Peptides & Proteins

The DYKDDDDK peptide was developed specifically for immunoaffinity chromatography. The peptide allows the competitive elution of proteins (amino terminal, metaminoterminal or carboxy-terminal) FLAG® fusion proteins from anti-FLAG M1 or anti-FLAG M2 antibodies (in solution or bound and agarose) under mild, non-denaturing conditions. Application Usual working concentration is 100µg/mL.For stock solution, dissolve in TBS (10mM Tris/HCl, 150mM NaCl, pH7.4) to a final concentration of 5mg/mL. FLAG®: FLAG is a registered trademark of Sigma-Aldrich Co. LLC

Albumin from hen egg white (ovalbumin) is a phosphorylated glycoprotein that contains 385 amino acid residues and has a molecular weight of 42.7 kDa. Chicken egg white is the protein component with the highest amount of egg white. It is used in protein research as a marker (approx. 45 kDa) in protein electrophoresis. In addition, it is used for structure elucidation and also serves as a comparison standard.

alpha-Chymotrypsin is a serine peptidase that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Leu) on the carboxyl end of the bond. Ca2+ activates and stabilizes the enzyme. The enzyme has 241 amino acid residues in total contained in three polypeptide chains (A chain: 13 amino acids; B chain: 131 amino acids, and C chain: 97 amino acids) linked by disulfide bridges. alpha-Chymotrypsin is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF) >, N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK) >, chymostatin, aprotinin, α1-antitrypsin, and α2-macroglobulin, 10mM Cu2+ and Hg2+.

Albumin - crystallised is a Fraction V Albumin recrystallised 3 times at temperatures below 0°C. This procedure ensures a very native protein, that is free of carbohydrates, globulines and fatty-acids.

IgG-free bovine serum albumin. Especially recommended as a blocking and stabilising reagent in all antibody-mediated detection systems. In addition to being IgG-free, this albumin also shows a very low fatty acid content of less than 0.01%. Feature:Prepared from bovine plasma or serum obtained from cattle less than 30 months old which have received ante and post mortem inspectors by USFDA inspected facilities.

Standard grade, lyophilised Albumin. Bovine serum albumin (BSA) is added as a stabilizing component for proteins/enzymes to several enzyme reaction and storage buffers. The concentration usually ranges from 0.01% (0.1mg/mL) to 3% (30mg/mL). BSA is added to the 10X concentrated buffers of DNA-modifying enzymes or restriction enzymes in a concentration of 0.5mg/mL. Alternatively, BSA can be substituted by gelatin for such purposes at the same concentration. Besides, albumin is applied as a blocking agent for blocking unbound surfaces of blotting membranes in immunoblots (3%) or ELISAs (3% in PBS) or for the dilution of antisera and antibody-stock solutions, respectively. In ELISAs, BSA is frequently replaced by non-fat dried milk. This fraction of albumin has been manufactured by a combination of the heat-shock method and alcohol precipitation. Albumin is stable as powder (3 years) or in solution (biological buffers like PBS, one year at +4°C to -20°C). Stock solutions are prepared in concentrations up to 20%. If crystals are formed during storage of the solutions, they can be redissolved by warming up to 37°C and mixing. Usually, sodium azide is added at a final concentration of 2 mM (or 0.02 - 0.2%) to prevent microbial contaminations.

Heat treated (equivalent to 10 hours at 60°C) Bovine Serum Albumin with a very low endotoxin value and no detectable IgG. In addition this albumin is free of mycoplasma and bovine viruses. The isolation and purification process prevent the product from impurities like capryllic acid or other stabilisers that could be cytotoxic to some cell lines. Tested for use in tissue culture.

Chymotrypsinogen is the practically inactive "precursor" (proenzyme, or zymogen) of chymotrypsin. In order to be activated, chymotrypsinogen has to be cleaved by trypsin between the amino acids arginine and isoleucine (R15 and I16) , which leads to structural changes and the formation of the substrate binding site (Sears 2010). Chymotrypsin is a trypsin-like serine protease. Chymotrypsin differs from trypsin in the selectivity of the cleavage site of proteins. While trypsin cleaves proteins between the amino acids Arg and Lys, Chymotrypsin prefers large hydrophobic amino acids as cleavage site. Unit definition: The amount of activated zymogen that causes a decrease in absorbance at 237 nm of 0.0075 per minute at 25°C resulting from the hydrolysis of ATEE (NF/USP unit).

Antigen peptide IE (316-324) (I1) HLA-A*02:01 (ILEETSVML) for stimulation of antigen-specific T cells in T cell assay such as ELISPOT, ICS, cytotoxicity or proliferation assays.ILEETSVML has an amino acid substitution at position 316 (Val versus Ile) compared to VLEETSVML.

CMV IE-1 (316-324) HLA-A * 0201 VLEETSVML for stimulation of T cells. The peptide was synthesized as presented by MHC class I molecules.IE-1 stands for immediate-early protein 1. CMV stands for human cytomegealovirus, or HCMV for human cytomegalovirus respective HPV human herpesvirus.

