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| Product | Description | |
|---|---|---|
| Buforin-1 | The source of Buforin-1 is Bufo gargarizans. Buforin I is generated from histone H2A by pepsin-directed proteolysis in the cytoplasm of gastric gland cells. After secretion into the gastric lumen, buforin I remains adhered to the mucous biofilm that lines the stomach, thus providing a protective antimicrobial coat. Buforins also are known to possess anti-endotoxin and anticancer activities, thus making these peptides attractive reagents for pharmaceutical applications. |  |
| Buforin-2 | Buforin II is a highly potent antimicrobial peptide which was derived from buforin I, a peptide isolated from the stomach of the Bufo gargarizans. Buforin II is an α-helical antimicrobial peptide, however it has far stronger antimicrobial activity against a broad spectrum of microorganisms compared with other α-helical antimicrobial peptides. Grade: >95% by HPLC. Mole weight: 2434.85. | |
| Buforin-EC | Buforin-EC was found in Euphlyctis cyanophlyctis. It has antibacterial activity against E.coli HP101BA (MIC=9.6 μM), K.pneumoniae PTCC1388 (MIC=10.6 μM), M.luteus PTCC1625 (MIC=6.0 μM) and S.aureus PTCC1431 (MIC=8.1 μM). Buforin-EC has no or very limited (<3%) hemolytic activity at concentrations of 15 μg/ml and 60 μg/ml, respectively. | |
| Buforin I | Buforin I is a 39-amino acid AMP that was first isolated from the stomach tissue of the Asian toad Bufo gargarizans. Compared with other amphibian AMPs, such as magainin 2, buforin I shows much stronger antimicrobial activities in vitro against a broad spectrum of microorganisms. Buforins have anti-endotoxin and anticancer activities. Synonyms: H-Ala-Gly-Arg-Gly-Lys-Gln-Gly-Gly-Lys-Val-Arg-Ala-Lys-Ala-Lys-Thr-Arg-Ser-Ser-Arg-Ala-Gly-Leu-Gln-Phe-Pro-Val-Gly-Arg-Val-His-Arg-Leu-Leu-Arg-Lys-Gly-Asn-Tyr-OH; L-alanyl-glycyl-L-arginyl-glycyl-L-lysyl-L-glutaminyl-glycyl-glycyl-L-lysyl-L-valyl-L-arginyl-L-alanyl-L-lysyl-L-alanyl-L-lysyl-L-threonyl-L-arginyl-L-seryl-L-seryl-L-arginyl-L-alanyl-glycyl-L-leucyl-L-glutaminyl-L-phenylalanyl-L-prolyl-L-valyl-glycyl-L-arginyl-L-valyl-L-histidyl-L-arginyl-L-leucyl-L-leucyl-L-arginyl-L-lysyl-glycyl-L-asparagyl-L-tyrosine. Grade: ≥90% by HPLC. CAS No. 173010-28-1. Molecular formula: C184H318N70O47. Mole weight: 4262.93. | |
| Buforin II | It is a 21 amino acid peptide derived from Buforin I peptide that is isolated from the Asian toad Bufo gargarizans. It has anti-microbial activity by penetrating bacteria and inhibiting cellular functions. Compared with magainin 2, It binds DNA and RNA from E.coli with a much greater affinity. It is also considered to be a cell-delivery peptide and has been shown to deliver SiRNAs into cells followed by effective mRNA degradation. Synonyms: H-Thr-Arg-Ser-Ser-Arg-Ala-Gly-Leu-Gln-Phe-Pro-Val-Gly-Arg-Val-His-Arg-Leu-Leu-Arg-Lys-OH; Buforin; L-Threonyl-L-arginyl-L-seryl-L-seryl-L-arginyl-L-alanylglycyl-L-leucyl-L-glutaminyl-L-phenylalanyl-L-prolyl-L-valylglycyl-L-arginyl-L-valyl-L-histidyl-L-arginyl-L-leucyl-L-leucyl-L-arginyl-L-lysine; Buforin 2. Grade: ≥95%. CAS No. 172998-24-2. Molecular formula: C106H184N40O26. Mole weight: 2434.88. | |
