domain

SEB Domain 144-153 acetate(210229-94-0 free base) is amino acid residues 163-172 of the staphylococcal enterotoxin B domain. SEB Domain 144-153 acetate(210229-94-0 free base) has been shown to inhibit the transcytosis of several staphylococcal enterotoxins, SEA, SEE, and TSST-1.

SEB Domain (144-153) peptide is Staphylococcal Enterotoxin B domain amino acid residue 163-172. SEB Domain (144-153) has been shown to inhibit transcytosis of multiple staphylococcal enterotoxins, SEA, SEE, and TSST-1.

Tau Peptide (275-305), also known as the R2 domain fragment, represents the second repeat unit of the microtubule-binding domain of the Alzheimer's tau peptide. Tau Peptide (275-305) is considered crucial in determining the biochemical characteristics of the complete tau protein.

PDZ1 Domain Inhibitor Peptide TFA, a cyclic peptide featuring a β-Ala lactam side chain linker, specifically targets the PDZ1 domains of postsynaptic density protein 95 (PSD-95). It effectively disrupts the GluR6/PSD-95 interaction, competing against the C terminus of GluR6 for the PDZ1 domain with high efficiency [1].

SEB Domain 144-153 TFA is Staphylococcal Enterotoxin B domain amino acid residue 144-153. It inhibits transcytosis of multiple staphylococcal enterotoxins, SEE, SEA, and TSST-1.

Novel cyclic peptide that disrupts interaction between GluR6 and PSD-95

Grb2 SH2 Domain Inhibitor 1 TFA is a cyclic cell-penetrating peptide (CPP) featuring a conformationally restricted d-pro-l-pro motif ring (AF Φ Rpprrfq), where Φ represents L-naphthylalanine, R signifies D-arginine, and P stands for D-proline. It primarily functions as a cyclic peptide inhibitor.

Caveolin-1 (82-101) amide (human, mouse, rat), also known as Caveolin-1 scaffolding domain peptide, mitigates aging-related detrimental alterations in various organs and inhibits tyrosine kinases [1].

Myr-Tat-CBD3 is a chemical compound that serves as an inhibitor of the protein-protein interaction between the N-type voltage-gated calcium channel Cav2.2 and collapsin response mediator protein 2 (CRMP2). This compound effectively disrupts the Cav2.2-CRMP2 interaction by about 81% at a 10 µM concentration and demonstrates an inhibitory concentration 50 (IC50) value of approximately 2.8 µM against potassium-induced calcium influx in primary rat dorsal root ganglion (DRG) neurons. Furthermore, at a concentration of 20 µM, Myr-Tat-CBD3 specifically inhibits calcium currents without affecting sodium currents in primary DRG neurons. Additionally, intrathecal administration of 20 µg/5 µl of Myr-Tat-CBD3 effectively mitigates carrageenan-induced declines in paw withdrawal latencies in rats, indicating its potential for pain relief. The compound also notably reduces cue-induced reinstatement of cocaine-seeking behavior in rats, suggesting therapeutic potential in addiction treatment.

Amyloid β-Protein 10-20 acetate (Amyloid β-Protein 10-20 acetate (152286-31-2 free base)) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.Amyloid β protein fragment containing the α-secretase processing site (Lys16-Leu17 bond). It also contains the HHQK domain (residues 13-16) responsible for binding to microglial cells.

Fibronectin Adhesion-promoting Peptide acetate (Heparin Binding Peptide acetate) is one of the heparin-binding amino acid sequences found in the carboxy-terminal heparin-binding domain of fibronectin.

PKC ζ pseudosubstrate acetate is an inhibitor of protein kinase C (PKC) ζ; attached to cell permeabilisation Antennapedia domain vector peptide. Consists of amino acids 113 - 129 of PKC ζ pseudosubstrate domain linked by a disulphide bridge to the Antenna

PUMA BH3 acetate (PUMA BH3 Free base) is a p53 positive regulator of apoptosis (PUMA) BH3 domain polypeptide that acts as a direct activator of Bak with a Kd of 26 nM.

BAD (103-127) (human) acetate is a 25-mer Bad polypeptide from the BAD BH3 domain that antagonizes the effects of Bcl-xl.

Tat-NR2B9c acetate (NA-1 acetate) is a postsynaptic density-95 (PSD-95) inhibitor, with EC50 values of 6.7 nM and 670 nM for PSD-95d2 (PSD-95 PDZ domain 2) and PSD-95d1, respectively. Tat-NR2B9c acetate disrupts the PSD-95/NMDAR interaction, inhibiting NR2A and NR2B binding to PSD-95 with IC50 values of 0.5 μM and 8 μM, respectively. Tat-NR2B9c acetate also inhibits neuronal nitric oxide synthase (nNOS)/PSD-95 interaction, and possesses neuroprotective efficacy.

CS1 peptide is present within type III homology connecting segment (IIICS) as well as C-274 (cell-binding domain). Fibronectin CS1 Peptide lacks the Arg-Gly-Asp-containing domain, actively inhibits tumor metastases in spontaneous and experimental metastas

Gly-Arg-Gly-Asp-Ser (GRGDS) acetate is a cell binding protein domain derived from the cell-binding region of fibronectin.

