Home >> Peptides

Peptides

Products for  Peptides

  1. Cat.No. Product Name Information
  2. GC68622 Acyl Carrier Protein (ACP) (65-74)

    Acyl Carrier Protein (ACP) (65-74) is an active fragment of the acyl carrier protein ACP.

    Acyl Carrier Protein (ACP) (65-74)  Chemical Structure
  3. GC31528 Adipokinetic Hormone (AKH) (24-32), locust Adipokinetic Hormone (AKH) (24-32), locust, isolated from locust corpora cardiaca, is a neurohormone that regulates lipid utilisation during flight. Adipokinetic Hormone (AKH) (24-32), locust  Chemical Structure
  4. GC33774 Adrenocorticotropic Hormone (ACTH) (1-10), human Adrenocorticotropic Hormone (ACTH) (1-10), human, an adrenocorticotropin hormone fragment, possesses a weak α-melanocyte stimulating hormone (α-MSH) potency only at high doses (100 and 1000 nM). Adrenocorticotropic Hormone (ACTH) (1-10), human  Chemical Structure
  5. GC35253 Adrenocorticotropic Hormone (ACTH) (1-39), human(TFA)

    1-39-Corticotropin (human)(TFA)

    Adrenocorticotropic Hormone (ACTH) (1-39), human(TFA) is a melanocortin receptor agonist. Adrenocorticotropic Hormone (ACTH) (1-39), human(TFA)  Chemical Structure
  6. GC35254 Adrenocorticotropic Hormone (ACTH) (1-39), rat

    ACTH (1-39) (mouse, rat)

    Adrenocorticotropic Hormone (ACTH) (1-39), rat is a potent melanocortin 2 (MC2) receptor agonist. Adrenocorticotropic Hormone (ACTH) (1-39), rat  Chemical Structure
  7. GC33788 Adrenocorticotropic Hormone (ACTH) (18-39), human (CLIP (human))

    Adrenocorticotropic Hormone (18-39), Corticotropin-like Intermediate Lobe Peptide, RPVKVYPNGAEDESAEAFPLEF

    Adrenocorticotropic Hormone (ACTH) (18-39), human (CLIP (human)) is a corticotropinlike intermediate lobe peptide, which is produced in the melanotrophs of the intermediate lobe of the pituitary. Adrenocorticotropic Hormone (ACTH) (18-39), human (CLIP (human))  Chemical Structure
  8. GC65059 Adrenocorticotropic Hormone (ACTH) (18-39), human TFA

    CLIP (human) (TFA)

    Adrenocorticotropic Hormone (ACTH) (18-39), human TFA is a corticotropinlike intermediate lobe peptide, which is is produced in the melanotrophs of the intermediate lobe of the pituitary. Adrenocorticotropic Hormone (ACTH) (18-39), human TFA  Chemical Structure
  9. GC33790 Adrenocorticotropic Hormone (ACTH) (4-10), human Adrenocorticotropic Hormone (ACTH) (4-10), human is a melanocortin 4 (MC4R) receptor agonist. Adrenocorticotropic Hormone (ACTH) (4-10), human  Chemical Structure
  10. GC42737 Adrenomedullin (1-12) (human) (trifluoroacetate salt) Adrenomedullin (1-12) is an N-terminal fragment of adrenomedullin (1-52). Adrenomedullin (1-12) (human) (trifluoroacetate salt)  Chemical Structure
  11. GC34230 Adrenomedullin (1-50), rat Adrenomedullin (1-50), rat is a 50 amino acid peptide, which induces a selective arterial vasodilation via activation of CGRP1 receptor. Adrenomedullin (1-50), rat  Chemical Structure
  12. GC35256 Adrenomedullin (11-50), rat Adrenomedullin (11-50), rat is the C-terminal fragment (11-50) of rat adrenomedullin. Adrenomedullin (11-50), rat  Chemical Structure
  13. GC42738 Adrenomedullin (13-52) (human) (trifluoroacetate salt) Adrenomedullin (13-52) is a truncated form of adrenomedullin (1-52). Adrenomedullin (13-52) (human) (trifluoroacetate salt)  Chemical Structure
  14. GC35257 Adrenomedullin (16-31), human Adrenomedullin (16-31), human is amino acid residues 16-31 fragment of human adrenomedullin (hADM). Adrenomedullin (16-31), human  Chemical Structure
  15. GC42741 Adrenomedullin (22-52) (human) (trifluoroacetate salt) Adrenomedullin (22-52) is a C-terminal fragment of adrenomedullin (1-52). Adrenomedullin (22-52) (human) (trifluoroacetate salt)  Chemical Structure
  16. GC33955 Adrenomedullin (AM) (1-52), human