IE-1 stands for immediate-early protein 1. CMV stands for human cytomgealovirus, HCMV for human cytomegalovirus or HPV human herpesvirus.

CMV pp50 (245-253) HLA-A*01:01 VTEHDTLLY zur Stimulation von T-Zellen. Das Peptid wurde so synthetisiert, wie es von MHC-Klasse-I-Molekülen präsentiert wird.

CMV pp65 (16-24) HLA-A*11:01 GPISGHVLK for stimulation of T cells. The peptide was synthesized as presented by MHC class I molecules. CMV stands for human cytomegalovirus, or HCMV for human cytomegalovirus or HPV human herpesvirus.

Single peptide (NLVPMVATV) for stimulation of human CMV specific CD8+ T-cells. The peptide is synthesised as it is presented by the MHC class I HLA-A*0201 allele. Purities offered: >95%. T-cell epitopes are presented on the surface of antigen-presenting cells by MHC molecules. T cell epitopes presented by MHC class I molecules are typically peptides between 8 and 11 amino acids in length and exhibiting MHC-specific sequence motifs.

Clostridium histolyticum collagenase is an enzyme mixture of collagenase, clostripain and tryptic and proteolytic activities. Collagenase type I shows a balanced activity of collagenase, clostripain as well as tryptic and proteolytic activities. Type I Collagenase is recommended for cell preparation from epithelial, liver, lung tissue, tissue of the suprarenal gland and adipose tissue. The specific activity is >90 Mandl-Units per mg dry substance. Collagenase is produced by two separate and distinct genes in Clostridium histolyticum. Both genes have been cloned and sequenced (Yoshihara 1994). The colG gene codes for type I collagenase, a 936 amino acid protein, while the colH gene codes for type II collagenase, a 1021 amino acid protein. Both genes share 72% identity, the proteins only 43%. Both gene products can be present as two or more isoforms differing in molecular weight. Therefore collagenase mixtures can contain six to eight different proteins in a molecular weight range from 68 to 130 kDa. Substrate specificity studies have demonstrated that the colG gene prefers natural substrates such as intact collagen, compared to the colH gene product which preferentially digests short synthetic substrates (FALGPA) (Eckhard et al. 2009 and Matsushita 1999). General description:The treatment of tissue with collagenase causes the careful, selective degradation of the intercellular matrix, and does not affect the growth of the cells. The collagenase offered by Genaxxon bioscience is a mixture of different proteolytically active enzymes and requires calcium ions for both the catalytic activity and the binding to the collagen molecule. In contrast to vertebrate collagenase, Clostridium histolyticum collagenase digests native triple helix collagen into small peptides, which is the major use of collagenases in cell culture application. For optimal results, a well balanced mixture of proteolytic enzymes is necessary. Four different collagenases, Collagenase Type I >, Collagenase Type II >, Collagenase Type III > and Collagenase Type IV > are available for this. Type IV is usually used together with other enzymes, such as trypsin >, elastase or hyaluronidase >. Trypsin or Trypsin/EDTA > conventionally used in the cell culture degrades the matrix only slowly and can cause irreversible damage to the released cells. Therefore, we recommend Accutase > instead of trypsin or trypsin/EDTA. Clostridium collagenases belongs to the metalloproteases, a large family of proteases that shares a zinc-containing motif at the center of the active site (Gonzales and Robert-Baudouy 1996). The enzyme is reversibly inactivated at high pH values and irreversibly inactivated at low pH values. Inhibitors of collagenase include cysteine, EDTA, o-phenanthroline, 8-hydroxyquinoline-5-sulfonate, bipyridyl, 2,3-dimercaptopropanol or Hg2+, Pb2+, Cd2+, Cu2+. Collagenase is NOT inhibited by diisopropylphosphorofluoridate (DFP) or serum. Lyphilised Collagenase should be stored at +2°C to +8°C and remain stable without loss of activity for at least three years. Enzyme should be protected from moisture. Dissolved Collagenase can be aliquoted and stored at -20°C for one year. Conversion rates of collagenase activity units: 1 PZ U/mg ~ 3.9 FALGPA U/mg - 1 PZ U/mg ~ 1000 Mandl or CDU U/mg - 1 PZ U/mg ~ 10 HP U/mg (PZ-units according to Wünsch).

