Peptidi

<p>Histone H3 (1-14) K4Me3 is derived from Histone 3 (H3) which is one of the four core histones (H2A, H2B, H3 and H4) fundamental in compacting eukaryotic DNA into the nucleosome. The nucleosome arises when 147 base pairs of DNA wrap around a H3-H4 tetramer and two H2A-H2B dimers, forming the histone octamer core. Both H4 and H3 are highly conserved and perform roles in binding to segments of DNA which enter and leave the nucleosome and in chromatin formation. Similar to the other core histone, H3 has a globular domain and a flexible N-terminal domain, 'histone tail' which can undergo modifications such as acetylation, methylation, phosphorylation and ubiquitination. Due to histones containing a large number of lysine and arginine residues they have a positive net charge which interacts in an electrostatic manner with the negatively charged phosphate groups in DNA. The transcriptional activation or silencing of the chromatin is controlled by ATP-dependent chromatin remodelling factors and histone modifying enzymes which target histone proteins. Both processes function to alter to change the positioning of the nucleosome, allowing the DNA it to be either available to the transcription machinery or inaccessible.The Histone H3 (1-14) lysine 4 has been trimethylated and contains 5-Carboxyfluorescein (5-FAM), a widely used green fluorescent tag.</p>

<p>Kinetensin was originally isolated from pepsin-treated plasma, and it shares some sequence homology with the C-terminal end of neurotensin (NT), having four of its nine amino acids in common with NT. Kinetensin is a potent histamine releaser and therefore may serve as an inflammatory mediator, it also has a role as a human metabolite and can increases vascular permeability. Kinetensin can be cleaved by ACE2.</p>

<p>Custom research peptide; min purity 95%. For different specs please use the Peptide Quote Tool</p>

<p>GSS-acid is a tripeptide consisting of a glycine residue followed by two serine residues. GSS-acid was synthesised from the dipeptide glycyl-L-serine (GS-acid)- the dipeptide GS-acid is also available in our catalogue. GSS-acid has a net charge of 0 and has diverse biological and chemical uses.</p>

<p>The synthetic canonical Flag sequence has been shown to be most effective with the Asp-Tyr-Lys-Xaa-Xaa-Asp motif triplicated for applications in protein analysis followed by the eight amino acids at the C-terminus of the classic FLAG sequence (Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys). Due to the hydrophilic nature of the peptide the Flag tag typically resides on the surface of the recombinant protein thus minimising any effects on the function or transport of the fusion protein. The tag can be used in conjunction with other tags such as HA or myc depending on the application. FLAG is an artificial antigen to which high affinity monoclonal antibodies have been raised, therefore allowing for highly effective protein purification by affinity chromatography as well as accurate localisation of FLAG tagged proteins within living cells, or Western blots. FLAG peptide can be used to effectively purify complexes with multiple proteins as its mild purification procedure tends not to disrupt such complexes. It can be used to obtain proteins of sufficient purity for x-ray crystallography. The 3 x Flag peptide provides powerful detection and purification of recombinant proteins that has been characterised in numerous applications including affinity chromatography, binding assays and structural analysis.</p>

<p>Tetanus Toxin P30 (947-967) is a protein that is derived from the single-chain polypeptide neurotoxin produced by Clostridium tetani. The neurotoxins produced by Clostridium tetani are among the most potent molecules known to humankind. Once in the body, the toxin binds to the basal lamina at the neuromuscular junction. From here, the toxin is transported to inhibitory interneurons in the spinal cord, where it prevents the release of neurotransmitters, which causes spastic paralysis.</p>

<p>Pathogenic Staphylococcus aureus strains produce N-formylmethionyl containing peptides. Peptides starting with an N-formylated methionyl group constitute a unique hallmark of bacterial as well as mitochondrial metabolism, and professional phagocytes of our innate immune system recognise this microbial/mitochondrial pattern as a danger signal that guides innate immune cells.All PSMα peptides have the same basic functions and promote virulence through effects on discrete neutrophil functions (i.e. chemotaxis) and by being cytotoxic at higher concentrations. PSMα2 and PSMα3 can both bind to FPR2 and trigger superoxide release in neutrophils at low nanomolar concentrations. In addition, at high nanomolar concentrations they display cytotoxicity selectively on apoptotic neutrophil membranes and this occurs in an FPR2 independent manner.</p>

<p>BCL6 encodes a transcription factor that represses genes necessary for the terminal differentiation of lymphocytes within germinal centers, and the misregulated expression of this factor is strongly implicated in several types of B cell lymphoma. The homodimeric BTB domain of BCL6 (also known as the POZ domain) is required for the repression activity of the protein and interacts directly with the SMRT and N-CoR corepressors that are found within large multiprotein histone deacetylase-containing complexes.</p>