    Human adrenomedullin-(1-52)-NH2

    Adrenomedullin (AM) (1-52), human is a 52-amino acid peptide, which affects cell proliferation and angiogenesis in cancer. Adrenomedullin (AM) (1-52), human  Chemical Structure
  17. GC32622 Adrenomedullin (AM) (13-52), human Adrenomedullin (AM) (13-52), human is a 40 amino acid peptide, which acts as an endothelium-dependent vasodilator agent. Adrenomedullin (AM) (13-52), human  Chemical Structure
  18. GC32615 Adrenomedullin (AM) (22-52), human (22-52-Adrenomedullin (human)) Adrenomedullin (AM) (22-52), human (22-52-Adrenomedullin (human)), an NH2 terminal truncated adrenomedullin analogue, is an adrenomedullin receptor antagonist, and also antagonizes the calcitonin generelated peptide (CGRP) receptor in the hindlimb vascular bed of the cat. Adrenomedullin (AM) (22-52), human (22-52-Adrenomedullin (human))  Chemical Structure
  19. GC11039 AF 12198 Type I IL-1 receptor antagonist AF 12198  Chemical Structure
  20. GC35264 AGA-(C8R) HNG17, Humanin derivative AGA-(C8R) HNG17, Humanin derivative is a potent humanin (HN) derivative. AGA-(C8R) HNG17, Humanin derivative  Chemical Structure
  21. GC61526 AGA-(C8R) HNG17, humanin derivative TFA AGA-(C8R) HNG17, humanin derivative TFA is a potent humanin (HN) derivative. AGA-(C8R) HNG17, humanin derivative TFA  Chemical Structure
  22. GC14867 Agitoxin 2 Shaker K+ channel blocker, potent Agitoxin 2  Chemical Structure
  23. GC15822 Akt/SKG Substrate Peptide substrate for Akt/PKB Akt/SKG Substrate Peptide  Chemical Structure
  24. GC35282 Alexamorelin Met 1 Alexamorelin Met 1  Chemical Structure
  25. GC68636 Alirinetide

    GM604

    Alirinetide (GM604) is a short peptide consisting of six amino acids. It can cross the blood-brain barrier and is used in research for various neurodegenerative diseases.

    Alirinetide  Chemical Structure
  26. GC19584 Alkaline Phosphatase

    10-50units/mg protein(37℃,pH 9.8)

    Alkaline Phosphatase  Chemical Structure
  27. GC35291 Allatostatin II Allatostatin II is a decapeptid. Allatostatin II  Chemical Structure
  28. GC35292 Allatostatin IV Allatostatin IV is an octapeptide. Allatostatin IV  Chemical Structure
  29. GC30940 Allergen Gal d 4 (46-61), chicken (Lysozyme C (46-61) (chicken))

    Lysozyme C (46-61) (chicken)

