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F8512

Sigma-Aldrich

Anti-Fibrinogen antibody produced in goat

whole antiserum

Synonym(s):

Anti-Fib2

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

goat

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

Gene Information

Related Categories

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

12 - Non Combustible Liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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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
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)
Marissa Jeme Andersen et al.
eLife, 11 (2022-03-30)
Microbial adhesion to medical devices is common for hospital-acquired infections, particularly for urinary catheters. If not properly treated these infections cause complications and exacerbate antimicrobial resistance. Catheter use elicits bladder inflammation, releasing host serum proteins, including fibrinogen (Fg), into the
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

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