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Key Documents

F8512

Sigma-Aldrich

Anti-Fibrinogen antibody produced in goat

whole antiserum

Sinonimo/i:

Anti-Fib2

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

goat

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

whole antiserum

Tipo di anticorpo

primary antibodies

Clone

polyclonal

contiene

15 mM sodium azide

Reattività contro le specie

human

tecniche

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

N° accesso UniProt

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

Descrizione generale

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.

Specificità

The antiserum has been determined to be immunospecific for fibrinogen by immunoelectrophoresis versus human plasma and fibrinogen.

Immunogeno

human fibrinogen

Applicazioni

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)

Azioni biochim/fisiol

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.

Nota sulla preparazione

treated to remove lipoproteins

Esclusione di responsabilità

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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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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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)
A quantitative immunoassay for lung cancer biomarker CIZ1b in patient plasma.
Coverley D, et al.
Clinical Biochemistry, 50(6), 336-343 (2017)
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)
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

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