Clostridium histolyticum collagenase is an enzyme mixture of collagenase, clostripain and tryptic and proteolytic activities. Type II Collagenase is recommended for the preparation of cells from liver, bone, thyroid gland, heart and salivary gland and has a specific activity of >180 Mandl units per mg of dry matter. Collagenase is produced by two separate and distinct genes in Clostridium histolyticum. Both genes have been cloned and sequenced (Yoshihara 1994). The colG gene codes for type I collagenase, a 936 amino acid protein, while the colH gene codes for type II collagenase, a 1021 amino acid protein. Both genes share 72% identity, the proteins only 43%. Both gene products can be present as two or more isoforms differing in molecular weight. Therefore collagenase mixtures can contain six to eight different proteins in a molecular weight range from 68 to 130 kDa. Substrate specificity studies have demonstrated that the colG gene prefers natural substrates such as intact collagen, compared to the colH gene product which preferentially digests short synthetic substrates (FALGPA) (Eckhard et al. 2009 and Matsushita 1999). General description:The treatment of tissue with collagenase causes the careful, selective degradation of the intercellular matrix, and does not affect the growth of the cells. The collagenase offered by Genaxxon bioscience is a mixture of different proteolytically active enzymes and requires calcium ions for both the catalytic activity and the binding to the collagen molecule. In contrast to vertebrate collagenase, Clostridium histolyticum collagenase digests native triple helix collagen into small peptides, which is the major use of collagenases in cell culture application. For optimal results, a well balanced mixture of proteolytic enzymes is necessary. Four different collagenases, Collagenase Type I >, Collagenase Type II >, Collagenase Type III > and Collagenase Type IV > are available for this. Type IV is usually used together with other enzymes, such as trypsin >, elastase or hyaluronidase >. Trypsin or Trypsin/EDTA > conventionally used in the cell culture degrades the matrix only slowly and can cause irreversible damage to the released cells. Therefore, we recommend Accutase > instead of trypsin or trypsin/EDTA. Clostridium collagenases belongs to the metalloproteases, a large family of proteases that shares a zinc-containing motif at the center of the active site (Gonzales and Robert-Baudouy 1996). The enzyme is reversibly inactivated at high pH values and irreversibly inactivated at low pH values. Inhibitors of collagenase include cysteine, EDTA, o-phenanthroline, 8-hydroxyquinoline-5-sulfonate, bipyridyl, 2,3-dimercaptopropanol or Hg2+, Pb2+, Cd2+, Cu2+. Collagenase is NOT inhibited by diisopropylphosphorofluoridate (DFP) or serum. Lyphilised Collagenase should be stored at +2°C to +8°C and remain stable without loss of activity for at least three years. Enzyme should be protected from moisture. Dissolved Collagenase can be aliquoted and stored at -20°C for one year. Conversion rates of collagenase activity units: 1 PZ U/mg ~ 3.9 FALGPA U/mg - 1 PZ U/mg ~ 1000 Mandl or CDU U/mg - 1 PZ U/mg ~ 10 HP U/mg (PZ-units according to Wünsch).

Clostridium histolyticum collagenase is an enzyme mixture of collagenase, clostripain and tryptic and proteolytic activities. Collagenase type III shows normal Collagenase, but very low proteolytic activity. Type III Collagenase is recommended for preparation of cells from mamary gland and fetal cells and has a specific activity of 100 to 250 Mandl units per mg of dry matter. Collagenase is produced by two separate and distinct genes in Clostridium histolyticum. Both genes have been cloned and sequenced (Yoshihara 1994). The colG gene codes for type I collagenase, a 936 amino acid protein, while the colH gene codes for type II collagenase, a 1021 amino acid protein. Both genes share 72% identity, the proteins only 43%. Both gene products can be present as two or more isoforms differing in molecular weight. Therefore collagenase mixtures can contain six to eight different proteins in a molecular weight range from 68 to 130 kDa. Substrate specificity studies have demonstrated that the colG gene prefers natural substrates such as intact collagen, compared to the colH gene product which preferentially digests short synthetic substrates (FALGPA) (Eckhard et al. 2009 and Matsushita 1999). General description:The treatment of tissue with collagenase causes the careful, selective degradation of the intercellular matrix, and does not affect the growth of the cells. The collagenase offered by Genaxxon bioscience is a mixture of different proteolytically active enzymes and requires calcium ions for both the catalytic activity and the binding to the collagen molecule. In contrast to vertebrate collagenase, Clostridium histolyticum collagenase digests native triple helix collagen into small peptides, which is the major use of collagenases in cell culture application. For optimal results, a well balanced mixture of proteolytic enzymes is necessary. Four different collagenases, Collagenase Type I >, Collagenase Type II >, Collagenase Type III > and Collagenase Type IV > are available for this. Type IV is usually used together with other enzymes, such as trypsin >, elastase or hyaluronidase >. Trypsin or Trypsin/EDTA > conventionally used in the cell culture degrades the matrix only slowly and can cause irreversible damage to the released cells. Therefore, we recommend Accutase > instead of trypsin or trypsin/EDTA. Clostridium collagenases belongs to the metalloproteases, a large family of proteases that shares a zinc-containing motif at the center of the active site (Gonzales and Robert-Baudouy 1996). The enzyme is reversibly inactivated at high pH values and irreversibly inactivated at low pH values. Inhibitors of collagenase include cysteine, EDTA, o-phenanthroline, 8-hydroxyquinoline-5-sulfonate, bipyridyl, 2,3-dimercaptopropanol or Hg2+, Pb2+, Cd2+, Cu2+. Collagenase is NOT inhibited by diisopropylphosphorofluoridate (DFP) or serum. Lyphilised Collagenase should be stored at +2°C to +8°C and remain stable without loss of activity for at least three years. Enzyme should be protected from moisture. Dissolved Collagenase can be aliquoted and stored at -20°C for one year. Conversion rates of collagenase activity units: 1 PZ U/mg ~ 3.9 FALGPA U/mg - 1 PZ U/mg ~ 1000 Mandl or CDU U/mg - 1 PZ U/mg ~ 10 HP U/mg (PZ-units according to Wünsch).

