Date published: 2026-5-30

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Gm996 Inhibitors

Gm996 inhibitors are chemical compounds designed to specifically target and regulate the activity of the Gm996 protein, a lesser-known entity within the family of GTPases or signaling proteins. These inhibitors generally work by binding to critical domains of the Gm996 protein, effectively modulating its function by preventing its natural interactions with other cellular components. Gm996, like other GTPases, is involved in cellular signaling pathways and influences diverse cellular processes such as growth, differentiation, and intracellular trafficking. By inhibiting Gm996, these compounds can influence the regulatory dynamics of these pathways, altering how signals are transmitted and processed within cells.

The development of Gm996 inhibitors requires a deep understanding of the structural biology of the Gm996 protein. Many inhibitors are designed based on the specific three-dimensional configuration of the GTP-binding pocket or other critical interaction sites. Structural studies often guide the rational design of these molecules to ensure they effectively target Gm996 with high affinity and selectivity. This specificity is essential to minimize off-target effects, which can disrupt other signaling proteins with similar structural features. The chemistry of Gm996 inhibitors may vary, with some compounds being small molecules, while others may be larger entities, such as peptides or nucleic acid-based inhibitors. These inhibitors are key tools for studying the biological role of Gm996 and the broader signaling pathways in which it participates.

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Items 1 to 10 of 12 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Genistein

446-72-0sc-3515
sc-3515A
sc-3515B
sc-3515C
sc-3515D
sc-3515E
sc-3515F
100 mg
500 mg
1 g
5 g
10 g
25 g
100 g
$45.00
$164.00
$200.00
$402.00
$575.00
$981.00
$2031.00
46
(1)

A tyrosine kinase inhibitor that can disrupt cell signaling involved in the maintenance of cell junctions, potentially affecting AJM1's role within them.

Staurosporine

62996-74-1sc-3510
sc-3510A
sc-3510B
100 µg
1 mg
5 mg
$82.00
$153.00
$396.00
113
(4)

A potent kinase inhibitor that can alter multiple signaling pathways, possibly affecting AJM1's function or localization.

GW 5074

220904-83-6sc-200639
sc-200639A
5 mg
25 mg
$106.00
$417.00
10
(1)

An inhibitor of Raf kinase which can disrupt downstream signaling that may be crucial for the proper functioning of AJM1.

LY 294002

154447-36-6sc-201426
sc-201426A
5 mg
25 mg
$123.00
$400.00
148
(1)

A PI3K inhibitor that can affect the PI3K/Akt signaling pathway, which is involved in cell survival and junction integrity, potentially influencing AJM1 activity.

Y-27632, free base

146986-50-7sc-3536
sc-3536A
5 mg
50 mg
$186.00
$707.00
88
(1)

A ROCK inhibitor that can affect cytoskeleton dynamics and tension at cell junctions, possibly impacting AJM1's association with those junctions.

Cytochalasin D

22144-77-0sc-201442
sc-201442A
1 mg
5 mg
$165.00
$486.00
64
(4)

An actin polymerization inhibitor that can disrupt cytoskeletal organization, potentially altering AJM1's cellular localization and function.

Thapsigargin

67526-95-8sc-24017
sc-24017A
1 mg
5 mg
$136.00
$446.00
114
(2)

A SERCA pump inhibitor that leads to increased cytosolic calcium levels, potentially affecting cellular processes that involve AJM1.

Brefeldin A

20350-15-6sc-200861C
sc-200861
sc-200861A
sc-200861B
1 mg
5 mg
25 mg
100 mg
$31.00
$53.00
$124.00
$374.00
25
(3)

Disrupts Golgi apparatus function and can affect protein trafficking to the membrane, potentially impacting AJM1's delivery to cell junctions.

U-0126

109511-58-2sc-222395
sc-222395A
1 mg
5 mg
$64.00
$246.00
136
(2)

An MEK inhibitor that can interfere with the MAPK/ERK pathway, possibly affecting AJM1-related signaling processes.

(S)-(−)-Blebbistatin

856925-71-8sc-204253
sc-204253A
sc-204253B
sc-204253C
1 mg
5 mg
10 mg
25 mg
$72.00
$265.00
$495.00
$968.00
(2)

An inhibitor of myosin II ATPase activity that can alter myosin II function and thus potentially affect AJM1's role in cell contractility and junction formation.