<p>ARF peptide, is the alternative frame (ARF) tumour suppressor protein which is expressed on the occurrence of oncogenic stimuli. It functions to prevent abnormal cell proliferation through inhibiting the p53 ubiquitin ligase protein Mdm2 from degrading p53. This results in the increased stability of the p53 tumour suppressor causing G1 cell cycle arrest. Additionally mouse ARF proteins can localise E2F1 and c-Myc transcriptions factors to the nucleolus therefore they are no longer able to activate S-phase promoting target gene. Again this results in cell cycle arrest, ultimately preventing tumour cell growth. It is evident that if the expression of the ARF peptide is inhibited tumour formation is more likely to occur.</p>

<p>Fragment of the angiotensin-converting enzyme 2 (ACE2) peptidase domain (PD) alpha1 helix, a domain important for the interaction of ACE2 with the severe acute respiratory syndrome (SARS coronavirus receptor binding domain (SARS-CoV-2-RBD). SBP1 associates with the SARS-CoV-2-RBD with nanomolar affinity and can potentially block the key mechanism by which SARS CoV-2 initiates entry into human cells.This peptide has a covalently bonded N-terminal Biotin tag that can be used for detection and purification and contains a polyethylene glycol spacer (PEG4).</p>

<p>Portion of EBV</p>

<p>Shepherdin is an antagonist of the interaction between the apoptosis protein, survivin, and the molecular chaperone, heat shock protein 90 (Hsp90). The sequence of shepherdin corresponds to the site where Hsp90 binds to survivin. Shepherdin therefore has high affinity for Hsp90 and thus disrupts survivin binding and acts as an inhibitor of Hsp90 ATPase function by competing with ATP.The survivin-Hsp90 complex is a regulator of cell proliferation and cell viability in cancer tissue. Shepherdin has anti-cancer properties and can significantly suppress the growth of lung cancer cell lines and acute myeloid leukaemia (AML) by inducing apoptosis.</p>

<p>Auto-inducing peptide (AIP) is a cyclic thiolactone quorum sensing peptide from Staphylococcus aureus which is responsible for activating the agr response. AIP is released from the bacteria and its extracellular concentration is then sensed by a two-component system on the bacterial surface, AgrC and AgrA. AgrC is the membrane histidine kinase receptor and AgrA is a response regulator- upon binding of AIP, AgrC phosphorylates AgrA.AIP accumulates during growth activating an AgrC and AgrA cascade when it reaches a critical signal level. This cascade activates P2 and P3 promoters which autoactivate the agr system and upregulate RNAIII transcription. RNAIII regulates the expression of virulence factors including toxins, super-antigens, and exo-enzymes. Extensive research to identify AIP:AgrC inhibitors aims to find therapeutics against pathogens.AgrD is the precursor peptide of AIP, and AgrB is an integral membrane endopeptidase essential to biosynthesize AIP. This AIP system is conserved among many Gram-positive bacteria. S. aureus strains are categorized into four groups (I-IV) according to their AIP signal and cognate extracellular receptor, AgrC.AIP-II has the conserved thiolactone macrocycle of the AIP family. Asn-3, Leu-8, and Phe-9 have been shown to be critical for activation of the agr response while inhibition relies on Leu-8 and Phe-9. The reactive thiol ester bond is only necessary for activation of the agr response. Further work may provide further AIP:AgrC inhibitors.</p>

<p>Nuclear Factor Erythroid 2-Related Factor 2 (Nrf2) and its negative regulator Kelch-Like ECH-Associated Protein 1 (Keap1) provide vital protection in maintaining cellular redox. In parallel, Nrf2 also aids the resolution of inflammation and also tissue repair. In homeostatic conditions, the transcription factor Nrf2 is controlled in a cytoplasmic complex with Keap1 with ubiquitination and protein degradation. Nrf2 has been linked to numerous cancers due to mutations affecting the binding region of Nrf2 to Keap1, resulting in Nrf2 dissociating from the complex. Nrf2 constitutively accumulates in the nucleus and activation of prosurvival genes that promote cancer cell proliferation.The Neh2 region of Nrf2 interacts with Keap1, as shown by nuclear magnetic resonance spectroscopy. The 16 amino acid peptide (AFFAQLQLDEETGEFL) (69-84) flanks the conserved ETGE motif and can replicate the binding to keap1.Therapeutics targeting the Nrf2 signalling pathway and activation of Nrf2 is a keen area of research, with many cancers being linked to Nrf2, particularly pancreatic cancer. Additionally, activation of Nrf2 has become a possible target as a treatment for COVID. Nrf2 (69-84) replicating full-length Nrf2 binding has been helpful in all cases. This Nrf2 (69-84) contains a covalently bonded N-terminal Biotin tag that can be used for detection and purification. If you would prefer the simple peptide, Nrf2 (69-84), it is available from our catalogue.</p>