Clostridium histolyticum collagenase is an enzyme mixture of collagenase, clostripain and tryptic and proteolytic activities. Collagenase type IV has low tryptic, high collagenase and normal clostripain activity. Type I Collagenase is recommended for cell preparation from epithelial, liver, lung tissue, tissue of the suprarenal gland and adipose tissue. The specific activity of >900 Mandl units per mg of dry matter. Collagenase is produced by two separate and distinct genes in Clostridium histolyticum. Both genes have been cloned and sequenced (Yoshihara 1994). The colG gene codes for type I collagenase, a 936 amino acid protein, while the colH gene codes for type II collagenase, a 1021 amino acid protein. Both genes share 72% identity, the proteins only 43%. Both gene products can be present as two or more isoforms differing in molecular weight. Therefore collagenase mixtures can contain six to eight different proteins in a molecular weight range from 68 to 130 kDa. Substrate specificity studies have demonstrated that the colG gene prefers natural substrates such as intact collagen, compared to the colH gene product which preferentially digests short synthetic substrates (FALGPA) (Eckhard et al. 2009 and Matsushita 1999). General description:The treatment of tissue with collagenase causes the careful, selective degradation of the intercellular matrix, and does not affect the growth of the cells. The collagenase offered by Genaxxon bioscience is a mixture of different proteolytically active enzymes and requires calcium ions for both the catalytic activity and the binding to the collagen molecule. In contrast to vertebrate collagenase, Clostridium histolyticum collagenase digests native triple helix collagen into small peptides, which is the major use of collagenases in cell culture application. For optimal results, a well balanced mixture of proteolytic enzymes is necessary. Four different collagenases, Collagenase Type I >, Collagenase Type II >, Collagenase Type III > and Collagenase Type IV > are available for this. Type IV is usually used together with other enzymes, such as trypsin >, elastase or hyaluronidase >. Trypsin or Trypsin/EDTA > conventionally used in the cell culture degrades the matrix only slowly and can cause irreversible damage to the released cells. Therefore, we recommend Accutase > instead of trypsin or trypsin/EDTA. Clostridium collagenases belongs to the metalloproteases, a large family of proteases that shares a zinc-containing motif at the center of the active site (Gonzales and Robert-Baudouy 1996). The enzyme is reversibly inactivated at high pH values and irreversibly inactivated at low pH values. Inhibitors of collagenase include cysteine, EDTA, o-phenanthroline, 8-hydroxyquinoline-5-sulfonate, bipyridyl, 2,3-dimercaptopropanol or Hg2+, Pb2+, Cd2+, Cu2+. Collagenase is NOT inhibited by diisopropylphosphorofluoridate (DFP) or serum. Lyphilised Collagenase should be stored at +2°C to +8°C and remain stable without loss of activity for at least three years. Enzyme should be protected from moisture. Dissolved Collagenase can be aliquoted and stored at -20°C for one year. Conversion rates of collagenase activity units: 1 PZ U/mg ~ 3.9 FALGPA U/mg - 1 PZ U/mg ~ 1000 Mandl or CDU U/mg - 1 PZ U/mg ~ 10 HP U/mg (PZ-units according to Wünsch).

CPPs, such as CyloP-1, are generally taken up by endocytic pathways, with vesicular encapsulation being a limiting factor in intracellular targeting. CyLoP-1 has been developed because it exhibits a pronounced diffuse cytosolic distribution along with endosomal uptake at low micromolar concentrations, thereby enhancing the delivery of a variety of drugs through the membrane barrier. Cell penetrating peptide (CPPs) are characterised by their ability to promote the receptor-independent cellular uptake of membrane-impermeable macromolecules, such as peptides, proteins, nucleic acids and nanoparticles. CPPs are usually short peptides with less than 30 amino acids. They are mostly amphipathic and highly cationic and usually rich of the amino acids arginine and lysine. Cellular internalisation of CPPs is observed for virtually all cells, although with different efficiencies that depend on the CPP, the cargo and the cell type (Verdurmen and Brock 2011, Trends Pharmacol. Sci. 32, 116-124). CyloP-1 is a cationic cysteine-rich CPP. Compared to other CPPs, CyloP-1 appeared to be a promising vector for access to the cytosol in a variety of cell types (Bioconjug Chem. 2011 Mar 16;22(3):319-28. doi: 10.1021/bc100045s. Epub 2011 Feb 14. CyLoP-1: a novel cysteine-rich cell-penetrating peptide for cytosolic delivery of cargoes. Jha D1, Mishra R, Gottschalk S, Wiesmüller KH, Ugurbil K, Maier ME, Engelmann J.). In addition to the positively charged residues, the presence of cysteines and tryptophans proved to be essential to maintain its functionality. The distinct feature of CyLoP-1 to enter the cytosol was further explored by the covalent attachment of cargoes of different nature and sizes. In particular, induction of caspase-3 activity (indicating apoptosis) by a CyLoP-1-SmacN7 conjugate proved successful delivery of the pro-apoptotic cargo to its site of action in the cytosol. Efficient intracellular delivery into the entire cytosol already at low micromolar concentrations makes CyLoP-1 a promising candidate for cytosolic delivery of cargoes of small sizes. Thus, this peptide might prove to be useful for efficient transmembrane delivery of agents directed to cytosolic targets.

