Date published: 2026-4-1

1-800-457-3801

SCBT Portrait Logo
Seach Input

TRIM64 Inhibitors

Chemical inhibitors of TRIM64 can interfere with its function in various biochemical pathways by inhibiting the degradation processes it may regulate. MG132, Lactacystin, Bortezomib, and Epoxomicin are compounds that directly inhibit the proteasome, a complex responsible for degrading ubiquitinated proteins. TRIM64, which tags proteins for degradation, relies on the proteasome to execute the turnover of these proteins. MG132 operates by inhibiting proteasomal degradation activities, leading to the accumulation of ubiquitinated substrate proteins, which results in the inhibition of TRIM64. Lactacystin irreversibly binds to the proteasomal subunits, thereby directly inhibiting the proteasome's activity and, by extension, TRIM64's function in protein degradation. Bortezomib selectively targets the 26S proteasome, impeding the breakdown of ubiquitinated proteins and consequently inhibiting TRIM64's role in this process. Similarly, Epoxomicin selectively inhibits the chymotrypsin-like activity of the proteasome, which would prevent the degradation of proteins tagged by TRIM64, thus inhibiting its function. Other inhibitors like Chloroquine and Bafilomycin A1 disrupt lysosomal function, which is another pathway for protein degradation that TRIM64 may utilize. Chloroquine raises the lysosomal pH, disrupting lysosome-dependent degradation pathways, while Bafilomycin A1 and Concanamycin A inhibit the vacuolar-type H+-ATPase, leading to dysfunction in lysosomal acidification. Both mechanisms can lead to the inhibition of TRIM64's role in lysosomal degradation. Protease inhibitors such as E64 and Leupeptin also play a role in inhibiting TRIM64 by targeting cysteine and serine proteases, possibly required for TRIM64's function or the processing of its substrates. 3-Methyladenine inhibits autophagy by blocking autophagosome formation, which could also inhibit the autophagic pathways involving TRIM64. Lastly, ALLN and Z-VAD-FMK inhibit calpains and caspases, respectively. ALLN inhibits calpain, which could prevent the proteolytic processing necessary for TRIM64's activity, while Z-VAD-FMK inhibits caspases, potentially disrupting apoptosis-related pathways where TRIM64 may play a role.

Items 1 to 10 of 11 total

Display:

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

MG-132 [Z-Leu- Leu-Leu-CHO]

133407-82-6sc-201270
sc-201270A
sc-201270B
5 mg
25 mg
100 mg
$60.00
$265.00
$1000.00
163
(3)

MG132 can inhibit the proteasomal degradation activities that TRIM64 may rely on for the regulation of protein turnover, leading to an accumulation of TRIM64's ubiquitinated substrate proteins and thus inhibiting TRIM64's function.

Lactacystin

133343-34-7sc-3575
sc-3575A
200 µg
1 mg
$188.00
$575.00
60
(2)

Lactacystin irreversibly binds to the proteasomal subunits, inhibiting the proteasome's activity. Since TRIM64 is thought to be involved in tagging proteins for proteasomal degradation, inhibition of the proteasome would result in functional inhibition of TRIM64's role in this pathway.

Bortezomib

179324-69-7sc-217785
sc-217785A
2.5 mg
25 mg
$135.00
$1085.00
115
(2)

Bortezomib inhibits the 26S proteasome, which is responsible for degrading ubiquitinated proteins. As TRIM64 is implicated in protein ubiquitination, its function is inhibited when proteasomal activity is blocked, preventing the degradation of its substrates.

Epoxomicin

134381-21-8sc-201298C
sc-201298
sc-201298A
sc-201298B
50 µg
100 µg
250 µg
500 µg
$137.00
$219.00
$449.00
$506.00
19
(2)

Epoxomicin selectively inhibits the chymotrypsin-like activity of the proteasome. Inhibition of this activity can prevent the degradation of TRIM64's ubiquitinated targets, thereby inhibiting TRIM64's function in proteostasis.

Chloroquine

54-05-7sc-507304
250 mg
$69.00
2
(0)

Chloroquine disrupts lysosomal function by raising the lysosomal pH, which could inhibit the lysosome-dependent degradation pathways that TRIM64 may utilize, leading to a functional inhibition of TRIM64's role in this pathway.

Bafilomycin A1

88899-55-2sc-201550
sc-201550A
sc-201550B
sc-201550C
100 µg
1 mg
5 mg
10 mg
$98.00
$255.00
$765.00
$1457.00
280
(6)

Bafilomycin A1 is a specific inhibitor of the vacuolar-type H+-ATPase (V-ATPase). If TRIM64 directs proteins to lysosomes for degradation, this inhibition would lead to functional inhibition of TRIM64's role in lysosomal degradation.

Concanamycin A

80890-47-7sc-202111
sc-202111A
sc-202111B
sc-202111C
50 µg
200 µg
1 mg
5 mg
$66.00
$167.00
$673.00
$2601.00
109
(2)

Concanamycin A inhibits the V-ATPase similar to Bafilomycin A1. Inhibition of V-ATPase can lead to dysfunction of lysosomal acidification, potentially inhibiting any lysosome-dependent pathways involving TRIM64.

E-64

66701-25-5sc-201276
sc-201276A
sc-201276B
5 mg
25 mg
250 mg
$281.00
$947.00
$1574.00
14
(0)

E64 is an inhibitor of cysteine proteases. If TRIM64 requires the activation of cysteine proteases for its function or the function of its substrates, E64's inhibition of these enzymes would inhibit TRIM64's activity.

Leupeptin hemisulfate

103476-89-7sc-295358
sc-295358A
sc-295358D
sc-295358E
sc-295358B
sc-295358C
5 mg
25 mg
50 mg
100 mg
500 mg
10 mg
$73.00
$148.00
$316.00
$499.00
$1427.00
$101.00
19
(3)

Leupeptin inhibits serine and cysteine proteases, and its activity could hinder the proteolytic processing necessary for TRIM64's functional activity or the activity of its substrate proteins.

Autophagy Inhibitor, 3-MA

5142-23-4sc-205596
sc-205596A
50 mg
500 mg
$65.00
$261.00
113
(3)

3-Methyladenine inhibits autophagy by blocking autophagosome formation. If TRIM64 is involved in autophagic degradation, this would inhibit TRIM64's role in mediating this pathway.