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Fibrinogen antibody

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Published customer image:
Sheep anti Human fibrinogen antibody (4440-8004) used for the evaluation of fibrinogen deposition in mouse brain by immunofluorescence.
Image caption:
Inhibition of 2-AG hydrolysis reduces LPS-induced BBB permeability. a, b Fibrinogen levels in b plasma and the a ratio of brain to plasma fibrinogen were assessed by ELISA. n = 5/7 mice per group. c, d Fluorescent immunostaining in the striatum for fibrinogen (red) and vascular marker (CD31; green) demonstrated leakage of fibrinogen into the brain with vehicle treatment, whereas vascular integrity was preserved when (e, f) MAGL was inhibited. g Extravascular fibrinogen was semi-quantitated in fluorescently labeled sections of the striatum. Bar graphs were plotted with mean ±SEM and data analyzed using one-way analysis of variance (ANOVA) with Tukey post-hoc comparisons. n = 5/7 mice per group. Significance is shown as *p <0.05, **p <0.01. Scale bar = 20 μm.

From: Piro JR, Suidan GL, Quan J, Pi Y, O'Neill SM, Ilardi M, Pozdnyakov N, Lanz TA, Xi H, Bell RD, Samad TA.
Inhibition of 2-AG hydrolysis differentially regulates blood brain barrier permeability after injury.
J Neuroinflammation. 2018 May 14;15(1):142.
This image is from an open access article distributed under the terms of the Creative Commons Attribution License.

Sheep anti Human Fibrinogen:FITC

Product Type
Polyclonal Antibody
Isotype
Polyclonal IgG
Specificity
Fibrinogen

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4440-8004F
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Sheep anti Human fibrinogen antibody recognizes human fibrinogen, a complex ~340 kDa hetero-hexameric (di-trimeric) glycoprotein consisting of 3 pairs of α, β and γ chains linked by a series of 29 disulphide bonds (Henschen et al. 1983). The six chains are arranged in such a way that all the N-Terminal ends adjoin to form a central E domain with two trimeric coiled coil structures connecting to outer D domains. Fibrinogen plays an important role in the coagulation process with the D and E domains interacting via the C-Terminal ends of the α chains during fibrin clot cross-linking.

Sheep anti human fibrinogen antibody shows minimal cross-reactivity with related serum proteins. Fibrinogen has been identified as a ferritin binding protein in the horse (Orino et al. 1993). Sheep anti human fibrinogen antibody has been successfully as a capture reagent for ferritin - anti ferritin IgG complexes in horse plasma to evaluate the antibody response to ferritin by ELISA (Takahashi et al. 2013).

Target Species
Human
Species Cross-Reactivity
Target SpeciesCross Reactivity
Mouse
Rat
N.B. Antibody reactivity and working conditions may vary between species.
Product Form
Purified IgG conjugated to Fluorescein Isothiocyanate Isomer 1 (FITC) - liquid
Antiserum Preparation
Antisera to human fibrinogen were raised by repeated immunisations of sheep with highly purified antigen. Purified IgG was prepared from whole serum by affinity chromatography.
Buffer Solution
Phosphate buffered saline
Preservative Stabilisers
0.09%Sodium Azide (NaN3)
Immunogen
Human fibrinogen purified from plasma.
Approx. Protein Concentrations
IgG concentration 1.0mg/ml
Max Ex/Em
Fluorophore Excitation Max (nm) Emission Max (nm)
FITC 490 525
Regulatory
For research purposes only
Guarantee
12 months from date of despatch

This product is shipped at ambient temperature. It is recommended to aliquot and store at -20°C on receipt. When thawed, aliquot the sample as needed. Keep aliquots at 2-8°C for short term use (up to 4 weeks) and store the remaining aliquots at -20°C.

Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.

This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Application Name Verified Min Dilution Max Dilution
Immunofluorescence 1/10 1/100
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using the appropriate negative/positive controls.

References for Fibrinogen antibody

  1. Grainger, D.J. et al. (2001) Suppressing Thrombin Generation is Compatible With the Development of Atherosclerosis in Mice
    Thromb Res. 102: 71-80.
  2. Grainger, D.J. et al. (2004) Apolipoprotein E modulates clearance of apoptotic bodies in vitro and in vivo, resulting in a systemic proinflammatory state in apolipoprotein E-deficient mice.
    J Immunol. 173: 6366-75.
  3. Plskova, J. et al. (2004) Quantitative evaluation of the corneal endothelium in the mouse after grafting.
    Br J Ophthalmol. 88: 1209-16.
  4. Brill, A. et al. (2011) von Willebrand factor-mediated platelet adhesion is critical for deep vein thrombosis in mouse models.
    Blood. 117: 1400-7.
  5. Barrera, V. et al. (2011) Host fibrinogen stably bound to hemozoin rapidly activates monocytes via TLR-4 and CD11b/CD18-integrin: a new paradigm of hemozoin action.
    Blood. 117: 5674-82.
  6. Takahashi, K. et al. (2013) The presence of heat-labile factors interfering with binding analysis of fibrinogen with ferritin in horse plasma.
    Acta Vet Scand. 55: 70.
  7. Ozaltin, F. et al. (2013) DGKE variants cause a glomerular microangiopathy that mimics membranoproliferative GN.
    J Am Soc Nephrol. 24: 377-84.
  8. Chien, H.W. et al. (2013) Surface conjugation of zwitterionic polymers to inhibit cell adhesion and protein adsorption.
    Colloids Surf B Biointerfaces. 107: 152-9.
    9. View The Latest Product References
  9. Dmitrieva, N.I. and Burg, M.B. (2014) Secretion of von Willebrand factor by endothelial cells links sodium to hypercoagulability and thrombosis.
    Proc Natl Acad Sci U S A. 111: 6485-90.
  10. Johnsen, D. et al. (2016) Disrupting protein tyrosine phosphatase σ does not prevent sympathetic axonal dieback following myocardial infarction.
    Exp Neurol. 276: 1-4.
  11. Piro, J.R. et al. (2018) Inhibition of 2-AG hydrolysis differentially regulates blood brain barrier permeability after injury.
    J Neuroinflammation. 15 (1): 142.
  12. Huet, F. et al. (2020) Low-dose colchicine prevents sympathetic denervation after myocardial ischemia-reperfusion: a new potential protective mechanism
    Future Science OA. : FSO656.
  13. Sepe, J.J. et al. (2022) Therapeutics That Promote Sympathetic Reinnervation Modulate the Inflammatory Response After Myocardial Infarction.
    JACC Basic Transl Sci. 7 (9): 915-30.

Further Reading

  1. Kamath, S. & Lip, G.Y. (2003) Fibrinogen: biochemistry, epidemiology and determinants.
    QJM. 96 (10): 711-29.
  2. Mosesson, M.W. (2005) Fibrinogen and fibrin structure and functions.
    J Thromb Haemost. 3 (8): 1894-904.

Immunofluorescence

RRID
AB_961497
UniProt
P02671
P02675
P02679
Entrez Gene
FGA
FGB
FGG
GO Terms
GO:0002576 platelet degranulation
GO:0030674 protein binding, bridging
GO:0005102 receptor binding
GO:0007165 signal transduction
GO:0005577 fibrinogen complex
GO:0009897 external side of plasma membrane
GO:0030168 platelet activation
GO:0031093 platelet alpha granule lumen
GO:0043499 eukaryotic cell surface binding
GO:0051258 protein polymerization
GO:0051592 response to calcium ion
GO:0051087 chaperone binding
GO:0005625 soluble fraction

4440-8004F

155084 1803

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