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DOMAIN STRUCTURE OF HUMAN FACTOR VII The domain structure of human factor VII is represented, where: GLA = region
containing γ-carboxyglutamic acid residues, EGF = region containing sequences homologous to human epidermal growth factor, CATALYTIC DOMAIN = region containing the serine protease catalytic triad. The site at which factor Xa cleaves factor VII to form factor VIIa is indicated with an arrow.
PURCHASING
AND PRODUCT INFORMATION
|
Catalog
Number
HCVII-0030 |
Description
Human Factor VII |
Size
20
µg |
Formulation
50% (vol/vol) glycerol/H2O |
|
Storage
-20oC |
Purity
>95%
by SDS-PAGE |
Activity
Determination
Clotting
assay |
Shelf
Life (properly stored)
12
months |
 |
Sample Gel
Information:
Gel:
Novex 4-12% Bis-Tris
Load:
Human Factor VII, 1 µg per lane
Buffer:
MOPS
Standard:
SeeBluePlus 2; Myosin (191 kDa), Phosphorylase B (97 kDa), BSA (64
kDa), Glutamic Dehydrogenase (51 kDa), Alcohol Dehydrogenase (39 kDa),
Carbonic Anhydrase (28 kDa), Myoglobin Red (19 kDa), Lysozyme (14
kDa)
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Overview
of Factor VII
Human factor VII is a single chain, vitamin K-dependent, plasma glycoprotein which is synthesized in the liver (1-3). Prior to secretion into the blood, post translational modification by a vitamin K-dependent carboxylase produces ten-carboxyglutamic acid (gla) residues located in the
NH2-terminal portion of the molecule, which facilitate cell membrane binding. Factor VII is proteolytically activated to the serine protease,
factor VIIa, during coagulation. Factor VII can be activated by
thrombin, factor
IXa, factor Xa or factor XIIa. The activation results in cleavage of the single chain molecule on the COOH-terminal side of arginine-152, to produce an
NH2-terminal derived light chain (Mr=20,000) and a COOH-terminal derived heavy chain (Mr=30,000) which remain covalently associated by a single disulfide bond. The light chain region contains the gla domain, as well as two growth factor domains which are homologous to human epidermal growth factor (EGF). A single
β-hydroxyaspartic acid identified in factor VII is also located in the light chain region. The heavy chain region of factor VIIa contains the catalytic domain. Factor VIIa and the cofactor, tissue factor, may combine on negatively charged cell surfaces in a calcium dependent manner to form the extrinsic factor Xase enzyme complex. This enzyme complex catalyzes the conversion of both
factor IX to factor IXa and factor X
to factor Xa. The cDNA for factor VII has been isolated and the nucleotide sequence determined (4). Factor VII shares extensive sequence homology with other serine proteases including factor IX, factor X and
protein C.
Human factor VII is purified using a combination of conventional techniques (2) and immunoaffinity chromatography (5). The purified protein is supplied in 50% (vol/vol) glycerol/H2O and should be stored at
-20oC. Purity is determined by SDS-PAGE analysis and activity is measured in a factor VII clotting assay.
Properties of Factor VII
| Localization: |
Plasma |
| Plasma concentration: |
0.5 µg/ml* (2) |
| Mode of action: |
Zymogen; precursor to the serine protease factor VIIa |
| Molecular weight: |
50,000 (2) |
| Extinction coefficient: |
|
| Isoelectric point: |
4.8-5.1** (6) |
| Structure: |
single chain, NH2-terminal
gla-domain, two EGF domains |
| Percent carbohydrate: |
13%** (7) |
| Post-translational modifications: |
one
β-hydroxyaspartate (8), ten gla residues (9) |
* based upon activity measurements
** based upon analysis of bovine factor VII
PURCHASING
AND PRODUCT INFORMATION
|
Catalog
Number
HCVII-0030 |
Description
Human Factor VII |
Size
20
µg |
Formulation
50% (vol/vol) glycerol/H2O |
|
Storage
-20oC |
Purity
>95%
by SDS-PAGE |
Activity
Determination
Clotting
assay |
Shelf
Life (properly stored)
12
months |
|
U.S.
Pricing |
Product
inquiry |
SAMPLE
DATA SHEET |
ORDER
NOW! |
References
1. Davie, E.W., et al., Adv. Enzymol., 48, 277 (1979).
2. Bajaj, S.P., et al., J. Biol. Chem., 256, 253 (1981).
3. Broze, G.J., et al., J. Biol. Chem., 255, 1242 (1980).
4. Hagen, F.S., et al., Proc. Natl. Acad. Sci., USA, 83, 2412 (1986).
5. Jenny, R.J., et al., Prep. Biochem., 16, 227 (1986).
6. Discipio, R.G., et al., Biochemistry, 18, 899 (1979).
7. Kisiel, W., et al., Biochemistry, 14, 4928 (1975).
8. McMullen, B.A., et al., BBRC, 115, 8 (1983).
9. Discipio, R.G., et al., Biochemistry, 16, 698 (1977).
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