β-Amyloid (12-28) (TFA)

β-Amyloid (12-28) (TFA), a peptide fragment of the β-amyloid protein (β1-42)—a 42 amino acid protein primarily found in senile plaque cores—exhibits aggregation properties. This compound holds significance for research into Alzheimer’s disease, highlighting its potential utility in understanding the disease's pathology [1].

β-amyloid (12-28) TFA, a peptide fragment of β-amyloid protein (β1-42), is the major component of senile plaque cores. β-amyloid (12-28) has aggregation properties and the potential for Alzheimer’s disease research.

3X FLAG peptide TFA (402750-12-3 free base) (3X FLAG peptide TFA) is a synthetic peptide of 23 amino acid residue. The Asp-Tyr-Lys-Xaa-Xaa-Asp motif is repeated three times in the peptide.

Rotigaptide TFA(355151-12-1 free base) is a novel and specific modulator of Cx43 and is a potent AAP. Rotigaptide TFA(355151-12-1 free base) prevents the uncoupling of Cx43-mediated gap junction communication and normalizes cell-to-cell communication during acute metabolic stress.

PAMP-12(human, porcine) TFA, a significant constituent of immunoreactive (ir)-PAMP, derives from the adrenomedullin precursor and functions as a potent hypotensive peptide involved in cardiovascular regulation [1].

Bovine Myeloid Antimicrobial Peptide (BMAP) 28, a synthetic peptide derived from bovine cathelicidin-5 (amino acids 132-158), exhibits antimicrobial activity against E. coli, S. aureus, MRSA, S. epidermidis, and the fungus C. albicans, with minimum inhibitory concentrations (MICs) of 2, 2, 4, 1, and 8 µM respectively. At a concentration of 200 nM, BMAP 28 permeabilizes the inner membrane of E. coli, and at 5 µM, it inhibits herpes simplex virus 1 (HSV-1) replication in Vero 76 cells. Furthermore, at 30 µM, it causes hemolysis in human erythrocytes and cytotoxicity in human neutrophils. In vivo, a dose of 0.8 mg/kg enhances survival in mice infected with E. coli or MRSA, but not P. aeruginosa.

Ac2-12 TFA, an annexin/lipocortin 1 (LC1)-mimetic peptide, inhibits neutrophil extravasation and demonstrates antimigratory effects by attenuating the recruitment of neutrophils in experimental models of inflammation [1] [2].

β-Amyloid(28-35) human is a neurotoxic β-amyloid peptide fragment that contributes to Alzheimer's disease pathogenesis by interacting with neuronal membranes, modulating its secondary structure and toxicity. It also exhibits anisotropic effects on the acidic phospholipid DPH, thereby increasing the internal fluidity within lipid membrane bilayers [1].

PAMP-12 (unmodified) TFA, an endogenous peptide and potent MRGPRX2 (MrgX2) agonist (EC50=20-50 nM), induces hypotension by inhibiting catecholamine secretion from sympathetic nerve endings and adrenal chromaffin cells [1].

β-Amyloid(17-28) human is a fragment of the β-amyloid peptide (Abeta) associated with Alzheimer's disease (AD), promoting the aggregation of the full-length β-Amyloid40 into toxic aggregates [1]. This lipid-induced amyloid core segment is implicated in AD pathogenesis.

Biotin-β-Amyloid (1-42), human TFA, also known as Biotin-Amyloid β-Peptide (1-42) (human) TFA, is a biotin-labeled 42-amino acid peptide implicated in the pathogenesis of Alzheimer's disease [1].

Cardiotoxin Analog IV (6-12) TFA, a partial peptide of Cardiotoxin Analog IV, is derived from the venom of the Taiwan Cobra, showcasing the unique properties of snake venom cardiotoxin[1].

Proadrenomedullin N-terminal 12 peptide (PAMP-12), an endogenous fragment originating from the adrenal medulla and spanning amino acids 9-20 of human PAMP-20, plays a role in causing hypotension. It functions as an agonist for the MAS-related G protein-coupled receptor family member X2 (MRGPRX2), inhibiting forskolin-stimulated cAMP accumulation in CHO cells expressing human MRGPRX2 (EC50 = 57.2 nM) and selectively prompting calcium mobilization in these cells (EC50 = 41 nM), but not in cells expressing MRGPRX1, MRGPRX3, or MRGPRX4 at 1 µM. As an antagonist of nicotinic acetylcholine receptors (nAChRs), PAMP-12 obstructs carbachol-triggered catecholamine release and the influx of calcium and sodium (IC50s = 1.3, 0.39, and 0.87 µM, respectively) in primary bovine adrenal chromaffin cells, with no effect on histamine-induced responses (IC50s = >1 µM for all). Additionally, it decreases mean arterial blood pressure in normotensive rats at doses ranging from 10 to 50 nmol/kg.