    Allergen Gal d 4 (46-61), chicken (Lysozyme C (46-61) (chicken)) is a hen egg white lysozyme peptide. Allergen Gal d 4 (46-61), chicken (Lysozyme C (46-61) (chicken))  Chemical Structure
  30. GC35304 Alpha 1(I) Collagen (614-639), human Alpha 1(I) Collagen (614-639), human is a peptide fragment of alpha-1 type I collagen. Alpha 1(I) Collagen (614-639), human  Chemical Structure
  31. GC32208 ALX 40-4C ALX 40-4C is a small peptide inhibitor of the chemokine receptor CXCR4, inhibits SDF-1 from binding CXCR4 with a Ki of 1 μM, and suppresses the replication of X4 strains of HIV-1; ALX 40-4C Trifluoroacetate also acts as an antagonist of the APJ receptor, with an IC50 of 2.9 μM. ALX 40-4C  Chemical Structure
  32. GC34386 ALX 40-4C Trifluoroacetate ALX 40-4C Trifluoroacetate is a small peptide inhibitor of the chemokine receptor CXCR4, inhibits SDF-1 from binding CXCR4 with a Ki of 1 μM, and suppresses the replication of X4 strains of HIV-1; ALX 40-4C Trifluoroacetate also acts as an antagonist of the APJ receptor, with an IC50 of 2.9 μM. ALX 40-4C Trifluoroacetate  Chemical Structure
  33. GC49262 Alytesin (trifluoroacetate salt) A neuropeptide with diverse biological activities Alytesin (trifluoroacetate salt)  Chemical Structure
  34. GC30514 AMARA peptide AMARA peptide is a substrate for SIK and AMPK. AMARA peptide  Chemical Structure
  35. GC34224 AMARA peptide TFA AMARA peptide (TFA) is a substrate for salt-inducible kinase (SIK) and adenosine monophosphate activated protein kinase (AMPK). AMARA peptide TFA  Chemical Structure
  36. GC35324 Amlodipine aspartic acid impurity Amlodipine aspartic acid impurity is the impurity of Amlodipine aspartic acid. Amlodipine aspartic acid impurity  Chemical Structure
  37. GC16513 Amylin Amylin, a 37-amino acid polypeptide, is a pancreatic hormone cosecreted with insulin that exerts unique roles in metabolism and glucose homeostasis. Amylin  Chemical Structure
  38. GA20710 Amylin (8-37) (human) Human IAPP (8-37), ATQRLANFLVHSSNNFGAILSSTNVGSNTY-amide, readily forms fibrils in vitro. Amylin (8-37) (human)  Chemical Structure
  39. GC35331 Amylin (8-37), rat

    Amylin (8-37) (mouse, rat)

    Amylin (8-37), rat is a truncated analog of native Amylin that selectively inhibits insulin-related glucose uptake and glycogen deposition in muscle tissue. Amylin (8-37), rat  Chemical Structure
  40. GA24066 Amylin (free acid) (human)

    IAPP (free acid) (human)

    Amylin (free acid) (human)  Chemical Structure
  41. GC42796 Amylin (human) (trifluoroacetate salt)

    IAPP (human), Islet Amyloid Polypeptide (human)

    Amylin is a 37-residue peptide hormone secreted from pancreatic β-cells that reduces food intake, decreases glucagon secretion, slows gastric emptying, and increases satiety. Amylin (human) (trifluoroacetate salt)  Chemical Structure
  42. GC35332 Amylin (IAPP), feline Amylin (IAPP), feline is a 37-amino acid polypeptide from feline. Amylin (IAPP), feline  Chemical Structure
  43. GC60581 Amylin (IAPP), feline TFA Amylin (IAPP), feline TFA is a 37-amino acid polypeptide from feline. Amylin (IAPP), feline TFA  Chemical Structure
  44. GC35333 Amylin, amide, rat

    Amylin (rat)