Protein Kinase C 19-31 acetate, a peptide inhibitor of protein kinase C (PKC), derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31) with a serine at position 25 replacing the wild-type alanine, is used as protein kinase C substrate

Hsp70-derived octapeptide acetate (Hsp70-derived octapeptide acetate) is a group of tetratricopeptide repeat (TPR)-containing proteins has been shown to interact with the C-terminal domain of the 70 kDa heat-shock cognate protein (hsc70). In the present study, the effect of the TPR-containing proteins, including the C-terminus of hsc70-interacting protein (CHIP), TPR1 and human glutamine-rich TPR-containing protein (hSGT), on refolding of luciferase by DnaJ and hsc70 was investigated.

IKKγ NBD Inhibitory Peptide acetate is a NEMO-binding domain peptide (NBD peptide) acetate corresponding to the NEMO amino-terminal alpha-helical region. IKKγ NBD Inhibitory Peptide acetate is shown to block TNF-alpha-induced NF-kB activation.

Calpastatin subdomain B is a bioactive peptide that inhibits calpain activity.

Tat-NTS peptide, a cell-penetrating compound, comprises the HIV-1 Tat protein transduction domain fused with a 10-amino acid sequence (residues 228-237) from the repeat III domain of annexin A1, serving as a nuclear translocation signal (NTS). This peptide hinders the interaction between annexin A1 and importin β, obstructing annexin A1's nuclear entry in primary mouse hippocampal neurons. Tat-NTS effectively prevents apoptosis triggered by glucose-oxygen deprivation and reperfusion in these neurons. When administered in vivo at a dosage of 10 mg/kg, it significantly reduces infarct size, minimizes neuronal apoptosis, and improves navigation performance in the Morris water maze test for mice subjected to ischemia-reperfusion injury via middle cerebral artery occlusion (MCAO).

PUMA BH3, a peptide that includes the BH3 domain from the p53-upregulated modulator of apoptosis (PUMA) and activates the pro-apoptotic protein Bak, demonstrates binding affinity to Bak with dissociation constants (Kds) of 290 nM in HEPES buffer and 26 nM in CHAPS buffer. This interaction with Bak induces its homo-oligomerization and facilitates Bak-mediated membrane permeabilization.

GPllb is composed of a 125 Kd heavy chain that is disulfide-linked to a 23 Kd light chain. Hydropathicity analysis of the cDNA sequence indicates that GPllb is anchored to the platelet through a single transmembrane domain located within 20 amino acids of

VSGLNPSLWSIFGLQFILLWLVSGSRHYLW, a 30-amino-acid peptide, mirrors the C-terminal domain of α2δ-1 and is recognized as the α2δ-1Tat peptide. It disrupts the α2δ-1 - NMDAR interaction both in vitro and in vivo, offering a potential research tool for neuropathic pain studies [1].

MPG, a 27-amino acid peptide compound, is derived from the fusion peptide domain of HIV-1 gp41 and the nuclear localisation sequence of SV40 large T antigen. As a potent delivery agent, MPG enables efficient and widespread transport of nucleic acids and oligonucleotides into cultured cells.

Fibronectin Adhesion-promoting Peptide (Heparin Binding Peptide) is a heparin-binding amino acid sequence located in the carboxy-terminal heparin-binding domain of fibronectin.

Caloxin 1B1, a bioactive peptide, exhibits selective inhibition of PMCA extracellularly by binding preferentially to the extracellular domain 1 of PMCA4 over PMCA1. Identified through a screening process for its high-affinity interaction with PMCA, Caloxin 1B1 is capable of direct application to cells and tissues, facilitating research into its impact on smooth muscle and endothelium.

VSGLNPSLWSIFGLQFILLWLVSGSRHYLW (TFA), a 30-amino-acid peptide, mimics the C-terminal domain of α2δ-1, known as α2δ-1Tat peptide. This compound disrupts the α2δ-1 - NMDAR interaction both in vitro and in vivo, demonstrating potential utility in neuropathic pain research [1].

TAT-P4-(DATC5)2 is a potent peptide inhibitor of the PDZ domain of protein interacting with C kinase-1 (PICK1), with a high affinity dissociation constant (K_i) of 1.7 nM. This compound has demonstrated the ability to mitigate addiction behaviors in rat models [1].

he connecting segment 1 (CS-1) is a cell attachment domain located in the type III homology connecting segment (IIICS) of fibronectin. CS1 peptide of fibronectin, which lacks the Arg-Gly-Asp-containing domain, actively inhibits tumor metastases in spontan

Phosphopeptide ligand for the src SH2 domain (IC50 = 42 nM); displays 30-fold higher affinity than N-acetyl-O-phosphono-Tyr-Glu-Glu-Ile-Glu (Ac-pYEEIE,).

LL-37(17-32) is a biologically active peptide fragment derived from the C-terminal domain of human cathelicidin antimicrobial peptide. This segment reverses ABCG2-mediated multidrug resistance in cancer cell lines, highlighting its potential therapeutic role against drug resistance.