| Butanoic acid,3-(((9H-fluoren-9-ylmethoxy)carbonyl)amino)-4- | Butanoic acid,3-(((9H-fluoren-9-ylmethoxy)carbonyl)amino)-4-. CAS No. 2350701-37-8. Molecular formula: C19H18FNO4. Mole weight: 343.3. | |
| Buthinin | Buthinin was found in Androctonus australis. It is active against both Gram-positive and Gram-negative bacteria. | |
| Butyl L-alaninate | Butyl L-alaninate. Synonyms: (S)-Butyl 2-aminopropanoate; L-Alanine, butyl ester; L-Ala-Onbu. CAS No. 2885-2-1. Molecular formula: C7H15NO2. Mole weight: 145.20. | |
| Butyrivibriocin AR10 | Butyrivibriocin AR10 is a new cyclic bacteriocin produced by the ruminal anaerobe Butyrivibrio fibrisolvens AR10. | |
| Butyrolacton-BCP-COOH | Butyrolacton-BCP-COOH. Synonyms: 3-(5-oxotetrahydrofuran-2-yl)bicyclo[1.1.1]pentane-1-carboxylic acid; 3-Butyrolacton-BCP-1-carboxylic acid. Molecular formula: C10H12O4. Mole weight: 196.20. | |
| Bz-Ala-Arg-OH | Bz-Ala-Arg-OH. Synonyms: Benzoylalanylarginine; N-Benzoyl-Ala-Arg-OH; L-Arginine, N(2)-(N-benzoyl-L-alanyl)-. Grade: 95%. CAS No. 71448-11-8. Molecular formula: C16H23N5O4. Mole weight: 349.38. | |
| Bz-Arg-4-Abz-OH HCl | Bz-Arg-4-Abz-OH HCl. Synonyms: Nα-Benzoyl-L-arginine 4-carboxyanilide hydrochloride; Bz-Arg-4-Abz-OH Hydrochloride. Grade: ≥ 98% by TLC. Molecular formula: C20H23N5O4.HCl. Mole weight: 433.89. | |
| Bz-Arg-4-Abz-OH·HCl | Bz-Arg-4-Abz-OH·HCl. Synonyms: Na-Benzoyl-L-arginine 4-carboxyanilide hydrochloride. CAS No. 60833-82-1. Molecular formula: C20H23N5O4. Mole weight: 397.43. | |
| Bz-Arg-Gly-Phe-Phe-Leu-4MbetaNA | A substrate for cathepsin D. Synonyms: benzoyl-Arg-Gly-Phe-Phe-Leu-MNA; Bz-Arg-Gly-Phe-Phe-Leu-4-methoxy-beta-naphthylamide; Bz-RGFFL-MNA. CAS No. 99112-24-0. Molecular formula: C50H59N9O7. Mole weight: 898.06. | |
| Bz-Arg-Gly-Phe-Phe-Pro-4MβNA HCl | Bz-Arg-Gly-Phe-Phe-Pro-4MβNA HCl. Synonyms: Bz-Arg-Gly-Phe-Phe-Pro-4MbNA HCl; Bz-RGFFP-MNA HCl. CAS No. 201928-98-5. Molecular formula: C49H56ClN9O7. Mole weight: 918.49. | |
| Bz-Arg-His-D-Asp-CH2Cl | Bz-Arg-His-D-Asp-CH2Cl is a peptide inhibitor of D-Aspartyl Endopeptidase. Synonyms: Bz-RHd-CMK; (Benzoyl-L-arginyl-L-histidyl-D-aspart-1-yl)chloromethane. CAS No. 468102-94-5. Molecular formula: C24H31N8O6Cl. Mole weight: 563.01. | |
| Bz-Cit-OMe HCl | Bz-Cit-OMe HCl. Grade: ≥ 95%. Molecular formula: C14H19N3O4·HCl. Mole weight: 329.8. | |
| Bz-Gly-Gly-OH | Bz-Gly-Gly-OH. Synonyms: Hippuryl glycine(N-Benzoylglycyl)glycine. Grade: ≥ 98% (HPLC). CAS No. 1145-32-0. Molecular formula: C11H12N2O4. Mole weight: 236.23. | |
| Bz-Gly-His-Leu hydrate | N-Hippuryl-His-Leu (hydrate) can be used for the identification of ACE inhibitors in vitro. Synonyms: N-Hippuryl-His-Leu hydrate; N-benzoylglycyl-L-histidyl-L-leucine, hydrate; N-Benzoyl-Gly-His-Leu. Grade: 95%. CAS No. 207386-83-2. Molecular formula: C21H27N5O5.xH2O. Mole weight: 447.5 (anhydrous). | |
| BZ-ILE-GLU-GLY-ARG-PNA | Bz-IEGR-pNA is a substrate for plasma kallikrein and coagulation factor XIIa. Synonyms: Nalpha-Benzoyl-L-isoleucyl-L-glutamyl-glycyl-L-arginine-4-nitroanilide; L-Argininamide, N-benzoyl-L-isoleucyl-L-alpha-glutamylglycyl-N-(4-nitrophenyl)-. CAS No. 59068-47-2. Molecular formula: C32H43N9O9. Mole weight: 697.74. | |