    Amylin, amide, rat is a potent and high affinity ligand of Amylin receptor AMY1 and AMY3 receptors and variably of AMY2 receptors; binding studies are generally used for the latter receptor. Amylin, amide, rat  Chemical Structure
  45. GC35334 Amyloid β Peptide (42-1)(human) Amyloid β Peptide (42-1)(human) is the inactive form of Amyloid β Peptide (1-42). Amyloid β Peptide (42-1)(human)  Chemical Structure
  46. GC35335 Amyloid β-peptide (1-40) rat Amyloid β-peptide (1-40) rat is a rat form of the amyloid β-peptide, which accumulates as an insoluble extracellular deposit around neurons, giving rise to the senile plaques associated with Alzheimer's disease (AD). Amyloid β-peptide (1-40) rat  Chemical Structure
  47. GA20721 Amyloid β-Protein (1-12) Amyloid β-Protein (1-12)  Chemical Structure
  48. GA20722 Amyloid β-Protein (1-14) The N-terminal Aβ fragments Aβ1-14, Aβ1-15 (H-6368), and Aβ1-16 (H-2958) are elevated in cell media and in CSF in response to γ-secretase inhibitor treatment. The presence of these small peptides is consistent with a catabolic amyloid precursor protein cleavage pathway by β- followed by α-secretase. It has been shown that Aβ1-14, Aβ1-15, and Aβ1-16 increase dose-dependently in response to γ-secretase inhibitor treatment while Aβ1-42 levels are unchanged. Amyloid β-Protein (1-14)  Chemical Structure
  49. GA20724 Amyloid β-Protein (1-24) Amyloid β-Protein (1-24)  Chemical Structure
  50. GA20725 Amyloid β-Protein (1-37) Amyloid β-Protein (1-37) correlates moderately with Mini-Mental State Examination (MMSE) scores in Alzheimer disease. Amyloid β-Protein (1-37)  Chemical Structure
  51. GA20726 Amyloid β-Protein (1-38) Like Aβ (25-35) (H-1192), the Aβ fragment (1-38) destabilizes calcium homeostasis and renders human cortical neurones vulnerable to environmental insults. Amyloid β-Protein (1-38)  Chemical Structure
  52. GA20727 Amyloid β-Protein (1-39) Small quantities of Aβ37, 38 and 39 can be detected in CSF together with Aβ40, the most abundant Aβ homolog, Aβ42, and N-terminally truncated amyloid peptides. The relative amounts depend on the variant of Alzheimer's disease. The C-terminally truncated amyloid peptides are also found in amyloid plaques. Amyloid β-Protein (1-39)  Chemical Structure
  53. GA20728 Amyloid β-Protein (1-40) (scrambled) Amyloid β-Protein (1-40) (scrambled)  Chemical Structure
  54. GA20729 Amyloid β-Protein (1-40) amide Amyloid β-Protein (1-40) amide  Chemical Structure
  55. GA24067 Amyloid β-Protein (1-40)-Lys(biotinyl) amide

    Abeta (1-40) Lys (Biotin) amide

    For immobilization of Aβ40. Amyloid β-Protein (1-40)-Lys(biotinyl) amide  Chemical Structure
  56. GA20733 Amyloid β-Protein (1-42)

    Compared to the inner salt, the HCl salt of Aβ42 aggregates more readily at pH 7.4.

    Amyloid β-Protein (1-42)  Chemical Structure
  57. GA20730 Amyloid β-Protein (1-42) (HFIP-treated) H-7442 was obtained by dissolving Amyloid β-Protein (1-42) (H-1368) in HFIP, aliquoting, and removing the solvent as described in the literature. Amyloid β-Protein (1-42) (HFIP-treated)  Chemical Structure
  58. GA20731 Amyloid β-Protein (1-42) (scrambled) Amyloid β-Protein (1-42) (scrambled)  Chemical Structure
  59. GA24068 Amyloid β-Protein (1-42)-Lys(biotinyl) amide

