PSA protein

By Targets:	Androgen Receptor (8) Apoptosis (4) Bacterial (1) Bcl-2 Family (1) Biochemical Assay Reagents (1) c-Myc (1) Caspase (2) CDK (3) EGFR (1) Epigenetic Reader Domain (1) HSP (1) Kallikrein (1) Molecular Glues (1) PROTACs (1) PSMA (3) Reactive Oxygen Species (ROS) (1) Reference Standards (1) Ser/Thr Protease (1)
By Research Areas:	Cancer (9) Infection (1) Inflammation/Immunology (1)
Click Chemistry:	PROTAC Synthesis (1)

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-N7045

Isosilybin B 2 Publications Verification	Androgen Receptor Apoptosis CDK Caspase PSMA	Cancer
Isosilybin B is a flavonolignan. Isosilybin B can be isolated from Silybum marianum. Isosilybin B can regulate cell cycle-related proteins (e.g., reduce cyclins (D3, D1, A, E), Cdk4, Cdk2, Cdc25A), and activate Caspases (Caspase-9 and Caspase-3). Isosilybin B can promote Apoptosis, reduce androgen receptor (AR) and *PSA*. Isosilybin B has anticancer activity against prostate cancer .

HY-114402

ARD-69	PROTACs Androgen Receptor	Cancer
ARD-69 is a PROTAC degrader based on the E3 ubiquitin ligase VHL and targeting the androgen receptor, which can induce androgen receptor (AR) protein degradation in AR-positive prostate cancer cells. ARD-69 inhibits AR-regulated gene expression, binds to the AR ligand binding domain at one end and binds to VHL at the other end, prompting AR to be recruited to the E3 ubiquitin ligase complex, triggering proteasome degradation, thereby inhibiting AR signaling pathways and downstream gene expression (such as PSA, TMPRSS2). ARD-69 can be used to study of castration-resistant prostate cancer (mCRPC) . ARD-69 is composed of a target protein ligand (pink part) AR antagonist 14 (HY-172624), a PROTAC linker (black part) tert-Butyl 4-ethynyl-[1,4'-bipiperidine]-1'-carboxylate (HY-W442074), and a VHL-type E3 ubiquitinase ligand (blue part) VH 101, acid (HY-47070); among them, the VHL ligand and the linker can form a conjugate VH 101-amide-piperidine-Pip-alkyne (HY-172625).

HY-143332

TRIM24/BRPF1-IN-2	Epigenetic Reader Domain	Cancer
TRIM24/BRPF1-IN-2 (compound 20l) is a potent TRIM24/BRPF1 dual inhibitor, with IC₅₀ values of 0.98 and 1.16 μM, respectively. TRIM24/BRPF1-IN-2 shows TRIM24/BRPF1 bromodomain binding affinity. TRIM24/BRPF1-IN-2 can be used for prostate cancer research .

HY-P99554

Topsalysin PRX-302	PSMA	Cancer
Topsalysin is a PSA-activated protoxin, a pore-forming protein (synthetic proaerolysin) fusion protein with human prostate-specific antigen. Topsalysin has tumor suppression effect in mice modle .

HY-NP002H

Porcine Serum Albumin (globulin free)	Biochemical Assay Reagents	Others
Porcine Serum Albumin (globulin free) is a serum albumin protein containing a flexible C-terminal region. Porcine Serum Albumin (globulin free) induces the production of anti-PSA IgG antibodies in rats and triggers severe immune responses upon secondary administration .

HY-40156

5-Fluoroindole	Bacterial Reactive Oxygen Species (ROS) Apoptosis	Infection
5-Fluoroindole is an orally active fluorinated indole derivative and antibacterial agent. 5-Fluoroindole induces ROS accumulation and triggers Apoptosis. 5-Fluoroindole inhibits the growth of pan-susceptible Mycobacterium tuberculosis (Mtb) H37Rv strains. 5-Fluoroindole has significant bactericidal activity against Pseudomonas syringae pv. actinidiae (Psa) with an EC₅₀ of 15.34 μg/mL. 5-Fluoroindole introduces fluorine labeling for protein research. 5-Fluoroindole can be used in the study of tuberculosis and kiwifruit bacterial canker .

