Date published: 2025-10-4

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p38 alpha Inhibitors

Santa Cruz Biotechnology now offers a broad range of p38 alpha Inhibitors for use in various applications. p38 alpha Inhibitors target the p38 alpha mitogen-activated protein kinase (MAPK), a crucial enzyme involved in cellular responses to stress and inflammatory signals. These inhibitors are essential tools for researchers studying the regulation of cellular processes such as apoptosis, differentiation, and autophagy. By inhibiting p38 alpha, scientists can explore its role in the MAPK signaling pathway, which is integral to understanding how cells react to external stimuli like cytokines, UV radiation, and osmotic shock. p38 alpha Inhibitors provide insights into the mechanisms of signal transduction and the modulation of gene expression in response to stress. They are particularly valuable in investigating the cellular and molecular basis of inflammation, as p38 alpha is a key player in the production of pro-inflammatory cytokines. These inhibitors facilitate the study of protein-protein interactions and phosphorylation events that govern cell fate decisions. Additionally, p38 alpha Inhibitors are used to understand the cross-talk between different signaling pathways and their collective impact on cellular behavior. Researchers leverage these inhibitors to dissect the intricate network of signals that maintain cellular homeostasis and respond to environmental changes. The ability to modulate p38 alpha activity allows for a deeper comprehension of the cellular stress response and its implications in various biological contexts. View detailed information on our available p38 alpha Inhibitors by clicking on the product name.

Items 21 to 29 of 29 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

SCIO 469 hydrochloride

309913-83-5sc-361353
sc-361353A
10 mg
50 mg
$205.00
$865.00
2
(0)

SCIO 469 hydrochloride is a selective p38 alpha MAP kinase inhibitor characterized by its unique interaction dynamics with the enzyme's active site. It forms stable complexes through a combination of van der Waals forces and electrostatic interactions, effectively altering the enzyme's conformation. This compound exhibits a distinctive reaction kinetics profile, allowing for precise modulation of downstream signaling pathways, thereby providing a deeper understanding of p38 alpha's role in cellular processes.

p38 MAP Kinase Inhibitor VIII

321351-00-2sc-203173
5 mg
$422.00
2
(1)

p38 MAP Kinase Inhibitor VIII is a potent inhibitor that selectively targets the p38 alpha isoform, showcasing unique binding affinity through hydrogen bonding and hydrophobic interactions. Its structural design facilitates a specific fit within the kinase domain, leading to altered phosphorylation patterns. The compound's kinetic properties reveal a slow dissociation rate, enhancing its efficacy in modulating cellular stress responses and inflammatory signaling pathways, thus providing insights into kinase regulation.

JX-401

349087-34-9sc-200687
sc-200687A
1 mg
10 mg
$62.00
$131.00
1
(0)

JX-401 is a selective p38 alpha inhibitor characterized by its unique interaction profile, which includes a combination of van der Waals forces and electrostatic interactions that stabilize its binding within the active site. This compound exhibits a distinctive conformational flexibility, allowing it to adapt to various substrate orientations. Its reaction kinetics indicate a prolonged residence time on the target, which may influence downstream signaling cascades and cellular responses.

VX 702

745833-23-2sc-361400
10 mg
$132.00
1
(0)

VX 702 is a selective inhibitor of p38 alpha, notable for its intricate binding dynamics that involve hydrogen bonding and hydrophobic interactions, enhancing its affinity for the target enzyme. The compound's structural rigidity contributes to its specificity, while its unique molecular conformation facilitates effective steric hindrance against competing substrates. Additionally, VX 702 demonstrates a favorable kinetic profile, characterized by a slow off-rate, which may modulate the enzyme's activity over extended periods.

Poly-ε-cbz-L-lysine

25931-47-9sc-396758
1 g
$174.00
(0)

Poly-ε-cbz-L-lysine exhibits remarkable selectivity for p38 alpha through its unique polymeric structure, which allows for multiple points of interaction with the enzyme's active site. This compound's flexible backbone enhances its ability to adapt to conformational changes in the target, promoting effective binding. Its distinct charge distribution facilitates electrostatic interactions, while the presence of aromatic side chains contributes to enhanced stability and specificity in enzyme inhibition.

CMPD1

41179-33-3sc-203138
10 mg
$250.00
4
(3)

CMPD1 demonstrates a remarkable specificity for p38 alpha through its unique molecular architecture, which promotes strong hydrogen bonding and hydrophobic interactions within the enzyme's active site. This compound's conformational flexibility allows it to adapt to various binding environments, enhancing its interaction dynamics. Additionally, CMPD1's influence on phosphorylation states within the signaling cascade reveals its potential to modulate downstream effects, offering insights into cellular response mechanisms.

SB202190 hydrochloride

350228-36-3sc-222294
sc-222294A
1 mg
5 mg
$128.00
$495.00
13
(1)

SB202190 hydrochloride exhibits a selective binding profile for p38 alpha, facilitated by its unique structural features that allow for effective engagement with the enzyme's active site. The compound's spatial arrangement fosters optimal van der Waals interactions and electrostatic complementarity, enhancing its affinity. Furthermore, its ability to influence the enzyme's allosteric sites contributes to altered reaction kinetics, providing insights into the modulation of signaling pathways.

BMS 582949

623152-17-0sc-507348
5 mg
$510.00
(0)

Losmapimod

585543-15-3sc-489299
sc-489299A
10 mg
50 mg
$224.00
$809.00
(0)

Losmapimod exhibits a distinctive binding affinity for p38 alpha, characterized by its ability to form intricate electrostatic interactions and a well-defined hydrophobic pocket. Its unique structural features facilitate a dynamic conformational change upon binding, optimizing its fit within the enzyme's active site. This adaptability not only influences the enzyme's catalytic activity but also alters the kinetics of substrate phosphorylation, providing a nuanced understanding of its role in cellular signaling pathways.