    Beta-Amyloid (1-42)-Lys(biotin) amide

    For immobilization of Aβ42. Amyloid β-Protein (1-42)-Lys(biotinyl) amide  Chemical Structure
  60. GA20736 Amyloid β-Protein (1-43) Amyloid β-Protein (1-43) is more prone to aggregation and has higher toxic properties than the long-known Aβ1-42. Amyloid β-Protein (1-43)  Chemical Structure
  61. GA20737 Amyloid β-Protein (1-46) Precursor of the secreted amyloid β-protein (1-40) and (1-42). The identification of amyloid-β-protein (1-46) led to the identification of a zeta-cleavage site between the known γ- and ε-cleavage sites within the transmembrane domain of amyloid-β precursor protein (APP). Amyloid β-Protein (1-46)  Chemical Structure
  62. GA20738 Amyloid β-Protein (1-6) Experiments using sub-peptides of Aβ42 revealed that the epitope identified by the antibody A8, as described by Ying and coworkers, lies within the 1-6 region of Aβ. The antibody displays high affinity for soluble Aβ42 oligomers in the molecular weight range of 16.5-25 kDa, and detected target antigen in brain sections from senescence-accelerated SAMP 8 mice. Amyloid β-Protein (1-6)  Chemical Structure
  63. GA20739 Amyloid β-Protein (1-6) amide Experiments using sub-peptides of Aβ42 revealed that the epitope identified by the antibody A8, as described by Ying and coworkers, lies within the 1-6 region of Aβ. The antibody displays high affinity for soluble Aβ42 oligomers in the molecular weight range of 16.5-25 kDa, and detected target antigen in brain sections from senescence-accelerated SAMP 8 mice. Amidated or acetylated and amidated forms of the sequence were used for example for quantitative structure retention relationships (QSRR) experiments. The latter could allow prediction of reversed-phase high-performance liquid chromatography (HPLC) retention of peptides, as reported by Kaliszan and coworkers. Amyloid β-Protein (1-6) amide  Chemical Structure
  64. GA20720 Amyloid β-Protein (10-35) Amyloid β-protein (10-35), YEVHHQKLVFFAEDVGSNKGAIIGLM, was used as a truncated peptide model for the full-length amyloid β-proteins (1-40) and (1-42) in high-resolution structural studies. In contrast to the full-length amyloid β-proteins, amyloid β-protein (10-35) allowed the controlled and reproducible formation of homogeneous fibrils from aqueous solutions of defined pH, ionic strength and soluble peptide concentration necessary for high-resolution structural studies. Amyloid β-Protein (10-35)  Chemical Structure
  65. GA20723 Amyloid β-Protein (11-42) Amyloid β-Protein (11-42)  Chemical Structure
  66. GA20740 Amyloid β-Protein (16-20) KLVFF corresponds to the minimum sequence binding the full-length amyloid β protein. The pentapeptide acts as a β-sheet breaker. Amyloid β-Protein (16-20)  Chemical Structure
  67. GA20741 Amyloid β-Protein (16-22) Self-assembling Aβ sequence. Amyloid β-Protein (16-22)  Chemical Structure
  68. GA20742 Amyloid β-Protein (17-40) Cleavage of APP by alpha- and gamma-secretase (i.e. the non-amyloidogenic pathway) yields p3 peptide, a mix of Aβ 17-40 and Aβ 17-42. p3 is a major constituent of diffuse plaques observed in AD brains and pre-amyloid plaques in people affected by Down syndrome. Amyloid β-Protein (17-40)  Chemical Structure
  69. GA24069 Amyloid β-Protein (17-42) Cleavage of APP by alpha- and gamma secretase (i. Amyloid β-Protein (17-42)  Chemical Structure
  70. GA20744 Amyloid β-Protein (2-42) Aβ 2-42 could be a biomarker for differentiating AD from other degenerative dementias, such as frontotemporal dementias (FTD). The peptide promotes phagocytosis by macrophages. Amyloid β-Protein (2-42)  Chemical Structure
  71. GA20743 Amyloid β-Protein (20-29) FAEDVGSNKG. Amyloid β-Protein (20-29)  Chemical Structure