HY-174391

AR antagonist 15	Androgen Receptor Apoptosis	Cancer
AR antagonist 15 is an orally active androgen receptor (AR) antagonist with the IC₅₀ of 97 nM for AR^T787A. AR antagonist 15 disrupts AR nuclear translocation, hinders AR homodimerization, and suppresses transcription of AR-regulated genes by competitive binding to the ligand binding pocket. AR antagonist 15 can significantly lower the prostate-specific antigen (PSA) level. AR antagonist 15 induces apoptosis by reducing the expression of apoptosis pathway related proteins. AR antagonist 15 can be used for the research of prostate cancer.

HY-170820

XYD049	Molecular Glues Bcl-2 Family CDK EGFR HSP Androgen Receptor c-Myc	Cancer
XYD049 is a CRBN-based molecular glue degrader targeting GSPT1, with a DC₅₀ of 19 nM. XYD049 mediates the formation of a ternary complex between CRBN and GSPT1, thereby triggering CRBN- and proteasome-dependent degradation of GSPT1. By degrading GSPT1, XYD049 downregulates castration-resistant prostate cancer (CRPC)-related oncogenes, including BCL2, CDK2, E2F3, EGFR, HSP90B1, TMPRSS2, AR, AR-V7, *PSA* and c-Myc. XYD049 inhibits cancer cell growth and suppresses tumor growth in mice. XYD049 can be used for research on castration-resistant prostate cancer. XYD049 consists of a linker (black part) NH2-C5-NH-Boc (HY-W004710), a CRBN-based E3 ligase ligand (blue part) Thalidomide 4-fluoride (HY-41547), and a target protein ligand (red part) GSPT1 ligand-1 (HY-170821), among which the E3 ligase ligand plus linker forms the conjugate E3 Ligase Ligand-linker Conjugate 158 (HY-170822) .

HY-173409

AR antagonist 11	Androgen Receptor Ser/Thr Protease	Inflammation/Immunology
AR antagonist 11 (Compound c2) is a selective AR antagonist with an IC₅₀ of 0.019 μM. AR antagonist 11 is also effective against AR ^F877L/T878A mutant (IC₅₀: 1.03 μM). AR antagonist 11 inhibits LNCaP cell proliferation and reduces PSA protein expression (IC₅₀: 0.54 μM). AR antagonist 11 can be used for research of prostate cancer (PCa) .

HY-173559

AR antagonist 12	Androgen Receptor	Cancer
AR antagonist 12 (compound 20i) is an orally active androgen receptor antagonist wiith IC₅₀ values of 119.3 μM and 98.2 μM for wt-AR and AR-F877L,respectively. AR antagonist 12 induces a dose-dependent and time-dependent reduction in AR, AR-V7, and PSA protein levels. AR antagonist 1 shows anticancer activuty and can be used for the study of Enzalutamide (HY-70002)-resistant Prostate cancer .

HY-N7045R

Isosilybin B (Standard)	Reference Standards Androgen Receptor Apoptosis CDK Caspase PSMA	Cancer
Isosilybin B (Standard) is the analytical standard of Isosilybin B (HY-N7045). This product is intended for research and analytical applications. Isosilybin B is a flavonolignan. Isosilybin B can be isolated from Silybum marianum. Isosilybin B can regulate cell cycle-related proteins (e.g., reduce cyclins (D3, D1, A, E), Cdk4, Cdk2, Cdc25A), and activate Caspases (Caspase-9 and Caspase-3). Isosilybin B can promote Apoptosis, reduce androgen receptor (AR) and *PSA*. Isosilybin B has anticancer activity against prostate cancer .

HY-183667

JNJ-pan-AR	Androgen Receptor Kallikrein	Cancer
JNJ-pan-AR is an orally active androgen receptor (AR) inhibitor with an IC₅₀ of 19 nM and a K_i of 8.4 nM against human wild-type AR. JNJ-pan-AR abolishes androgen-induced KLK2 and KLK3 mRNA expression and reduces androgen-dependent colony formation in prostate cancer cells. JNJ-pan-AR blocks AR nuclear translocation, inhibits *PSA* protein expression, and represses the growth of AR-dependent tumor cells and ARF877L-driven tumor xenografts. JNJ-pan-AR blocks transactivation and signaling of wild-type AR and various mutant AR variants. JNJ-pan-AR is applicable for research on castration-resistant prostate cancer .

