F8512

Sigma-Aldrich

Anti-Fibrinogen antibody produced in goat

whole antiserum

MDL number:
NACRES:
NA.41

Quality Level

biological source

goat

antibody form

whole antiserum

antibody product type

primary antibodies

clone

polyclonal

contains

15 mM sodium azide

species reactivity

human

application(s)

indirect ELISA: 1:10,000
quantitative precipitin assay: 2.0 mg/mL

conjugate

unconjugated

UniProt accession no.

storage temp.

−20°C

Gene Information

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.

RIDADR

NONH for all modes of transport

WGK Germany

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Platelet adhesion and plasma protein adsorption control of collagen surfaces by He+ ion implantation.
Kurotobi K, et al.
Nucl. Instrum. Methods Phys. Res. Sect. B, 206(6), 532-537 (2003)
Ana L Flores-Mireles et al.
The Journal of urology, 196(2), 416-421 (2016-02-02)
Catheter associated urinary tract infections account for approximately 40% of all hospital acquired infections worldwide with more than 1 million cases diagnosed annually. Recent data from a catheter associated urinary tract infection animal model has shown that inflammation induced by...
N E Kirschbaum et al.
The Journal of biological chemistry, 265(23), 13669-13676 (1990-08-15)
The COOH-terminal portion of the A alpha chain of human fibrinogen is highly susceptible to proteolytic degradation. This property has prevented isolation of the COOH-terminal domain of fibrinogen for the direct investigation of its functional characteristics. Human fibrinogen was degraded...
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)
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)

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