  72. GA20745 Amyloid β-Protein (25-35) amide The amidation of amyloid β-protein (25-35) leads to a product in which the amyloidogenic capacity of amyloid β-protein (25-35) has been strongly reduced, while the neurotoxic activity was found to be independent of the aggregated state of the peptide. Amyloid β-Protein (25-35) amide  Chemical Structure
  73. GA20747 Amyloid β-Protein (3-40) Amyloid β-Protein (3-40)  Chemical Structure
  74. GA20748 Amyloid β-Protein (3-42) The N-terminally truncated Aβ42 may be formed in increased amounts as AD progresses. Aβ 3-42 is the precursor of the Pyr-peptide. (Pyr³)-Aβ 3-42 positive plaques are resistant to age-dependent degradation likely due to their high stability and propensity to aggregate. Amyloid β-Protein (3-42)  Chemical Structure
  75. GA20746 Amyloid β-Protein (33-42) GLMVGGVVIA, a partial sequence of β-amyloid protein which is used for raising antibodies against Aβ 1-42. Li et al. studied the aggregation behavior of this and other Aβ 1-42 C-terminal fragments. Amyloid β-Protein (33-42)  Chemical Structure
  76. GA20749 Amyloid β-Protein (35-25) Reverse sequence of Aβ 25-35, inactive control. Amyloid β-Protein (35-25)  Chemical Structure
  77. GA20750 Amyloid β-Protein (36-38) Amyloid β-Protein (36-38)  Chemical Structure
  78. GA20751 Amyloid β-Protein (37-39) Amyloid β-Protein (37-39)  Chemical Structure
  79. GA20754 Amyloid β-Protein (4-42) Aβ 4-42 could be one of the earliest and most prominent Aβ species deposited in AD brain. Sequencing of amyloid plaque cores showed that 64% of the isolated Aβ had a phenylalanine at its N-terminus, and indeed, IP/MS experiments identified Aβ 4-42 as a major Aβ species in AD patients. Additionally, Aβ 4-42 was found to be a component of cotton wool plaques in familial AD patients with the V261I PS1 mutation. Aβ 4-42 was discovered as well in amyloid deposits from vascular dementia and familial Danish dementia patients. These observations indicate that Aβ 4-42 may contribute to the development of multiple CNS diseases. Amyloid β-Protein (4-42)  Chemical Structure
  80. GA20753 Amyloid β-Protein (40-1) Inactive control Amyloid β-Protein (40-1)  Chemical Structure
  81. GA20752 Amyloid β-Protein (40-1) Reverse sequence of Aβ 1-40. Amyloid β-Protein (40-1)  Chemical Structure
  82. GA20755 Amyloid β-Protein (5-42) Abeta 5-42 is produced from amyloid precursor protein by action of caspases. It is deposited in Alzheimer's disease brain as well, but less prone to aggregation. Amyloid β-Protein (5-42)  Chemical Structure
  83. GA20756 Amyloid β-Protein (6-20) Amyloid β-Protein (6-20)  Chemical Structure
  84. GA20718 Amyloid β/A4 Protein Precursor₇₇₀ (667-676) The peptide substrate APP (667-676), SEVKMDAEFR, corresponds to the wild-type amyloid precursor protein (APP) β-secretase cleavage site. SEVKMDAEFR has been used for assaying β-secretase activity. Amyloid β/A4 Protein Precursor₇₇₀ (667-676)  Chemical Structure
  85. GA20719 Amyloid β/A4 Protein Precursor₇₇₀ (740-770) Amyloid β/A4 Protein Precursor??? (740-770) corresponds to a C-terminal amyloid precursor protein (APP) fragment known as C31. This fragment is intracellularly generated by proteolytic cleavage of APP by caspases-8 and -9. C31 had a proapoptotic and a cytotoxic effect on neuronal cells and was shown to be present in brains of Alzheimer's disease (AD) patients. In cultured cells caspase cleavage of APP was induced by amyloid β-protein and the subsequent generation of C31 contributed to the apoptotic cell death associated with amyloid β-protein. Amyloid precursor binding protein BP1 (APP-BP1) a cell cycle protein which is increased in AD brain was demonstrated to bind to the C31 region of APP and to mediate APP-induced apoptosis. Amyloid β/A4 Protein Precursor₇₇₀ (740-770)  Chemical Structure
  86. GP10118 Amyloid Beta-Peptide (1-40) (human)

