Comparison

SHEEP ANTI HUMAN FIBRINOGEN:FITC

Item no. 18-783-313981
Manufacturer GENWAY
Amount 1 ml
Category
Type Antibody
Applications IF
Specific against Human (Homo sapiens)
Host Sheep
ECLASS 10.1 32160702
ECLASS 11.0 32160702
UNSPSC 12352203
Alias GWB-259E02
Similar products 18-783-313981
Available
Genway ID:
GWB-259E02
Specificity:
FIBRINOGEN
Isotype:
Polyclonal IgGSpecies Cross Reactivity: Reacts with: Mouse RatN. B. Antibody reactivity and working conditions may vary between species.
Buffer Solution:
Phosphate buffered saline pH7. 4
Preservative Stabilisers:
0. 09% Sodium Azide (NaN3)Approx. Protein Concentrations: IgG concentration 1. 0mg/ml
Immunogen:
Native
Specificity:
Detects human fibrinogen a 340kDa soluble plasma glycoprotein which is synthesized by the liver. Fibrinogen is an inactive zymogen which is activated by thrombin in the coagulation cascade to form fibrin the most abundant component of blood clots. Fibrinogen activation is also involved in cellular and matrix interactions the inflammatory response cardiovascular disease and neoplasia.
Function:
Fibrinogen has a double
Function:
yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Subunit structureHeterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain. Ref. 18Subcellular locationSecreted. Tissue specificityPlasma. Ref. 26
Domain:
A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back contributing a fourth strand to the coiled coil structure. Post-translational modificationThe alpha chain is not glycosylated. Ref. 16Ref. 25Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue forming fibronectin-fibrinogen heteropolymers. About one-third of the alpha chains in the molecules in blood were found to be phosphorylated. Ref. 26Ref. 20Ref. 21Ref. 22Ref. 23Conversion of fibrinogen to fibrin is triggered by thrombin which cleaves fibrinopeptides A and B from alpha and beta chains and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. Phosphorylation sites are present in the extracelllular medium. Involvement in diseaseDefects in FGA are a cause of congenital afibrinogenemia [MIM:202400]. This is a rare autosomal recessive disorder characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias. Defects in FGA are a cause of amyloidosis type 8 (AMYL8) [MIM:105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1 fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome arterial hypertension hepatosplenomegaly cholestasis petechial skin rash. Ref. 36Sequence similaritiesContains 1 fibrinogen C-terminal domain. 1. Abrams J. et al. (1992) Strategies of anti-cytokine monoclonal antibody development: Immunoassay of IL-10 and IL-5 in clinical samples. Immunol. Rev. 127: 5-24. 2. Othieno C. et al. (1999) Interaction of mycobacterium tuberculosis - induced transforming growth factor beta 1 and interleukin-10. Infect. Immun. 67:5730-5735. [1] \" Isolation and expression of human cytokine synthesis inhibitory factor cDNA clones: homology to Epstein-Barr virus open reading frame BCRFI. \" Vieira P. de Waal-Malefyt R. Dang M. -N. Johnson K. E. Kastelein R. Fiorentino D. F. Devries J. E. Roncarolo M. -G. Mosmann T. R. Moore K. W. Proc. Natl. Acad. Sci. U. S. A. 88:1172-1176(1991) [PubMed: 1847510] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: T-cell. [2] \" The structure of the human IL-10 gene. \" Sanjanwala B. de Waal-Malefyt R. Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. [3] \" Cloning sequencing of human interleukin-10 cDNA and construction of its eukaryotic expression vector. \" Dai W. -J. Jiang H. -C. Pan S. -H. Haerbin Yi Ke Da Xue Xue Bao 35:4-6(2001)Cited for: NUCLEOTIDE SEQUENCE [MRNA]. [4] SeattleSNPs variation discovery resourceSubmitted (SEP-2001) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. [5] \" Identification of functional domains on human interleukin 10. \" Gesser B. Leffers H. Jinquan T. Vestergaard C. Kirstein N. Sindet-Pedersen S. Jensen S. L. Thestrup-Pedersen K. Larsen C. G. Proc. Natl. Acad. Sci. U. S. A. 94:14620-14625(1997) [PubMed: 9405662] [Abstract]Cited for: PROTEIN SEQUENCE OF 26-34 AND 170-178. [6] \" Signal peptide prediction based on analysis of experimentally verified cleavage sites. \" Zhang Z. Henzel W. J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract]Cited for: PROTEIN SEQUENCE OF 19-33. [7] \" Disulfide bond assignments and secondary structure analysis of human and murine interleukin 10. \" Windsor W. T. Syto R. Tsarbopoulos A. Zhang R. Durkin J. Baldwin S. Paliwal S. Mui P. W. Pramanik B. Trotta P. P. Biochemistry 32:8807-8815(1993) [PubMed: 8364028] [Abstract]Cited for: DISULFIDE BONDS. [8] \" Crystal structure of interleukin 10 reveals an interferon gamma-like fold. \" Walter M. R. Nagabhushan T. L. Biochemistry 34:12118-12125(1995) [PubMed: 7547951] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2. 0 ANGSTROMS). [9] \" Crystal structure of interleukin-10 reveals the functional dimer with an unexpected topological similarity to interferon gamma. \" Zdanov A. Schalk-Hihi C. Gustchina A. Tsang M. Wheatherbee J. Wlodawer A. Structure 3:591-601(1995) [PubMed: 8590020] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1. 8 ANGSTROMS). [10] \" Crystal structure of human interleukin-10 at 1. 6-A resolution and a model of a complex with its soluble receptor. \" Zdanov A. Schalk-Hihi C. Wlodawer A. Protein Sci. 5:1955-1962(1996) [PubMed: 8897595] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1. 6 ANGSTROMS).

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 1 ml
Available: In stock
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