Human fibrinopeptide B (hFpB)

Human fibrinopeptide B (hFpB)

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

Pyr-GVNDNEEGFFSAR-OH

Pyr-Gly-Val-Asn-Asp-Asn-Glu-Glu-Gly-Phe-Phe-Ser-Ala-Arg-OH

14

95.69%

C₆₆H₉₃N₁₉O₂₅

1552.55

36204-23-6

16132131

Synthetic

Powder

Human fibrinopeptide B (hFpB) is a peptide of 14 amino acids that is released from the amino-terminus of the Bβ-chains of fibrinogen by thrombin. It is also contained within the primary plasmin cleavage product of fibrinogen, Bβ1-42. hFpB stimulates the migration of PMN, with a peak effect occurring at 10^-8 M. This chemotactic activity is blocked by preincubating hFpB with antiserum to hFpB. PMN chemotaxis to hFpB does not involve the receptors for C5a, LTB4, or fMLP. hFpB also exerts chemotactic activity for fibroblasts, and its potency is comparable to that observed with PDGF under identical test conditions. hFpB causes an increase in cytoskeletal-associated actin in PMN within 30 s, showing a clear dose response with the maximal effect at 10^-8 M. However, it does not cause PMN aggregation, release of lysosomal enzymes (lysozyme and β-glucuronidase), or the production of superoxide anion. The chemotactic potency of hFpB for PMN is equivalent to that of C5a, LTB4, and fMLP, and its chemotactic activity for PMN occurs in the same concentration range as these other well-defined PMN chemoattractants.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual: Handling and Storage of Synthetic Peptides

• Senior RM, Skogen WF, Griffin GL, Wilner GD. Effects of fibrinogen derivatives upon the inflammatory response. Studies with human fibrinopeptide B. J Clin Invest. 1986 Mar;77(3):1014-9. doi: 10.1172/JCI112353. PMID: 3005361; PMCID: PMC423507.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.