| Bz-Nle-Lys-Arg-Arg-AMC | Bz-Nle-Lys-Arg-Arg-AMC is a substrate of dengue virus NS2B-NS3 and yellow fever virus NS3 protease. Synonyms: BZ-NLE-LYS-ARG-ARG-AMC. CAS No. 863975-32-0. Molecular formula: C41H60N12O7. Mole weight: 832.99. | |
| BzO-BCP-NH-Boc | BzO-BCP-NH-Boc. Synonyms: 3-(t-butoxycarbonylamino)bicyclo[1.1.1]pentan-1-yl benzoate. Molecular formula: C17H21NO4. Mole weight: 303.36. | |
| BZ-PHE-VAL-ARG-AMC | BZ-PHE-VAL-ARG-AMC is a sensitive fluorogenic substrate for the quantitative determination of thrombin. Synonyms: N-Benzoyl-Phe-Val-Arg 7-amido-4-methylcoumarin; 4-Methyl-7-(Bz-L-Phe-L-Val-L-Arg-amino)coumarin. CAS No. 88899-22-3. Molecular formula: C37H43N7O6. Mole weight: 681.78. | |
| Bz-Val-Gly-Arg-AMC | Bz-VGR-AMC acts as a substrate for the tricorn core protease from Thermoplasma acidophilum. Synonyms: benzoyl-Val-Gly-Arg 4-methyl-7-coumarylamide; benzoyl-Val-Gly-Arg-4-methylcoumaryl-7-amide. CAS No. 87779-49-5. Molecular formula: C30H37N7O6. Mole weight: 591.67. | |
| C14orf49 protein (221-232) | C14orf49 protein (221-232) is a peptide derived from C14orf49 protein. C14orf49 protein is a probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Synonyms: SYNE3 (221-232). | |
| C20-OtBu-Glu-OtBu | C20-OtBu-Glu-OtBu. Synonyms: (S)-2-(19-tert-Butoxycarbonylnonadecanoylamino)pentanedioic acid 1-tert-butyl ester; (S)-5-(tert-Butoxy)-4-(20-(tert-butoxy)-20-oxoicosanamido)-5-oxopentanoic acid. CAS No. 1119061-70-9. Molecular formula: C33H61NO7. Mole weight: 583.85. | |
| C3a 70-77 2TFA | C3A (70-77) is an octapeptide corresponding to the COOH terminal of C3A, shows C3a specificity and 1-2% bioactivity. Synonyms: Complement 3a (70-77) 2TFA. Molecular formula: C39H63F6N13O14. Mole weight: 1051.98. | |
| C5a Anaphylatoxin (human) | Complement 5a plays, a central role in host defense, is involved in related functions in sepsis, adult respiratory distress syndrome, rheumatoid arthritis, psoriasis, neurodegeneration and ischemia/reperfusion injury. It has powerful chemoattractant and pro-inflammatory properties. Synonyms: H-Thr-Leu-Gln-Lys-Lys-Ile-Glu-Glu-Ile-Ala-Ala-Lys-Tyr-Lys-His-Ser-Val-Val-Lys-Lys-Cys-Cys-Tyr-Asp-Gly-Ala-Cys-Val-Asn-Asn-Asp-Glu-Thr-Cys-Glu-Gln-Arg-Ala-Ala-Arg-Ile-Ser-Leu-Gly-Pro-Arg-Cys-Ile-Lys-Ala-Phe-Thr-Glu-Cys-Cys-Val-Val-Ala-Ser-Gln-Leu-Arg-Ala-Asn-Ile-Ser-His-Lys-Asp-Met-Gln-Leu-Gly-Arg-OH (Disulfide bridge: Cys21-Cys47, Cys22-Cys54, Cys34-Cys55). Grade: ≥95%. CAS No. 1816940-05-2. Molecular formula: C350H578N108O107S8. Mole weight: 8267.63. | |
| CAD-2 | It is a cell penetrating peptide. Grade: >98%. | |
| Cadherin Peptide, avian Acetate | Cadherins are a class of type-1 transmembrane proteins. Molecular formula: C46H79N17O15. Mole weight: 1110.22. | |
| CADY | CADY is a secondary amphiphilic peptide that has been shown to efficiently deliver short nucleic acids, especially siRNA, but cannot deliver any peptides, even short negatively charged peptides. Synonyms: Ac-Gly-Leu-Trp-Arg-Ala-Leu-Trp-Arg-Leu-Leu-Arg-Ser-Leu-Trp-Arg-Leu-Leu-Trp-Arg-Ala-cysteamide. Grade: >98%. Molecular formula: C132H205N41O26S. Mole weight: 2814.41. | |
| Caenacin-1 | Caenacin-1 was found in Caenorhabditis elegans. It has antifungal activity. | |
| Caenacin-5 | Caenacin-5 was found in Caenorhabditis elegans. It has antifungal activity. | |
