Date published: 2025-12-18

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STI1 Activators

STI1 activators, representing a unique chemical class, have emerged as key players in the modulation of the protein STI1, also known as stress-inducible protein 1. The exploration of these activators involves a meticulous investigation into the methods governing the activation of STI1, focusing on elucidating the intricate signaling pathways and molecular interactions that contribute to the regulation of STI1 expression. Stress-induced-phosphoprotein 1 Activators encompass a variety of chemical compounds that functionally enhance Stress-induced-phosphoprotein 1 by intricately modulating the activity of its associated chaperone, Hsp90. Geldanamycin fortifies the role of Stress-induced-phosphoprotein 1 in the protein folding machinery by binding to Hsp90, thereby stabilizing the protein complex that Stress-induced-phosphoprotein 1 is part of. This stabilization is critical as it directly escalates the co-chaperone activity of Stress-induced-phosphoprotein 1. Similarly, Radicicol, by inhibiting Hsp90, necessitates an increased affinity and interaction of Stress-induced-phosphoprotein 1 with client proteins, which in turn, amplifies its co-chaperone functions.

The Hsp90 inhibitors such as 17-AAG, 17-DMAG, and Novobiocin, by disrupting Hsp90 chaperone cycles, indirectly elevate the demand and utilization of Stress-induced-phosphoprotein 1 in maintaining protein homeostasis. These inhibitors operate on a compensatory principle, where the inhibition of one component of the chaperone machinery escalates the activity of its partners, in this case, Stress-induced-phosphoprotein 1. The functional activity of Stress-induced-phosphoprotein 1 is further influenced by a range of Hsp90 inhibitors including CCT018159, PU-H71, BIIB021, SNX-2112, Luminespib, and Ganetespib. Each of these compounds, by disrupting the normal functions of Hsp90, indirectly potentiates the action of Stress-induced-phosphoprotein 1, which compensates for the loss of Hsp90 activity by enhancing its own chaperoning role.

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Items 1 to 10 of 11 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Geldanamycin

30562-34-6sc-200617B
sc-200617C
sc-200617
sc-200617A
100 µg
500 µg
1 mg
5 mg
$38.00
$58.00
$102.00
$202.00
8
(1)

Geldanamycin binds to Hsp90, a chaperone protein that interacts with Stress-induced-phosphoprotein 1, stabilizing its conformation and enhancing its co-chaperone activity in protein folding and stabilization processes.

Radicicol

12772-57-5sc-200620
sc-200620A
1 mg
5 mg
$90.00
$326.00
13
(1)

Radicicol functions as an Hsp90 inhibitor. Since Stress-induced-phosphoprotein 1 acts as a co-chaperone with Hsp90, the inhibition of Hsp90 can lead to an increased affinity of Stress-induced-phosphoprotein 1 for client proteins, indirectly enhancing its co-chaperoning role.

17-AAG

75747-14-7sc-200641
sc-200641A
1 mg
5 mg
$66.00
$153.00
16
(2)

17-AAG inhibits Hsp90, which in turn can enhance the role of Stress-induced-phosphoprotein 1 in the chaperone complex due to compensatory mechanisms that maintain protein homeostasis.

17-DMAG

467214-20-6sc-202005
1 mg
$201.00
8
(1)

Similar to other Hsp90 inhibitors, 17-DMAG enhances the activity of Stress-induced-phosphoprotein 1 by disrupting the normal Hsp90 functions, thereby potentially increasing the demand for Stress-induced-phosphoprotein 1's co-chaperone activity.

Novobiocin

303-81-1sc-362034
sc-362034A
5 mg
25 mg
$96.00
$355.00
(0)

Novobiocin is a coumarin antibiotic that also acts as an Hsp90 C-terminal inhibitor, which may lead to enhanced interaction between Hsp90 and Stress-induced-phosphoprotein 1, increasing its functional activity.

CCT128930

885499-61-6sc-364459
sc-364459A
5 mg
10 mg
$153.00
$286.00
2
(1)

CCT018159 is a small molecule inhibitor of Hsp90, which can indirectly enhance the functional role of Stress-induced-phosphoprotein 1 by increasing its requirement in the chaperone cycle.

Salinomycin

53003-10-4sc-253530
sc-253530C
sc-253530A
sc-253530B
5 mg
10 mg
25 mg
100 mg
$159.00
$236.00
$398.00
$465.00
1
(1)

PU-H71 is an Hsp90 inhibitor that could indirectly increase the functional activity of Stress-induced-phosphoprotein 1 by disrupting the Hsp90 chaperone cycle, leading to a compensatory increase in Stress-induced-phosphoprotein 1 activity.

BIIB 021

848695-25-0sc-364434
sc-364434A
5 mg
25 mg
$128.00
$650.00
(0)

BIIB021 is an orally bioavailable Hsp90 inhibitor that can indirectly enhance the functional activity of Stress-induced-phosphoprotein 1 by perturbing the Hsp90 chaperone machinery.

NVP-AUY922

747412-49-3sc-364551
sc-364551A
sc-364551B
sc-364551C
sc-364551D
sc-364551E
5 mg
25 mg
100 mg
250 mg
1 g
5 g
$150.00
$263.00
$726.00
$1400.00
$2900.00
$11000.00
3
(1)

Luminespib is an isoxazole-based Hsp90 inhibitor that may enhance the functional activity of Stress-induced-phosphoprotein 1 by causing a compensatory increase in its activity due to Hsp90 inhibition.

Ganetespib

888216-25-9sc-364496
sc-364496A
10 mg
250 mg
$268.00
$1020.00
(0)

Ganetespib is a triazolone-containing Hsp90 inhibitor that, by hindering Hsp90 function, may indirectly increase the requirement for Stress-induced-phosphoprotein 1 co-chaperone activity.