35048-47-6

Usage

Uses

Used in Pharmaceutical Industry:
1,3,5[10]-ESTRATRIENE-3,17-DIOL-6-ONE 6-[O-CARBOXYMETHYL]OXIME is used as a regulatory agent for controlling the expression of leptin, a protein hormone that plays a crucial role in appetite/hunger and metabolism. It modulates the secretion of leptin via membrane-associated estrogen receptor alpha in human placental cells, potentially contributing to the development of treatments for conditions related to appetite regulation and metabolism.
Used in Research Applications:
In the field of research, 1,3,5[10]-ESTRATRIENE-3,17-DIOL-6-ONE 6-[O-CARBOXYMETHYL]OXIME serves as a valuable tool for studying the effects of estrogen and its derivatives on various biological processes. Its unique structure allows scientists to investigate the interactions between estrogen receptors and other cellular components, leading to a better understanding of the underlying mechanisms and potential therapeutic applications.

InChI:InChI=1/C20H25NO5/c1-20-7-6-13-12-3-2-11(22)8-15(12)17(21-26-10-19(24)25)9-14(13)16(20)4-5-18(20)23/h2-3,8,13-14,16,18,22-23H,4-7,9-10H2,1H3,(H,24,25)/b21-17+/t13?,14?,16?,18-,20-/m0/s1

Upstream product

• 571-92-6 6-ketoestradiol 
• 20295-82-3 O-carboxymethylhydroxylamine hydrochloride 
• 2921-14-4 (aminooxy)acetic acid hemihydrochloride 
• 3434-45-5 6-oxo-3,17β-estradiol diacetate 
• 1474-52-8 estradiol-3,17-diacetate 
• 645-88-5 aminooxyacetic acid 
• 65132-67-4 Benzoic acid (8R,9S,13S,14S,17S)-6-[(E)-carboxymethoxyimino]-17-hydroxy-13-methyl-7,8,9,11,12,13,14,15,16,17-decahydro-6H-cyclopenta[a]phenanthren-3-yl ester 

Relevant academic research and scientific papers

Facile synthesis of CIDs: Biotinylated estrone oximes efficiently heterodimerize estrogen receptor and streptavidin proteins in yeast three hybrid systems

We synthesized estrone oximes as chemical inducers of protein heterodimerization (CIDs). Estrone-17-(O-carboxymethyl)oxime coupled to biotinamidocaproic acid via N,N′-dimethylhexane-1,6-diamine efficiently heterodimerizes estrogen receptors (ERs) and stre

Specificity of antibodies to ovarian hormones in relation to the site of attachment of the steroid hapten to the peptide carrier

Estradiol-17β, estriol and progesterone were rendered antigenic by covalent attachment to bovine serum albumin through ring B or C of the steroid molecule. Coupling to lysine residues of the protein was effected via the 6-(O-carboxymethyl)-oximes of the estrogens and via the 6-(carboxymethylene) thioether or the 11α-hemisuccinate of progesterone, by use of the carbodiimide reagent. Antisera to the estradiol 6-conjugate raised in rabbits or goats distinguished estradiol-17β more efficiently from estrone, estradiol-17α and estriol than did antisera to estradiol-17β-hemisuccinate-BSA; neither serum reacted with non-phenolic steroids or non-steroidal estrogens. Antisera to estriol 6-conjugates showed minimal cross-reaction with estradiol-17β and estrone. Rabbit antisera against the progesterone 6-conjugate did not react with phenolic or C19-steroids, cr with corticosterone, and only feebly with 11-deoxycorticosterone and 20α-or 20β-dihydroprogesterone; significant crossreaction occurred with 17β-hydroxyprogesterone and 3β,17α-dihydroxypregn-5-en-20-one (3-4%), Δ5-pregnenolone (8-14%) and with 5β- and 5β-dihydro-progesterone (100%). Sera against the 11-conjugate were better able to recognize changes about the A-ring and failed to cross-react with 5α-dihydroprogesterone ( 3%). Both sera showed greater specificity than reported for antibodies to 20-conjugates of progesterone towards the D-ring and 17-sidechain and were similar in this respect to antibodies elicited by 3-conjugates described in the literature. It is concluded that the site of attachment of steroid haptens to the peptide carrier importantly affects the specificity of the antibodies produced.

An efficient synthesis of 6-oxo-17-β-estradiol and its O-carboxymethyl oxime

Estradiol was efficiently oxidized into 6-oxo estradiol using pyridinium chlorochromate. Previously reported yields were considerably increased by the use of oxidizing agent adsorbed onto celite. The oxo compound was then transformed into the corresponding O-carboxymethy] oxime derivative in quantitative yield.