Atrial Natriuretic Peptide (ANP) (1-28),rat (TFA) is the main circulating forms of Atrial Natriuretic Peptide (ANP) in rats, which strongly inhibit the secretion of Ang II - stimulated endothelin-1.

Secretin (28-54), human TFA is a 27-amino acid peptide that works on the human Secretin receptor.

β-Amyloid (1-40) TFA, a principal protein in plaques observed in the brains of Alzheimer's disease patients [1], is pivotal in research focused on this neurodegenerative disorder.

β-Amyloid 22-35 (Amyloid β-Protein 22-35) TFA, a fragment comprising residues 22-35 of the β-amyloid protein, exhibits cytotoxicity towards cultured rat hippocampal neurons in serum-free media. It aggregates and forms typical amyloid fibrils in neutral buffer solution, mirroring those observed with the full-length β-amyloid protein [1].

β-Amyloid (42-1), human TFA, a 42-amino acid peptide, represents the inactive form of Amyloid β Peptide (1-42) and is pivotal in the development of Alzheimer's disease [1].

β-Amyloid (1-40), FAM-labeled TFA is a FAM fluorescently-labelled?β-Amyloid (1-40) peptide (λ ex =?492?nm and λ em =?518?nm) [1] .

β-Amyloid (1-42), rat TFA is a 42-aa peptide, shows the effects of cytotoxicity on acute hippocampal slices, and has been used in studies of alzheimer's disease.

β-Amyloid (1-43)(human) TFA exhibits greater aggregation tendencies and heightened toxicity compared to its well-established counterpart, Aβ1-42. Additionally, this compound demonstrates associations with both sAPPα and sAPPβ. It has the potential to serve as an additional biomarker for Alzheimer’s disease (AD), complementing existing markers [1].

Somatostatin-28 (1-12) is a somatostatin fragment which is monitored in brain tissue to track processing of somatostatin.

GLP-1(28-36)amide TFA, a C-terminal nonapeptide derived from GLP-1 cleavage by neutral endopeptidase (NEP), acts as an antioxidant targeting mitochondria. It inhibits mitochondrial permeability transition (MPT), exhibiting anti-diabetic and cardioprotective effects [1].

Amyloid β-peptide fragment; minimum section required to bind to brain proteins. Binds with high affinity to α7-nicotinic ACh receptors, and impairs memory retention following central administration in mice in vivo.

AUNP-12 TFA (NP-12 TFA) is a polypeptide antagonist in the pd-1 signaling pathway, which has the same antagonistic effect on pd-l1 and pd-l2, and can protect the proliferation and effector function of lymphocytes.

Intracerebroventricular administration of synthetic peptides Beta-amyloid (12-20), (12-28), and (18-28) causes amnesia in mice. These peptides have only amino acid residues VFF at position 18 to 20 in common, suggesting the amnestic effect of the triad.

LfcinB 17–28 TFA, a fragment of Bovine Lactoferricin (LfcinB), exhibits weak antimicrobial activity, with a minimum inhibitory concentration (MIC) of 200 μM against E. coli [1].

β-Amyloid (12-20) is a peptide fragment of β-Amyloid.Thsis peptide contain the amino acid residues VFF at position (18-20), suggesting that this triad has amnestic effects.

AUNP-12 TFA (NP-12 TFA), a peptide antagonist of the PD-1 signaling pathway, exhibits equipotent antagonism toward PD-L1 and PD-L2, enhancing lymphocyte proliferation and effector functions. It promotes immune activation, shows significant antitumor activity, and holds potential for improved management of immune-related adverse events (irAEs) [1].

Amyloid β-Protein (33-42) TFA, a fragment encompassing residues 33-42 of the β-amyloid protein, mitigates the toxicity induced by Aβ42 [1].

β-Amyloid (1-28) is a β-Amyloid protein fragment involved in metal binding.

β-Amyloid (1-42), (rat mouse) (TFA) is a peptide fragment consisting of 42 amino acids that can be used to study Alzheimer's disease.