Selective cell-permeable peptide inhibitor of protein kinase C (IC50 ~ 0.5 μM). Consists of amino acids 19 - 31 of PKC pseudosubstrate domain linked by a disulphide bridge to a cell permeabilisation Antennapedia domain vector peptide. The Antennapedia pep

PNC-28 acetate, a peptide derived from the mdm-2-binding domain (residues 17–26) of the p53 protein featuring a penetratin sequence for membrane crossing, is utilized in pancreatic cancer research [1] [2].

TAT-DEF-Elk-1 TFA (TDE TFA) is a cell-penetrating peptide that inhibits Elk-1 by mimicking its DEF domain and disrupting its function. It effectively blocks Elk-1 phosphorylation and nuclear translocation without affecting ERK or MSK1 activation. This compound is a valuable tool for investigating Elk-1's role in neuronal plasticity development [1].

Caffeic acid-pYEEIE TFA, a non-phosphopeptide inhibitor, demonstrates strong binding affinity for the GST-Lck-SH2 domain [1].

Protein Kinase C (19-31) TFA, a peptide inhibitor of protein kinase C (PKC), derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31) with a serine at position 25 replacing the wild-type alanine, is used as protein kinase C substrate p

BH3 hydrochloride, a peptide that crosses the blood-brain barrier, induces apoptosis either through direct activation of the pro-apoptotic proteins Bax/Bak or by inhibiting anti-apoptotic Bcl-2 proteins (Bcl-2, Bcl-XL, Bcl-w, Mcl-1, and A-1) through their BH3 domain [1][2].

Mad1 (6-21) TFA, a fragment encompassing amino acids 6 to 21 of the Mad1 protein, exhibits a strong affinity for the PAH2 domain of mammalian Sin3A with a dissociation constant (Kd) of approximately 29 nM [1].

Noxa B BH3, a biologically active peptide encompassing the BH3 domain of the Noxa protein, displays targeted biological activity.

Dynorphin A (1-10) (TFA), an endogenous opioid neuropeptide, binds in the transmembrane domain of the κ-receptor.

TP508 TFA, a 23-amino acid segment of the thrombin molecule's receptor-binding domain, is a nonproteolytic thrombin peptide. It activates endothelial NO synthase (eNOS) to enhance nitric oxide (NO) production in human endothelial cells, thereby stimulating both endothelial cells and stem cells for tissue revascularization and regeneration [1] [2].

Peptide comprising residues 33 - 57 of the JNK binding (δ) domain of human c-Jun. Disrupts JNK/c-Jun interaction leading to inhibition of serum-induced c-Jun phosphorylation, up-regulation of p21cip/waf and modulation of inflammatory gene expression. Spec

This peptide, generated from the BH3 domain of Bak (Flu-BakBH3), has been shown to have high-affinity binding to a surface pocket of the Bcl-XL protein that is required for its death antagonist function.

MUC1, mucin core is a type I transmembrane glycoprotein that is characterized by its overexpression and abnormal glycosylation in carcinoma cells. It specifically binds to domain 1 of ICAM-1.

F1, an anti-inflammatory peptide, incorporates the HIV-1 Tat protein transduction domain linked with a 15-amino acid sequence from residues 46-60 of the inhibitor of NF-κB kinase-interacting peptide (IKIP). It effectively blocks LPS-induced phosphorylation of IκB kinase α (IKKα) and IKKβ, along with the nuclear translocation of NF-κB (p65) in mouse peritoneal macrophages at 5 µM concentration. F1, administered at 5 mg/kg in vivo, significantly reduces IL-6, TNF-α, and IL-1β serum levels and enhances survival in a mouse sepsis model induced by LPS.

A11, a cell-penetrating peptide, integrates the HIV-1 Tat protein transduction domain with an 11-amino acid segment from the annexin A1 N-terminus (residues 20-30). This compound disrupts the interaction between annexin A1 and the Eph receptor tyrosine kinase A2 (EphA2), leading to enhanced EphA2 ubiquitination in HK1 nasopharyngeal carcinoma (NPC) cells. At a concentration of 10 µM, A11 curtails proliferation, migration, and invasion of HK1 and 5-8F NPC cells. Furthermore, A11 demonstrably diminishes tumor volume in mouse xenograft models of 5-8F and HK1 NPC in vivo.

Surfactant protein A (SP-A) (196-215) is a synthetic peptide derived from the C-terminal carbohydrate recognition domain of human SP-A, specifically amino acids 196-215. This peptide suppresses LPS-induced TNF-α release in JAWSII mouse dendritic cells at 1 and 10 µM concentrations and promotes phagocytosis of P. aeruginosa at a 75 µM concentration. Furthermore, intratracheal administration of SP-A (196-215) at a dose of 50 µg per animal reduces disease severity and lung colony-forming units in mice infected with P. aeruginosa.

EPQpYEEIPIYL, a phosphopeptide, is a ligand for the Src homology 2 (SH2) domain, activating Src family members such as Lck, Hck, and Fyn through binding interactions with SH2 domains.