr=20,000), and a COOH-terminal derived heavy chain (Mr= 30,000), which remain associated through a single disulfide bond (cys135-cys262). The light chain contains the membrane binding "Gla domain", while the heavy chain contains the catalytic domain.
Unlike other serine proteases, factor VIIa alone is not readily inhibited by the antithrombin III/heparin complex. However, in the presence of tissue factor, antithrombin III/heparin exhibits significant inhibition of factor VIIa (6).
The conversion of factor VII to factor VIIa is catalyzed by a number of proteases including thrombin, factor IXa, factor Xa, factor XIa, and factor XIIa. Rapid activation also takes place when factor VII is combined with tissue factor in the presence of calcium (5-9). This latter event is consistent with autocatalysis, and is likely initiated by a small amount of pre-existing factor VIIa. The activation reaction results in cleavage of the peptide bond between arginine 152 and isoleucine 153.
The resulting factor VIIa consists of an NH2-derived light chain (Mr=20,000), and a COOH-terminal derived heavy chain (Mr= 30,000), which remain associated through a single disulfide bond (cys135-cys262). The light chain contains the membrane binding "Gla domain", while the heavy chain contains the catalytic domain.
Unlike other serine proteases, factor VIIa alone is not readily inhibited by the antithrombin III/heparin complex. However, in the presence of tissue factor, antithrombin III/heparin exhibits significant inhibition of factor VIIa (6).
Product Categories/Family for Factor VIIa active protein
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Product Notes
The Factor VIIa (Catalog #AAA634657) is an Active Protein produced from Human plasma and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "Factor VIIa, Active Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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