EBV (EBNA-3a) Peptide Pool is a Pool of 234 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Epstein-Barr nuclear antigen 3 (EBNA3a) (UniProt ID: P12977) of Epstein-Barr virus (HHV4) for T cell assays. One pack size allows the stimulation of 2,5 x 10E8 cells.

Single peptide (GLCTLVAML) for stimulation of humanEBV BMLF-1(280-288) CD8+ specific CD8+ T-cells. The peptide is synthesised as it is presented by the MHC class I HLA-A*0201 allele. Purities offered: >95%. T-cell epitopes are presented on the surface of antigen-presenting cells by MHC molecules. T- cell epitopes presented by MHC class I molecules are typically peptides between 8 and 11 amino acids in length and exhibiting MHC-specific sequence motifs.

The Epstein–Barr virus (EBV), formally called Human gammaherpesvirus 4, is one of eight known human herpesvirus types in the herpes family, and is one of the most common viruses in humans.

EBV EBNA-1 407-417 (HLA-B*35:01) peptide with the amino acid sequence HPVGEADYFEY is used for stimulation of antigen-specific T cells in T cell assays such as ELISPOT, ICS, cytotoxity or proliferation assays. The peptide is also used for stimulation of human EBV EBNA-1-specific CD8+ T-cells. HPVGEADYFEY is synthesised as it is presented by the MHC class I HLA-B*3501 allele. HPVGEADYFEY is a linear peptide (epitope ID24536) studied as part of Epstein-Barr nuclear antigen 1 from Human herpesvirus 4 (Epstein Barr virus). It has been studied for immune reactivity, tested in T cell assays and MHC ligand assays. Other peptide / peptide epitops from GenaxxonIf you can't find the peptide / peptide sequence you are looking for, please ask for at info@genaxxon.com. We can offer a broad range of peptides from stock.Examples:EBV EBNA-1 407-417 (HLA-B*35:01)EBV EBNA-1 407-417 mutant (HLA-B*35:01) 410A EBV EBNA-1 407-417 mutant (HLA-B*35:08) 411DEBV EBNA-3A 379-387 (HLA-B*07:02) EBV EBNA-3A 325-333 (HLA-B*08:01)EBV EBNA-3A 603-611 (HLA-A*03:01) EBV EBNA-3A 458-466 (HLA-B*35:01) EBV (EBNA-3a) Peptide Pool EBV LMP-2 340-349 (HLA-A*11:01) EBV LMP-2 426-434 (HLA-A*02:01) EBV LMP-2 131-139 (HLA-A*24:02) EBV control Peptide Pool (>95% HPLC)

Antigenic peptide EBV EBNA-3A HLA-B*08:01 (FLRGRAYGL) for stimulation of human EBV EBNA-3A(325-333) -specific CD8+ T-cells. The peptide is synthesised as it is (FLRGRAYGL) presented by the MHC class I HLA-B*0801 allele. Other peptide / peptide epitops from GenaxxonIf you can't find the peptide / peptide sequence you are looking for, please ask for at info@genaxxon.com. We can offer a broad range of peptides from stock.Examples:EBV EBNA-1 407-417 (HLA-B*35:01)EBV EBNA-1 407-417 mutant (HLA-B*35:01) 410A EBV EBNA-1 407-417 mutant (HLA-B*35:08) 411DEBV EBNA-3A 379-387 (HLA-B*07:02) EBV EBNA-3A 325-333 (HLA-B*08:01)EBV EBNA-3A 603-611 (HLA-A*03:01) EBV EBNA-3A 458-466 (HLA-B*35:01) EBV (EBNA-3a) Peptide Pool EBV LMP-2 340-349 (HLA-A*11:01) EBV LMP-2 426-434 (HLA-A*02:01) EBV LMP-2 131-139 (HLA-A*24:02) EBV control Peptide Pool (>95% HPLC)

Single peptide (RPPIFIRRL) for stimulation of human EBV EBNA-3A (379-387) specific CD8+ T-cells.The peptide is synthesised as it is presented by the MHC class I HLA-B*0702 allele. T-cell epitopes are presented on the surface of antigen-presenting cells by MHC molecules. T cell epitopes presented by MHC class I molecules are typically peptides between 8 and 11 amino acids in length and exhibiting MHC-specific sequence motifs.