    Amyloid β-Peptide (1-40) (human), (C194H295N53O58S1), a peptide with the sequence H2N-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA-OH, MW= 4329.8. Amyloid beta (Aβ or Abeta) is a peptide of 36–43 amino acids that is processed from the Amyloid precursor protein.

    Amyloid Beta-Peptide (1-40) (human)  Chemical Structure
  87. GP10049 Amyloid Beta-Peptide (12-28) (human) Amyloid Beta-Peptide (12-28) (human) is a peptide fragment of amyloid beta protein (1-42) (Aβ (1-42)). Amyloid Beta-Peptide (12-28) (human)  Chemical Structure
  88. GP10082 Amyloid Beta-peptide (25-35) (human) Amyloid beta(Aβ)-peptide (25-35) (human) is an fragment of Alzheimer's Amyloid beta peptide which is commonly found in the brains of people with Alzheimer's disease (AD) and is a major component of Alzheimer's amyloid plaques. Amyloid Beta-peptide (25-35) (human)  Chemical Structure
  89. GC18339 Amyloid β-Peptide (1-42) human

    β-Amyloid (1-42), human

    Amyloid β-Peptide (1-42) human is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.

    Amyloid β-Peptide (1-42) human   Chemical Structure
  90. GP10057 Amyloid β-Peptide (10-20) (human)

    Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe

    Amyloid β-Peptide (10-20) (human)  Chemical Structure
  91. GP10094 Amyloid β-peptide (10-35), amide

    H2N-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-NH2

    Amyloid β-peptide (10-35), amide  Chemical Structure
  92. GP10097 Amyloid β-Protein (1-15)

    H2N-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-OH

    Amyloid β-Protein (1-15)  Chemical Structure
  93. GC45382 Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt)

    Aβ (1-28), Aβ28

      Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  94. GC42798 Amyloid-β (1-38) Peptide (trifluoroacetate salt)

    β-Amyloid (1-38), Aβ38, Aβ (1-38)

    Amyloid-β (1-38) (Aβ38) peptide is a fragment of the Aβ42 peptide. Amyloid-β (1-38) Peptide (trifluoroacetate salt)  Chemical Structure
  95. GC46850 Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt)

    Aβ (1-40), Aβ40

    A neuropeptide with diverse biological activities Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  96. GC46851 Amyloid-β (1-42) Peptide (trifluoroacetate salt)

    Aβ (1-42), Aβ42

    A 42-amino acid protein fragment of amyloid-β Amyloid-β (1-42) Peptide (trifluoroacetate salt)  Chemical Structure
  97. GC42801 Amyloid-β (1-8) Peptide

    Aβ (1-8)

    Amyloid-β (1-8) is a wild-type control for the mutation-containing amyloid-β (1-8, A2V) peptide . Amyloid-β (1-8) Peptide  Chemical Structure
  98. GC42802 Amyloid-β (1-8, A2V) Peptide

    Aβ (1-8, A2V), Aβ (1-8) mutant, Amyloid-β (1-8) dominant negative

    Amyloid-β (1-8, A2V) is a truncated form of amyloid-β (Aβ) that contains a valine to alanine substitution at position 2 of the Aβ numbering convention (Aβ A2V), which corresponds to position 673 of the amyloid precursor protein (APP) numbering convention (APP A673V). Amyloid-β (1-8, A2V) Peptide  Chemical Structure
  99. GC42799 Amyloid-β (17-40) Peptide (human) (trifluoroacetate salt)

    Aβ (17-40)

    Amyloid-β (Aβ) (17-40) is a 24-residue fragment of the Aβ protein that is formed via post-translational processing of amyloid precursor protein (APP) by α- and γ-secretases. Amyloid-β (17-40) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  100. GC42800 Amyloid-β (17-42) Peptide (human) (trifluoroacetate salt)

    Aβ (17-42), LVFFAEDVGSNKGAIIGLMVGGVVIA

    Amyloid-β (Aβ) (17-42) is a 26-residue fragment of the Aβ protein that is formed via post-translational processing of amyloid precursor protein (APP) by α- and γ-secretases. Amyloid-β (17-42) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  101. GC40127 Amyloid-β (22-35) Peptide (trifluoroacetate salt)

    Aβ (22-35)

    Amyloid-β (Aβ) (22-35) is a 13-residue fragment of Aβ that corresponds to residues 693-705 of the human amyloid precursor protein (APP) full-length sequence. Amyloid-β (22-35) Peptide (trifluoroacetate salt)  Chemical Structure

Items 401 to 500 of 2095 total

per page
  1. 3
  2. 4
  3. 5
  4. 6
  5. 7

Set Descending Direction