| Caerin 11 | Caerin 11 was found in Litoria peronii. It has antibacterial activity. | |
| Caerin-1.1 | Caerin-1.1 was found in Litoria gilleni. Caerin-1.1 is an antibacterial and antiviral peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin-1.10 | Caerin-1.10 was found in Litoria rothii. Caerin-1.10 is an antibacterial peptide with wide spectrum of activity. | |
| Caerin 1.11 | Caerin 1.11 was produced by Litoria eucnemis. Caerin 1.11 is a cationic amphipathic alpha-helical antimicrobial peptide with weak or no activity against both Gram-positive and Gram-negative bacteria. It is weakly active against E.coli (MIC=25 μM), E.cloacae (MIC=50 μM), K.pneumoniae (MIC=25 μM), and S.haemolyticus (MIC=50 μM). | |
| Caerin 1.12 | Caerin 1.12 is originally isolated from Litoria caerulea. It has antibacterial activity. | |
| Caerin-1.1.2 | Caerin-1.1.2 has antibacterial activity. The source of Caerin-1.1.2 is Litoria caerulea. Grade: >97% by HPLC. Molecular formula: C107H178N30O26. Mole weight: 2300.74. | |
| Caerin 1.13 | Caerin 1.13 is originally isolated from Litoria caerulea. It has antibacterial activity. | |
| Caerin 1.14 | Caerin 1.14 is originally isolated from Litoria caerulea. It has antibacterial activity. | |
| Caerin 1.15 | Caerin 1.15 is originally isolated from Litoria caerulea. It has antibacterial activity. | |
| Caerin-1.17 | Caerin-1.17 was found in Litoria gracilenta. Caerin-1.17 shows significant activity against Gram-positive organisms, but is less effective against Gram-negative organisms. Grade: >95% by HPLC. Molecular formula: C124H206N32O29. Mole weight: 2609.15. | |
| Caerin-1.18 | Caerin-1.18 was found in Litoria gracilenta. It shows significant activity against Gram-positive organisms, but is less effective against Gram-negative organisms. Grade: >96% by HPLC. | |
| Caerin-1.19 | Caerin-1.19 was found in Litoria gracilenta. Caerin-1.19 shows significant activity against Gram-positive organisms, but is less effective against Gram-negative organisms. | |
| Caerin-1.2 | Caerin 1.2 was found in Litoria caerula. Caerin 1.2 is an antibacterial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin 1.20 | Caerin 1.20 has antibacterial activity. The source of Caerin 1.20 is the skin secretions, hybrid between female Litoria splendida and male Litoria caerulea, Australia. Grade: >98% by HPLC. Molecular formula: C124H201N33O28. Mole weight: 2602.12. | |
| Caerin 1.3 | Caerin 1.3 was found in Litoria caerula. Caerin 1.3 is an antibacterial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin-1.4 | Caerin-1.4 was found in Litoria gilleni. Caerin-1.4 is an antibacterial and antiviral peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin 1.5 | Caerin 1.5 was found in Litoria caerula. Caerin 1.5 is an antibacterial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin-1.6 | Caerin 1.6 was found in Litoria chloris. Caerin 1.6 is an antimicrobial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. | |
| Caerin-1.7 | Caerin 1.7 was found in Litoria chloris. Caerin 1.7 is an antimicrobial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. | |
| Caerin-1.8 | Caerin 1.8 was found in Litoria chloris. Caerin 1.8 is an antimicrobial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. | |
