F8512
Anti-Fibrinogen antibody produced in goat
whole antiserum
Synonym(s):
Anti-Fib2
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2 ML
€196.00
About This Item
Recommended Products
biological source
goat
Quality Level
conjugate
unconjugated
antibody form
whole antiserum
antibody product type
primary antibodies
clone
polyclonal
contains
15 mM sodium azide
species reactivity
human
technique(s)
indirect ELISA: 1:10,000
quantitative precipitin assay: 2.0 mg/mL
UniProt accession no.
storage temp.
−20°C
target post-translational modification
unmodified
General description
Fibrinogen is a thrombin-coagulable soluble plasma 340 kDa glycoprotein, composed of paired sets of three subunits i.e. α, β, γ. It plays a crucial role in protecting the vascular network against the loss of blood after tissue injury. Among three subunits, β and γ subunits contain one N-glycosylation site, which is occupied by a biantennary N-glycan. It contains three pairs of disulfide-bonded chains called α, β and γ which further folded into four structural domains: the D, E, connector, and the COOH-terminal region of the Aα chain.
The fibrinogen gene cluster consists of fibrinogen α, β and γ chains. It is localized on human chromosome locus 4q31.3−4q32.1.
Specificity
The antiserum has been determined to be immunospecific for fibrinogen by immunoelectrophoresis versus human plasma and fibrinogen.
Immunogen
human fibrinogen
Application
Anti-Fibrinogen antibody is suitable for immunostaining in fibrin deposition analysis of mouse livers and capturing antibodies in the sandwich ELISA. It is also suitable for indirect ELISA at a dilution of 1:10,000 and quantitative precipitin assay at 2.0mg/mL concentration.
Anti-Fibrinogen antibody produced in goat has been used in:
- western blotting detection in human colon adenocarcinoma cell line
- detecting fibrinogen in plasma
- immunoassay of human platelet free plasma (PFP)
Biochem/physiol Actions
Plasmin attacks the Aα chain COOH domain to produce the heterogeneous fragment X. Multiple round of degradation ended with terminal digestion products−fragments D and E which represent the major globular domains in fibrinogen. Mutations in this gene lead to several disorders, including hypofibrinogenemia and afibrinogenemia.
Preparation Note
treated to remove lipoproteins
Disclaimer
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.
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Storage Class Code
12 - Non Combustible Liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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A quantitative immunoassay for lung cancer biomarker CIZ1b in patient plasma.
Coverley D, et al.
Clinical Biochemistry, 50(6), 336-343 (2017)
Congenital afibrinogenaemia caused by uniparental isodisomy of chromosome 4 containing a novel 15-kb deletion involving fibrinogen Aalpha-chain gene.
Spena S, et al.
European Journal of Human Genetics, 12(11), 891-891 (2004)
Integrin alphavbeta6 mediates HT29-D4 cell adhesion to MMP-processed fibrinogen in the presence of Mn2+.
Fouchier F, et al.
European Journal of Cell Biology, 86(3), 143-160 (2007)
Dawn Coverley et al.
Clinical biochemistry, 50(6), 336-343 (2016-11-22)
Non-invasive tests for early detection of lung cancer are an important unmet clinical need. CIZ1b plasma biomarker can discriminate stage 1 lung cancer from within high-risk groups with clinically useful accuracy, with ROC AUCs in excess of 0.9 for two
Targeting the Mitochondrial Chaperone TRAP1 Alleviates Vascular Pathologies in Ischemic Retinopathy.
So-Yeon Kim et al.
Advanced science (Weinheim, Baden-Wurttemberg, Germany), 11(2), e2302776-e2302776 (2023-11-20)
Activation of hypoxia-inducible factor 1α (HIF1α) contributes to blood-retinal barrier (BRB) breakdown and pathological neovascularization responsible for vision loss in ischemic retinal diseases. During disease progression, mitochondrial biology is altered to adapt to the ischemic environment created by initial vascular
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