Antigenic peptide EBV LMP-2 419-427 (HLA-A*24:02) TYGPVFMCL for stimulation of antigen-specific T cells in T cell assays such as ELISPOT, ICS, cytotoxity or proliferation assays. Other peptide / peptide epitops from GenaxxonIf you can't find the peptide / peptide sequence you are looking for, please ask for at info@genaxxon.com. We can offer a broad range of peptides from stock.Examples:EBV EBNA-1 407-417 (HLA-B*35:01)EBV EBNA-1 407-417 mutant (HLA-B*35:01) 410A EBV EBNA-1 407-417 mutant (HLA-B*35:08) 411DEBV EBNA-3A 379-387 (HLA-B*07:02) EBV EBNA-3A 325-333 (HLA-B*08:01)EBV EBNA-3A 603-611 (HLA-A*03:01) EBV EBNA-3A 458-466 (HLA-B*35:01) EBV (EBNA-3a) Peptide Pool EBV LMP-2 340-349 (HLA-A*11:01) EBV LMP-2 426-434 (HLA-A*02:01) EBV LMP-2 131-139 (HLA-A*24:02) EBV control Peptide Pool (>95% HPLC)

Peptide (PYLFWLAAI) for stimulation of human EBV LMP2(131-139)-specific CD8+ T-cells. The peptide is synthesised as it is presented by the MHC class I HLA-A*2402 allele.Other peptide / peptide epitops from GenaxxonIf you can't find the peptide / peptide sequence you are looking for, please ask for at info@genaxxon.com. We can offer a broad range of peptides from stock.Examples:EBV EBNA-1 407-417 (HLA-B*35:01)EBV EBNA-1 407-417 mutant (HLA-B*35:01) 410A EBV EBNA-1 407-417 mutant (HLA-B*35:08) 411DEBV EBNA-3A 379-387 (HLA-B*07:02) EBV EBNA-3A 325-333 (HLA-B*08:01)EBV EBNA-3A 603-611 (HLA-A*03:01) EBV EBNA-3A 458-466 (HLA-B*35:01) EBV (EBNA-3a) Peptide Pool EBV LMP-2 340-349 (HLA-A*11:01) EBV LMP-2 426-434 (HLA-A*02:01) EBV LMP-2 131-139 (HLA-A*24:02) EBV control Peptide Pool (>95% HPLC)

Peptide pool with 14 peptides that covers all mutations in the Spike Glycoprotein derived from the epsilon variant  B.1.427/B.1.429 of SARS-CoV-2. Possilbe applications: T-cell assays, Immune monitoring, Antigen specific T-cell stimulation, T-cell expansion, Cellular immune response. Each peptide is purified by solid phase extraction and checked on its purity by ESI-MS.This peptide pool is supplied lyophilized as trifluoroacetate salt. Peptide sequences included (15 nmol (approx. 25ug)/peptide for stimulation of 2.5 x 10E8 cells):MFVFLVLLPLVSIQC AVLYQGVNCTEVPVA LVLLPLVSIQCVNLT QGVNCTEVPVAIHAD PLVSIQCVNLTTRTQ IQCVNLTTRTQLPPA LGVYYHKNNKSCMES YHKNNKSCMESEFRV NKSCMESEFRVYSSA LDSKVGGNYNYRYRL VGGNYNYRYRLFRKS YNYRYRLFRKSNLKP GTNTSNQVAVLYQGV SNQVAVLYQGVNCTE Dissolve in a minimum amount of pure DMSO (approx. 40µL) and dilute with water to the desired concentration. Please pay attention that the final concentration of DMSO must be below 1% (v/v) to avoid toxicity in the biological system. Protein ID: P0DTC2 (swiss prot) 

This peptide pool with 31 peptides covers all mutations in the Spike Glycoprotein derived from the eta variant B.1.525 of SARS-CoV-2 which emerged in Angola in December 2020.. Possilbe applications: T-cell assays, Immune monitoring, Antigen specific T-cell stimulation, T-cell expansion, Cellular immune response. Each peptide is purified by solid phase extraction and checked on its purity by ESI-MS.This peptide pool is supplied lyophilized as trifluoroacetate salt. Peptide sequences included (15 nmol (approx. 25ug)/peptide for stimulation of 2,5 x 108 cells):KVFRSSVLHSTRDLF PFLGVHKNNKSWMES PIGAGICASYQTHTN SSVLHSTRDLFLPFF VHKNNKSWMESEFRV GICASYQTHTNSPRR HSTRDLFLPFFSNVT NKSWMESEFRVYSSA SYQTHTNSPRRARSV DLFLPFFSNVTWFHVMESEFRVYSSANNCT HTNSPRRARSVASQS PFFSNVTWFHVISGT FRVYSSANNCTFEYV LLAGTITSGWTLGAG NVTWFHVISGTNGTK YQAGSTPCNGVKGFN TITSGWTLGAGAALQ FHVISGTNGTKRFDN STPCNGVKGFNCYFPGWTLGAGAALQIPFA SGTNGTKRFDNPVLP NGVKGFNCYFPLQSY GTKRFDNPVLPFNDG GTNTSNQVAVLYQGV VIKVCEFQFCNDPFL SNQVAVLYQGVNCTE CEFQFCNDPFLGVHK AVLYQGVNCTEVPVA FCNDPFLGVHKNNKSQGVNCTEVPVAIHAD Dissolve in a minimum amount of pure DMSO (approx. 40µL) and dilute with water to the desired concentration. Please pay attention that the final concentration of DMSO must be below 1% (v/v) to avoid toxicity in the biological system. Protein ID: P0DTC2 (swiss prot) 

