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AB141416

Pepstatin A, aspartic protease inhibitor

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(3 Publications)

MW 685.9 Da, Purity >90%. Achieve your results faster with highly validated, pure and trusted compounds.

View Alternative Names

ADAM metallopeptidase domain 9, ADAM9_HUMAN, Angiotensin forming enzyme precursor, Angiotensinogenase, Angiotensinogenase precursor, CATD_HUMAN, CATL, CATL1_HUMAN, CD, CLN10, CORD9, CPSD, CTSD, CTSL, CTSL1, Cathepsin D, Cathepsin D heavy chain, Cathepsin L, Cathepsin L1, Cathepsin L1 light chain, Cellular disintegrin-related protein, Ceroid lipofuscinosis neuronal 10, Cone rod dystrophy 9, Disintegrin and metalloproteinase domain-containing protein 9, Epididymis secretory sperm binding protein Li 130P, FLJ10761, FLJ31037, HEL S 130P, HNFJ2, Lysosomal aspartyl peptidase, Lysosomal aspartyl protease, MCMP, MDC 9, MEP, MGC123162, MGC2311, Major excreted protein, Meltrin-gamma, Metalloprotease/disintegrin/cysteine-rich protein 9, Mltng, Myeloma cell metalloproteinase, PGA, PGA3, PGA5, Pepsin, Pepsin A, Pepsin A 3, Pepsin A 4, Pepsin A 5, Pepsinogen, Pepsinogen 3, Pepsinogen 4, Pepsinogen 5, REN, RENI_HUMAN, Ren1, Renin, Renin precursor renal, angiotensin-forming enzyme, cathepsin L, 1 b, cb15, ctsl1b, hgg1, wu:fb30g09

1 Images
Chemical Structure - Pepstatin A, aspartic protease inhibitor (AB141416)
  • Chemical Structure

Lab

Chemical Structure - Pepstatin A, aspartic protease inhibitor (AB141416)

2D chemical structure image of ab141416, Pepstatin A, aspartic protease inhibitor

Key facts

CAS number

26305-03-3

Purity

>90%

Form

Solid

form

Molecular weight

685.9 Da

Molecular formula

C<sub>3</sub><sub>4</sub>H<sub>6</sub><sub>3</sub>N<sub>5</sub>O<sub>9</sub>

PubChem

5478883

Nature

Synthetic

Solubility

Soluble in ethanol to 1 mg/ml with heating

Biochemical name

Pepstatin

Canonical smiles

CC(C)CC(C(CC(=O)O)O)NC(=O)C(C)NC(=O)CC(C(CC(C)C)NC(=O)C(C(C)C)NC(=O)C(C(C)C)NC(=O)CC(C)C)O

Isomeric smiles

C[C@@H](C(=O)N[C@@H](CC(C)C)[C@H](CC(=O)O)O)NC(=O)C[C@@H]([C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C)O

InChi

InChI=1S/C34H63N5O9/c1-17(2)12-23(37-33(47)31(21(9)10)39-34(48)30(20(7)8)38-27(42)14-19(5)6)25(40)15-28(43)35-22(11)32(46)36-24(13-18(3)4)26(41)16-29(44)45/h17-26,30-31,40-41H,12-16H2,1-11H3,(H,35,43)(H,36,46)(H,37,47)(H,38,42)(H,39,48)(H,44,45)/t22-,23-,24-,25-,26-,30-,31-/m0/s1

InChiKey

FAXGPCHRFPCXOO-LXTPJMTPSA-N

IUPAC Name

(3S,4S)-3-hydroxy-4-[[(2S)-2-[[(3S,4S)-3-hydroxy-6-methyl-4-[[(2S)-3-methyl-2-[[(2S)-3-methyl-2-(3-methylbutanoylamino)butanoyl]amino]butanoyl]amino]heptanoyl]amino]propanoyl]amino]-6-methylheptanoic acid

Product details

This product is manufactured by BioVision, an Abcam company and was previously called 1732 Pepstatin A. 1732-100 is the same size as the 100 mg size of ab141416.

Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Storage information
The product can be stored for up to 12 months

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Pepsin Cathepsin D Cathepsin L/MEP Renin and ADAM9 are proteolytic enzymes involved in various physiological processes. Pepsin a well-known aspartyl protease weights around 35 kDa and plays a role in the digestive system by breaking down proteins in the stomach. It originates from pepsinogen secreted by gastric chief cells and becomes active in the acidic environment of the stomach. Cathepsin D another aspartate protease is present in lysosomes and has a mass of approximately 48 kDa. It gets involved in protein degradation within cellular compartments. Cathepsin L weighing around 24 kDa functions in protein catabolism within lysosomes and extracellular matrix remodeling apart from the other two Renin begins the renin-angiotensin system involved in blood pressure regulation. It generates angiotensin I from angiotensinogen and is secreted by kidney juxtaglomerular cells. ADAM9 a membrane-anchored metalloprotease is expressed across several tissues including the heart and kidneys participating in shedding cell surface proteins.
Biological function summary

These proteases influence various cell functions beyond their mechanical actions. Pepsin facilitates protein digestion critical for nutrient absorption and metabolism. Cathepsin D plays a role in apoptosis and neurodegeneration contributing to cellular homeostasis and response to stress. Cathepsin L affects immune responses through antigen processing and presentation. Renin integral to the renin-angiotensin system controls fluid balance and blood pressure with effects on cardiovascular health. ADAM9 involved in cell signaling modulates cell-cell interactions and influences the inflammatory response particularly important in wound healing and tissue remodeling processes.

Pathways

These proteases participate in significant biological pathways essential for maintaining physiological balance. Pepsin through protein catabolism links to metabolic pathways that provide energy from nutrients. Cathepsin D interacts with the apoptosis pathway and is involved in lysosomal degradation pathways. Cathepsin L part of immune response pathways facilitates antigen processing in the adaptive immune system. Renin directly engages in the renin-angiotensin-aldosterone pathway affecting cardiovascular functions and blood pressure. ADAM9 connects to the Notch signaling pathway important for cell differentiation and communication. These pathways demonstrate the interconnected roles of these proteases with other proteins like angiotensin-converting enzyme (ACE) and matrix metalloproteinases (MMPs).

These proteases associate with significant health conditions. Pepsin as part of excessive acid release can contribute to peptic ulcers and gastroesophageal reflux disease (GERD). Cathepsin D has links to neurodegenerative disorders including Alzheimer's disease where dysregulated proteolysis affects neuronal survival. Cathepsin L connects to cancers given its role in degrading extracellular matrix components which aid tumor metastasis. Renin's dysregulation associates with hypertension where its excessive activity leads to elevated blood pressure through continued angiotensin production. ADAM9 has connections to cancer particularly in promoting tumor invasiveness due to its role in modulating cell surface receptors. These proteases highlight critical points in pathogenesis where they interlink with proteins like amyloid precursor protein (APP) in Alzheimer's or interleukins in inflammation-related conditions.

Product protocols

Publications (3)

Recent publications for all applications. Explore the full list and refine your search

Foods (Basel, Switzerland) 12: PubMed36981165

2023

Protein and Lipid Digestibility of Pasture-Raised and Grain-Finished Beef: An In Vitro Comparison.

Applications

Unspecified application

Species

Unspecified reactive species

Lovedeep Kaur,Amrutha Elamurugan,Feng Ming Chian,Xianqian Zhu,Mike Boland

Foods (Basel, Switzerland) 10: PubMed33804354

2021

Effects of Pulsed Electric Field Processing and Sous Vide Cooking on Muscle Structure and In Vitro Protein Digestibility of Beef Brisket.

Applications

Unspecified application

Species

Unspecified reactive species

Feng Ming Chian,Lovedeep Kaur,Indrawati Oey,Thierry Astruc,Suzanne Hodgkinson,Mike Boland

Foods (Basel, Switzerland) 10: PubMed33557126

2021

Physico-Chemical Characteristics and In Vitro Gastro-Small Intestinal Digestion of New Zealand Ryegrass Proteins.

Applications

Unspecified application

Species

Unspecified reactive species

Lovedeep Kaur,Harmandeepsingh Lamsar,Ignacio F López,Manon Filippi,Dayna Ong Shu Min,Kévin Ah-Sing,Jaspreet Singh
View all publications

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