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MAB038
Sigma-AldrichAnti-Factor VIII Antibody, 83 kDa light chain
Anti-Factor VIII Antibody, 83 kDa light chain is an antibody against Factor VIII for use in ELISA & WB.
More>>Anti-Factor VIII Antibody, 83 kDa light chain is an antibody against Factor VIII for use in ELISA & WB. Less<<
SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Anti-Factor VIII Antibody, 83 kDa light chain is an antibody against Factor VIII for use in ELISA & WB.
Key Applications
ELISA
Western Blotting
Application Notes
ELISA (indirect): 1:16,000.
Western blotting: Factor VIII makes up only about 1% of the ciruculating FactorVIII/vWF complex with the bulk of the complex being vWF (99% by mass, see Blood 58:1-13, 1981). Thus it is recommended that the FactorVII/vWF be precipitated out of plasma prior to detection of Factor VII with MAB038. Also, when blotting plasma preparations, background, non-specific bands, caused by the serum proteins are common. More complex blocking solutions or higher salt concentrations can help remove non-specific bands. Rotblat, et al (1985) Biochemistry 24(16):4294-4300. Should be consulted for additional tips with regard to detecting Factor VII via westerns.
Optimal working dilutions must be determined by the end user.
Biological Information
Immunogen
Purified Human Factor VIII.
Epitope
83 kDa light chain
Host
Mouse
Specificity
By Western blot the antibody recognizes the 83 kDa light chain of human Factor VIII. No cross reactivity with von Willebrand factor.
This gene encodes coagulation factor VIII, which participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.
FUNCTION: SwissProt: P00451 # Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa. SIZE: 2351 amino acids; 267009 Da SUBUNIT: Interacts with VWF. VWF binding is essential for the stabilization of F8 in circulation. SUBCELLULAR LOCATION: Secreted, extracellular space. DOMAIN: SwissProt: P00451 Domain F5/8 type C 2 is responsible for phospholipid- binding and essential for factor VIII activity. DISEASE: SwissProt: P00451 # Defects in F8 are the cause of hemophilia A (HEMA) [MIM:306700]. HEMA is a common recessive X-linked coagulation disorder. The frequency of hemophilia A is 1-2 in 10,000 male births in all ethnic groups. About 50% of patients have severe hemophilia A with F8C activity less than 1% of normal; they have frequent spontaneous bleeding into joints, muscles and internal organs. Moderately severe hemophilia A occurs in about 10% of patients; F8C activity is 2-5% of normal, and there is bleeding after minor trauma. Mild hemophilia A, which occurs in 30-40% of patients, is associated with F8C activity of 5-30% and bleeding occurs only after significant trauma or surgery. Of particular interest for the understanding of the function of F8C is the category of CRM (cross-reacting material) positive patients (approximately 5%) that have considerable amount of F8C in their plasma (at least 30% of normal), but the protein is nonfunctional; i.e., the F8C activity is much less than the plasma protein level. CRM-reduced is another category of patients in which the F8C antigen and activity are reduced to approximately the same level. Most mutations are CRM negative, and probably affect the folding and stability of the protein. SIMILARITY: Belongs to the multicopper oxidase family. & Contains 3 F5/8 type A domains. & Contains 2 F5/8 type C domains. & Contains 6 plastocyanin-like domains.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Maintain at -20°C in undiluted aliquots for up to 12 months from date of receipt. Avoid repeated freeze/thaw cycles.
Combinatorial peptides directed to inhibitory antibodies against human blood clotting factor VIII. Eva-Maria Kopecky, Sabine Greinstetter, Ingrid Pabinger, Andrea Buchacher, Jürgen Römisch, Alois Jungbauer Thrombosis and haemostasis
94
933-41
2004
The development of antibodies against blood clotting factor VIII is a major complication affecting 20-30% of hemophilia A patients receiving replacement with FVIII concentrates.This study investigated generating peptides acting as broadly neutralizing agents to block factor VIII antibodies.These peptides were selected from dual positional scanning decapeptide libraries on cellulose membranes. From this library comprising 6.8 x 10(12) peptides we selected 468 peptides for further screening rounds. Finally we identified two decapeptides with the ability to block 8 out of 10 inhibitory antibodies from sera of patients with FVIII inhibitors demonstrated by competition assays. Sequence alignment of the peptides showed similarity with several domains in the FVIII molecule demonstrating the mimotope nature of the selected peptides. Our results show the efficiency of the combinatorial library approach and show the potential of combinatorial peptides to compete out polyclonal inhibitor IgG from a broad range of patients' sera. Combinatorial peptides could be novel and highly effective drug candidates for alternative treatment in patients with factor VIII inhibitors.
Binding of factor VIII inhibitors to discrete regions of the factor VIII C2 domain disrupt phospholipid binding. Deborah A Lewis, Karen D Moore, Thomas L Ortel Blood coagulation fibrinolysis : an international journal in haemostasis and thrombosis
14
361-8
2003
We characterized seven factor VIII inhibitors with epitopes in the C2 domain of factor VIII using a series of factor V C2 domain chimeras that substituted exon-sized fragments of the C2 domain of factor VIII for the corresponding regions of factor V. All inhibited co-factor activity of factor VIII and six inhibited binding of factor VIII to phosphatidylserine. Inhibitors Hz, JN and GK32 bound epitopes within amino acids S2173-K2281; inhibitors GK24 and TO bound epitopes within amino acids V2223-Y2332; and inhibitors UNC11 and UNC12 bound epitopes throughout the C2 domain (amino acids S2173-Y2332). Inhibitors Hz, JN and UNC12 inhibited the co-factor activity of chimera 5A, which substituted amino acids S2173-Q2222 of factor VIII for the corresponding region of factor V, in a prothrombinase assay. This inhibition could be partially reversed by pre-incubation of chimera 5A with phospholipid vesicles, suggesting that these antibodies interfered with phospholipid binding. Inhibitors UNC11 and UNC12, on the other hand, did not inhibit the binding of chimera 1 A to phosphatidylserine, suggesting that binding to the segment spanning amino acids V2282-Y2332 does not necessarily block phospholipid binding. These results agree with the model of the phospholipid-binding site determined by crystal structure of the C2 domain of factor VIII.