The DYKDDDDK peptide was specifically designed for immunoaffinity chromatography. It allows elution under mild and non-denaturing conditions. Several antibodies against this peptide have been developed. Usual working concentration is 100µg/mL.For stock solution, dissolve in TBS (10mM Tris/HCl, 150mM NaCl, pH7.4) to a final concentration of 5mg/mL.

gp100 (154-162) HLA-A*02:01 KTWGQYWQV is a linear peptidic epitope (epitope ID 33915) studied as part of Melanocyte protein PMEL from Homo sapiens (human). This epitope has been studied for immune reactivity, tested in T cell assays, B cell assay and MHC ligand assays. Other name: gp100 (pmel17) 154-162 (HLA-A*02:01).

gp100 (280-288) HLA-A*02:01 YLEPGPVTA is a linear peptidic epitope studied as part of Melanocyte protein PMEL from Homo sapiens (human). gp100 peptide YLEPGPVTA (HLA-A*0201)  for stimulation of human gp100-specific CD8+ T-cells. The peptide is synthesised as it is presented by the MHC class I HLA-A*0201 allele.

HBV envelope (183-191) (HLA-A*02:01) - FLLTRILTI is a linear peptidic epitope (epitope ID16755) studied as part of Large envelope protein from Hepatitis B virus. This epitope has been studied for immune reactivity. Tested in T cell assays, B cell assays and MHC ligand assays.

HBV core (18-27) (HLA-A*02:01) - FLPSDFFPSV is a linear peptidic epitope studied as part of Capsid protein from Hepatitis B virus and External core antigen from Hepatitis B virus. HBV core peptide FLPSDFFPSV (HLA-A*02:01) for stimulation of human HBV core-specific CD8+ T-cells. The peptide is synthesised as it is presented by the MHC class I HLA-A*02:01 allele.

HBV core (18-27) (subtype ADR4) (HLA-A*02:01) - FLPSDFFPSI is a linear peptidic epitope (epitope ID16832) studied as part of External core antigen from Hepatitis B virus and Capsid protein from Hepatitis B virus. This epitope has been studied for immune reactivity, tested in T cell assays, B cell assays and MHC ligand assays

HBV core (19-27) (HLA-B*35:01) (HLA-B*51:01) LPSDFFPSV is a linear peptidic epitope (epitope ID38701) studied as part of Large envelope protein from Hepatitis B virus. This epitope has been studied for immune reactivity. Tested in T cell assays, B cell assays and MHC ligand assays.

HBV core antigen (88-96) (HLA-A*11:01) YVNVNMGLK is a linear peptidic epitope (epitope ID76370) studied as part of Capsid protein from Hepatitis B virus and External core antigen from Hepatitis B virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays.

HBV envelope (183-191) (HLA-A*02:01) - FLLTRILTI is a linear peptidic epitope (epitope ID16755) studied as part of Large envelope protein from Hepatitis B virus. This epitope has been studied for immune reactivity. Tested in T cell assays, B cell assays and MHC ligand assays.

HBV envelope (348-357) (HLA-A*02:01) - GLSPTVWLSV peptide for stimulation of antigen-specific T cells in T cell assays such as ELISPOT, ICS, cytotoxity or proliferation assays.

HBV HBsAg (190-197) (H-2 Kb) - VWLSVIWM is a linear peptidic epitope (epitope ID71948) studied as part of Large envelope protein from Hepatitis B virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays.

HBV HBsAg (371-378) (H2-Kb) - IVSPFIPL is a linear peptidic epitope (epitope ID29454) studied as part of Large envelope protein from Hepatitis B virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays.

HBV Polymerase (455-463) (HLA-A*02:01) - GLSRYVARL is a linear peptidic epitope (epitope ID21145) studied as part of the Hepatitis B virus polymerase. This epitope has been studied for immune reactivity. Tested in T cell assays, B cell assays and MHC ligand assays. The peptide is delivered as lypphilized endotoxin free salt.

HCMV IE-1 ELRRKMMYM is a linear peptidic epitope (epitope ID 13133) studied as part of 55 kDa immediate-early protein 1 from Human herpesvirus 5 (Human cytomegalovirus). This epitope has been studied for immune reactivity, tested in T-cell assays and MHC ligand assays.