| Caerin 1.9 | Caerin 1.9 was found in Litoria chloris. Caerin 1.9 is an antimicrobial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Synonyms: Caerin 1.9; NH2-Gly-Leu-Phe-Gly-Val-Leu-Gly-Ser-Ile-Ala-Lys-His-Val-Leu-Pro-His-Val-Val-Pro-Val-Ile-Ala-Glu-Lys-Leu-NH2. Molecular formula: C124H206N32O28. Mole weight: 2593.2. | |
| Caerin 21 | Caerin 21 was found in Litoria peronii. It has antibacterial activity. | |
| Caerin-2.1 | Caerin 2.1 was found in Litoria splendida. Caerin 2.1 is an antimicrobial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin-2.2 | Caerin 2.2 was found in Litoria gilleni. Caerin 2.2 is an antimicrobial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin-2.4 | Caerin 2.4 was found in Litoria caerula. Caerin 2.4 is an antibacterial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin-2.5 | Caerin 2.5 was found in Litoria gilleni. Caerin 2.5 is an antimicrobial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin 2.6 | Caerin 2.6 was isolated from Hybrid between female Litoria splendida and male Litoria caerulea. It has antibacterial activity. | |
| Caerin 2.7 | Caerin 2.7 was isolated from Hybrid between female Litoria splendida and male Litoria caerulea. It has antibacterial activity. | |
| Caerin-3.2 | Caerin 3.2 was found in Litoria caerula. Caerin 3.2 is an antibacterial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin-3.3 | Caerin 3.3 was found in Litoria caerula. Caerin 3.3 is an antibacterial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin-3.4 | Caerin 3.4 was found in Litoria caerula. Caerin 3.4 is an antibacterial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin-3.5 | Caerin-3.5 was found in Litoria gracilenta. It shows significant activity against Gram-positive organisms, but is less effective against Gram-negative organisms. | |
| Caerin-4.1 | Caerin 4.1 was found in Litoria caerula. Caerin 4.1 is an antibacterial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. Grade: >97% by HPLC. Molecular formula: C104H175N29O31. Mole weight: 2327.67. | |
| Caerin-4.2 | Caerin 4.2 was found in Litoria caerula. Caerin 4.2 is an antibacterial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerin-4.3 | Caerin 4.3 was found in Litoria caerula. Caerin 4.3 is an antibacterial peptide that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. | |
| Caerulein precursor-related fragment Ea | The source of Caerulein precursor-related fragment Ea is Rana esculenta. This peptide has no sequence similarity with antimicrobial peptides isolated from other species of ranid frogs. It potently and selectively inhibits the growth of the Gram-positive bacterium Escherichia coli (minimal inhibitory concentration (MIC<5 microM)). Synonyms: CPRF-Ea. | |
| Caerulein precursor-related fragment Eb | The source of Caerulein precursor-related fragment Eb is Rana esculenta. This peptide has no sequence similarity with antimicrobial peptides isolated from other species of ranid frogs. It potently and selectively inhibits the growth of the Gram-positive bacterium Escherichia coli (minimal inhibitory concentration (MIC<5 microM)). Synonyms: CPRF-Eb. | |
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