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F3254

Sigma-Aldrich

Fibrinopeptide A human

≥96% (HPLC)

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About This Item

Empirical Formula (Hill Notation):
C63H97N19O26
CAS Number:
25422-31-5
Molecular Weight:
1536.56
MDL number:
MFCD00076437
UNSPSC Code:
12352202
PubChem Substance ID:
24894837
NACRES:
NA.77

biological source

human

Quality Level

200

Assay

≥96% (HPLC)

form

powder

technique(s)

ELISA: suitable
mass spectrometry (MS): suitable

UniProt accession no.

P02671

storage temp.

−20°C

SMILES string

CC(C)CC(NC(=O)C(Cc1ccccc1)NC(=O)C(CC(O)=O)NC(=O)CNC(=O)C(CCC(O)=O)NC(=O)CNC(=O)C(CO)NC(=O)C(CC(O)=O)NC(=O)C(C)N)C(=O)NC(C)C(=O)NC(CCC(O)=O)C(=O)NCC(=O)NCC(=O)NCC(=O)NC(C(C)C)C(=O)NC(CCCNC(N)=N)C(O)=O

InChI

1S/C63H97N19O26/c1-29(2)19-37(57(102)73-32(6)53(98)76-35(15-17-48(91)92)55(100)70-24-43(85)68-23-42(84)69-25-46(88)82-51(30(3)4)61(106)77-36(62(107)108)13-10-18-67-63(65)66)79-58(103)38(20-33-11-8-7-9-12-33)80-59(104)39(21-49(93)94)75-45(87)27-71-54(99)34(14-16-47(89)90)74-44(86)26-72-56(101)41(28-83)81-60(105)40(22-50(95)96)78-52(97)31(5)64/h7-9,11-12,29-32,34-41,51,83H,10,13-28,64H2,1-6H3,(H,68,85)(H,69,84)(H,70,100)(H,71,99)(H,72,101)(H,73,102)(H,74,86)(H,75,87)(H,76,98)(H,77,106)(H,78,97)(H,79,103)(H,80,104)(H,81,105)(H,82,88)(H,89,90)(H,91,92)(H,93,94)(H,95,96)(H,107,108)(H4,65,66,67)

InChI key

JWICNZAGYSIBAR-UHFFFAOYSA-N

Gene Information

human ... FGA(2243)

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Amino Acid Sequence

Ala-Asp-Ser-Gly-Glu-Gly-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg

General description

Fibrinopeptide A (FPA) is produced from the N-terminal Aα region of fibrinogen protein, on cleavage by thrombin. It is composed of 16 amino acids.

Application

Fibrinopeptide A human has been used for protein control experiments performed during sandwich ELISA microarray assay to distinguish between plasma and serum fibrinogen samples. It has also been used in a peptide mixture along with BSA (bovine serum albumin) to ascertain the relation between fragmentation voltage and peptide ion drift time for IMS-MS (ion mobility spectrometry coupled with mass spectrometry).

Biochem/physiol Actions

Fibrinogen plays essential roles in coagulation of blood, wound healing, platelet aggregation and has roles in various other physiological processes. Increase in the levels of fibrinopeptide A (FPA) is found in multiple disorders such as coronary artery disease, disseminated intravascular coagulation, arterial thrombosis, deep venous thrombosis and cancers.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Xi Chen et al.
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Laura A Da Costa et al.
The Journal of nutritional biochemistry, 24(1), 396-400 (2012-12-04)
Vitamin E is a lipophilic antioxidant that has been inversely associated with certain chronic diseases; however, the biological processes regulated by this vitamin have not been fully elucidated. The objective of the present study was to examine the association between
H L Nossel et al.
The Journal of clinical investigation, 54(1), 43-53 (1974-07-01)
Since thrombin cleaves fibrinopeptides A (FPA) and B from the NH(2)-terminal end of the fibrinogen molecule, measurement of fibrinopeptide levels in plasma may provide a direct index of thrombin action. Recently a radioimmunoassay for FPA has been developed, and in
J I Weitz
Thrombosis and haemostasis, 75(4), 529-535 (1996-04-01)
There is good evidence that thrombolytic therapy induces a procoagulant state that retards the lytic process and triggers reocclusion. Thus, both in experimental animal systems and in humans, potent inhibitors of platelets and antithrombin III-independent thrombin inhibitors have been shown
Reidun Øvstebø et al.
Innate immunity, 18(4), 580-591 (2011-12-20)
Neisseria meningitidis causes sepsis with coagulopathy. The present study evaluated the tissue factor (TF)-inducing capacity of bacterial LPS in different presentation forms, i.e. membrane-bound LPS versus purified LPS, and of non-LPS components of N. meningitidis. By using a wild-type N.
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