HCMV UL40 15-23 acts as an important negative regulator of natural killer cell activity. For this the HCMV UL40 15-23 peptide (epitope ID69921) is often used as positive control. HCMV UL40 15-23 is part of the immune evasion strategie of the Human Cytomegalovirus (HCMV). The virus downregulates HLA class Ia molecule expression in order to evade T cell recognition. However, a lack of surface HLA class Ia molecules triggers cytotoxicity of Natural Killer (NK) cells. To counteract this effect, the Cytomegalovirus promotes upregulation of HLA-E and provides the peptide HCMV UL40 15-23 (VMAPRTLIL), which is identical with the leader sequence of HLA-Cw03 (VMAPRTLIL). When loaded onto HLA-E, this peptide conferres resistance to NK cell lysis via the CD94/NKG2A receptor. HLA-E is presenting peptides derived from self-proteomic content and peptides of pathogenic origin.VMAPRTLIL is part of the following proteins of human origin: - Major histocompatibility complex, class I, C (UniProt:A0A140T9M0, A0A140T9U0, A0A0G2JH50, A0A140T912 and A0A140T9Z4) - HLA class I histocompatibility antigen C alpha chain (UniProt:Q53YP1, Q5RIP0) - HLA class I antigen (UniProt:Q5QT33) - Isoform 2 of HLA class I histocompatibility antigen, C alpha chain (UniProt:P10321-2)

CMV pp65 Control Pool of 138 peptides derived from a peptide scan (15mers with 11 aa overlap) through 65 kDa phosphoprotein (pp65) (UniProtKB - P06725) of Human cytomegalovirus (HHV-5) frequently used as positive control. 15 nmol (approx. 25µg/peptide) for stimulation of 2.5 x 10E8 cells µg. Length 65 kDa phosphoprotein: 561 amino acidsSequence:MESRGRRCPEMISVLGPISGHVLKAVFSRGDTPVLPHETRLLQTGIHVRVSQPSLILVSQYTPDSTPCHRGDNQLQVQHTYFTGSEVENVSVNVHNPTGRSICPSQEPMSIYVYALPLKMLNIPSINVHHYPSAAERKHRHLPVADAVIHASGKQMWQARLTVSGLAWTRQQNQWKEPDVYYTSAFVFPTKDVALRHVVCAHELVCSMENTRATKMQVIGDQYVKVYLESFCEDVPSGKLFMHVTLGSDVEEDLTMTRNPQPFMRPHERNGFTVLCPKNMIIKPGKISHIMLDVAFTSHEHFGLLCPKSIPGLSISGNLLMNGQQIFLEVQAIRETVELRQYDPVAALFFFDIDLLLQRGPQYSEHPTFTSQYRIQGKLEYRHTWDRHDEGAAQGDDDVWTSGSDSDEELVTTERKTPRVTGGGAMAGASTSAGRKRKSASSATACTSGVMTRGRLKAESTVAPEEDTDEDSDNEIHNPAVFTWPPWQAGILARNLVPMVATVQGQNLKYQEFFWDANDIYRIFAELEGVWQPAAQPKRRRHRQDALPGPCIASTPKKHRG

CINGVCWTV is a linear peptidic epitope (epitope ID6435) studied as part of Genome polyprotein from Hepatitis C virus. This epitope has been studied for immune reactivity, tested in T cell assays, B cell assay and MHC ligand assays Antigen Peptide HCV NS3 1073-1081 (HLA-A*02:01) CINGVCWTV for stimulation of antigen-specific T cells in T cell assays such as ELISPOT, ICS, cytotoxity or proliferation assays.

HCV NS3 (1406-1415) is a peptidic epitope studied as part of Genome polyprotein from Hepatitis C virus. The single peptide (Sequence: KLVALGINAV) can be used for stimulation of human HCV NS3 (1406-1415)-specific CD8+ T cells. The peptide is synthesised as it is presented by the MHC class I HLA-A*02:01 allele.

HCV NS3 1373–1380 is a linear peptide (epitope ID27847) with the amino acid sequence IPFYGKAI. The peptide/epitope is studied as part of Genome polyprotein from Hepatitis C virus.  The epitope has been studied for immune reactivity, tested in T cell assays, B cell assays and MHC ligand assays

HCV NS3 1436-1444 is a linear peptidic epitope (epitope ID4917) with the amino acid sequence ATDALMTGY. The peptide is studied as part of Genome polyprotein from Hepatitis C virus. The epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays.

T cell epitopes are presented on the surface of antigen-presenting cells by MHC molecules. T cell epitopes presented by MHC class I molecules are typically peptides between 8 and 11 amino acids in length and exhibiting MHC-specific sequence motifs Results of B. Vali et al. We identified a relatively high degree of amino acid sequence similarity between HLA-A2-restricted epitopes HIV (HXB2) gag: 77-85 (SLYNTVATL: SL9) and HCV (H77) NS5b:2594-2602 (ALYDVVSKL: AL9). Of the screened HIV-infected individuals, 5 subjects showed significant response to both peptides. PBMCs from these individuals were used for tetramer analysis. Among the examined responders, three individuals showed CD8+ T-cells distinctly double-stained for both tetramers. Flow cytometry was conducted for expression analysis of IFN-g and the degranulation marker CD107a on PBMCs stained with SL9 tetramer and stimulated with either SL9 or AL9 peptides ... . Conclusions: The preliminary findings of the group indicate a potential T-cell cross-recognition between HIV derived HLA-A2 restricted SLYNTVATL and HCV derived HLA-A2 restricted ALYDVVSKL epitopes. This degeneracy of HIV-specific T-cells may play a role in the underlying immunological mechanisms related to pathological profile of HCV/HIV co-infection and variable clinical outcomes influenced by different CD8 T-cell repertoire.