Date published: 2026-5-30

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GRAMD1B Inhibitors

GRAM Domain Containing 1B (GRAMD1B) is a protein that has garnered attention in the field of cellular biology due to its involvement in lipid metabolism and transport. The GRAMD1B protein is characterized by the presence of a GRAM domain, a feature common to a family of proteins implicated in various cellular processes, including membrane trafficking and signal transduction. GRAMD1B's specific role in the regulation of intracellular lipid distribution and homeostasis marks it as a critical player in cellular physiology. It has been suggested that GRAMD1B may influence the formation and maintenance of lipid droplets, as well as the transport of lipids between cellular organelles. Understanding the function of GRAMD1B is crucial for elucidating the complex networks that govern cellular lipid metabolism, an area of research that has significant implications for the understanding of metabolic disorders and diseases linked to lipid dysregulation.

The inhibition of GRAMD1B, like that of many proteins involved in cellular metabolism, can occur through a variety of mechanisms. Given the lack of specificity in targeting proteins such as GRAMD1B with small molecules, research into its inhibition may focus on genetic approaches such as RNA interference (RNAi) or CRISPR/Cas9-mediated gene editing to reduce or knock out its expression. These methods allow for the direct investigation of GRAMD1B's function by observing the phenotypic consequences of its decreased activity. Alternatively, the modulation of signaling pathways upstream of GRAMD1B that control its expression or activity could represent another avenue for inhibition. For example, transcription factors or kinases that regulate the synthesis of GRAMD1B could be targeted indirectly to reduce its levels. Understanding the inhibition mechanisms of GRAMD1B is not only important for dissecting its role in lipid metabolism but also for exploring strategies for conditions associated with lipid imbalance.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Fluvastatin

93957-54-1sc-279169
50 mg
$250.00
(0)

Fluvastatin inhibits GRAMD1B by blocking HMG-CoA reductase, a key enzyme in cholesterol biosynthesis. Reduced cholesterol levels lead to decreased lipid raft formation and disrupt membrane organization.

Simvastatin

79902-63-9sc-200829
sc-200829A
sc-200829B
sc-200829C
50 mg
250 mg
1 g
5 g
$31.00
$89.00
$135.00
$443.00
13
(1)

Simvastatin works similarly to fluvastatin by inhibiting HMG-CoA reductase, leading to reduced cholesterol levels and disrupting GRAMD1B function by altering membrane lipid composition.

Pravastatin

81093-37-0sc-222188
50 mg
$408.00
1
(1)

Pravastatin inhibits cholesterol biosynthesis via HMG-CoA reductase inhibition, affecting membrane lipid composition and disrupting GRAMD1B function.

Atorvastatin

134523-00-5sc-337542A
sc-337542
50 mg
100 mg
$257.00
$505.00
9
(1)

Atorvastatin inhibits HMG-CoA reductase, reducing cholesterol levels and altering membrane lipid composition to impair GRAMD1B function.

Lovastatin

75330-75-5sc-200850
sc-200850A
sc-200850B
5 mg
25 mg
100 mg
$29.00
$90.00
$339.00
12
(1)

Lovastatin inhibits HMG-CoA reductase, reducing cholesterol synthesis and affecting GRAMD1B by altering membrane lipid composition.

Mevastatin (Compactin)

73573-88-3sc-200853
sc-200853A
10 mg
50 mg
$77.00
$179.00
18
(1)

Mevastatin inhibits HMG-CoA reductase, leading to reduced cholesterol levels and interfering with GRAMD1B through membrane lipid changes.

Rosuvastatin

287714-41-4sc-481834
10 mg
$145.00
8
(0)

Rosuvastatin inhibits HMG-CoA reductase, lowering cholesterol levels, and disrupting GRAMD1B by altering membrane lipid composition.

Itraconazole

84625-61-6sc-205724
sc-205724A
50 mg
100 mg
$78.00
$142.00
23
(1)

Itraconazole inhibits fungal ergosterol synthesis, which could alter membrane lipid composition and affect GRAMD1B indirectly in fungal cells.

Amphotericin B

1397-89-3sc-202462
sc-202462A
sc-202462B
100 mg
500 mg
1 g
$70.00
$142.00
$223.00
10
(1)

Amphotericin B disrupts fungal cell membranes by binding to ergosterol, potentially impacting GRAMD1B indirectly through membrane changes.