<p>C-type natriuretic peptide (CNP) is a novel urinary biomarker which is part of the natriuretic peptide family. CNP is produced in the kidney and the endothelium and has been localised to renal tubules. CNP expression has also been detected in cardiomyocytes, vascular endothelium, and bone.CNP is synthesized as the precursor 103 amino acid (AA) protein, proCNP (AA 1-103), which is then cleaved into NT-proCNP (AA 1-50) and CNP53 (AA 51-103) by the intracellular endoprotease furin. CNP53 is then cleaved to give the biologically active mature form CNP22 (AA 82-103) and inactive form NT-CNP53 (51-81). CNP primarily acts as an autocrine or paracrine factor and has anti-proliferative and anti-fibrotic properties, including suppression of fibroblast proliferation and collagen production, inhibition of vascular smooth muscle cell proliferation and accelerated regeneration of endothelial cells. CNP is a vasodilator and potent venodilator and slightly elevated levels have been detected in heart failure and renal disease states. CNP has renoprotective properties and is activated during renal injury, where it helps preserve glomerular function and suppress pro-fibrotic processes. Hypoxia, cytokines and fibrotic growth factors, are stimuli for CNP production and release.CNP selectively activates the cell surface particulate guanylyl cyclase receptor B (GC-B), catalysing the conversion of GTP to the downstream second messenger, cyclic guanosine monophosphate (cGMP).</p>

<p>Duck liver-derived peptide 3 is a novel bioactive peptide with high antioxidant activity. The antioxidant activity is attributed to forming hydrogen bonds between their amino acid residues and free radical molecules. Duck liver-derived peptide 2 increases the activities and mRNA expression levels of intracellular antioxidant enzymes (SOD, CAT, and GSH-Px) in HepG2 oxidative damage cell models. Duck liver-derived peptide 3 can reduce the content of malondialdehyde (MDA) and reactive oxygen species (ROS) accumulation, thereby inhibiting intracellular oxidative damage. Duck liver-derived peptide 3 has the following activity: immunomodulation, ACE inhibitor, dipeptidyl peptidase IV inhibitor, and antioxidant. This peptide may be used in the research for food-derived bioactive peptides for modified-food development.Of the identified duck-liver derived peptides, this is the only peptide in this group that has a proposed site of action as a HLA class I histocompatibility antigen.</p>

<p>Sakamototide is phosphorylated by members of the 5'-adenosine monophosphate-activated protein kinase (AMPK) family of kinases as is therefore ideal for use in kinase assays to test the activity of AMPK family members. The AMPK family includes- salt inducible kinases (SIKs), NUAK, sucrose non-fermenting (Snf1)-related kinase (SNRK), microtubule affinity regulating kinases (MARKs) and brain specific kinase/BR serine/threonine kinase (BRSK). The kinase activity of AMPK and AMPK-related kinases, is dependent on its phosphorylation at Thr175 by the upstream kinase LKB1 (also known as STK11).</p>

<p>Thyroglobulin (Tg) is a widely used biomarker of various differentiated thyroid cancer (DTC)- Tg is a substrate for thyroid hormone production. Detection and quantification of serum thyroglobulin levels remain challenging due to Tg's size, heterogeneity, and thyroglobulin autoantibodies (TgAb). Immunoassays offer the opportunity to tailor DTC treatments, but many patients are TgAb positive, excluding them from analysis during regression.Liquid chromatography-tandem mass spectrometry (LC-MS/MS) can overcome immunoassay issues by digestion of Tg to a tryptic peptide removing the interference from TgAbs.</p>

<p>14-3-3 proteins are highly conserved from yeast to plants and mammals where they are found in various organs and tissues. 14-3-3 proteins regulate numerous signalling pathways via direct binding to proteins carrying phosphorylated 14-3-3-binding motifs, several hundred binding partners have been identified for 14-3-3 proteins. Their functions include a role in viral infections and innate immunity, protein trafficking, cell-cycle control, apoptosis, autophagy and other cell signal transduction pathways, as well as the associated mechanisms. There are seven 14-3-3 subtypes (alpha/β,γ, ε,η, σ, τ [also called θ] and ζ/δ) in mammals. 14-3-3 ζ has been shown to interact with Hepatitis B virus (HBV) protein X (HBx), E6 oncoprotein, Caspase-2: a protease involved in apoptosis, and to be is involved in the subcellular localisation of the FOXO forkhead transcription factor. 14-3-3 ζ acts as a molecular block that covers the DNA-binding site of FOXO4, thus blocking its interaction with the target DNA. 14-3-3 ζ also participates in the TLR3-TICAM-1 signalling pathway by promoting multimerization of TICAM-1 to form a signalosome. 14-3-3 ζ isoform may also be the target of SARS-CoV-2 in the nervous system.</p>

<p>Portion of Influenza NP</p>