Cat. No.	Product Name

HY-L908

Lead-like Covalent Screening Library	1,248 compounds
Small molecule covalent inhibitors, or irreversible inhibitors, are a type of inhibitors that exert their biological functions by irreversibly binding to target through covalent bonds. Compared with non-covalent inhibitors, covalent inhibitors have obvious advantages in bioactivity, such that covalent warheads can target rare residues of a particular target protein, thus leading to the development of highly selective inhibitors and achieving a more complete and continued target occupancy in living systems. In recent years, the distinct strengths of covalent inhibitors in overcoming drug resistance had been recognized. However, toxicity can be a real challenge related to this class of therapeutics due to their potential for off-target reactivity and has led to these drugs being disfavored as a drug class. The drug design and optimization of covalent inhibitors has become a hot spot in drug discovery. MCE Lead-like Covalent Screening Library offers a valuable resource of 1,049 lead-like compounds with commonly used covalent warheads. These warheads, such as acrylamide, activated terminal alkyne, acyloxymethyl ketone, and boronic acid, are capable of reacting with specific amino acid residues, including cysteine, lysine, serine, and histidine. The inclusion of these reactive warheads in the library allows researchers to explore the potential of covalent inhibition, a powerful approach in drug discovery.

Lead-like Covalent Screening Library

1,248 compounds

Small molecule covalent inhibitors, or irreversible inhibitors, are a type of inhibitors that exert their biological functions by irreversibly binding to target through covalent bonds. Compared with non-covalent inhibitors, covalent inhibitors have obvious advantages in bioactivity, such that covalent warheads can target rare residues of a particular target protein, thus leading to the development of highly selective inhibitors and achieving a more complete and continued target occupancy in living systems. In recent years, the distinct strengths of covalent inhibitors in overcoming drug resistance had been recognized. However, toxicity can be a real challenge related to this class of therapeutics due to their potential for off-target reactivity and has led to these drugs being disfavored as a drug class. The drug design and optimization of covalent inhibitors has become a hot spot in drug discovery.

MCE Lead-like Covalent Screening Library offers a valuable resource of 1,049 lead-like compounds with commonly used covalent warheads. These warheads, such as acrylamide, activated terminal alkyne, acyloxymethyl ketone, and boronic acid, are capable of reacting with specific amino acid residues, including cysteine, lysine, serine, and histidine. The inclusion of these reactive warheads in the library allows researchers to explore the potential of covalent inhibition, a powerful approach in drug discovery.

HY-L942

Allosteric Modulator Fragment Library	1802 compounds
In contrast to the high conservation of conventional orthosteric sites, allosteric sites possess structural characteristics of low conservation, high hydrophobicity, weak polarity, confined spatial geometry, and dynamic cryptic properties. There is a significant difference between their core structures and orthosteric pockets — allosteric pockets are mostly dynamic grooves formed by protein conformational changes, subunit interface clefts, or shallow depressions, rather than the rigid "keyhole" structure of orthosteric sites. With looser spatial constraints, allosteric sites have the advantages of high selectivity and low off-target risk, and have become an important direction in new drug discovery. Based on the dynamic, hydrophobic, and narrow-long spatial characteristics of allosteric pockets, MCE has performed targeted modification and screening of fragments. The screening criteria strictly conform to the requirements of allosteric binding: molecular weight is controlled at 120–280 Da (to meet the core needs of small molecules in fragment libraries and high derivatization), hydrogen bond donors (HBD ≤ 2), hydrogen bond acceptors (HBA ≤ 3), polar surface area (PSA = 30–80 Å²), rotatable bonds (≤ 2), moderate hydrophobicity (cLogP = 1–3.5), no strongly ionizable groups, and both appropriate rigidity and conformational flexibility to adapt to the dynamic changes of the pocket. Meanwhile, combined with the results of principal moment of inertia (PMI) analysis, fragments with high 3D diversity were obtained. Such fragments have good shape complementarity with allosteric pockets, ensuring that the fragments can smoothly enter the allosteric pockets and form stable binding, while providing room for subsequent optimization and derivation. This library contains 1,800 structurally diverse fragment molecules with excellent drug-like properties, suitable for allosteric drug development and the design and optimization of allosteric sites. It combines the

Allosteric Modulator Fragment Library

1802 compounds

In contrast to the high conservation of conventional orthosteric sites, allosteric sites possess structural characteristics of low conservation, high hydrophobicity, weak polarity, confined spatial geometry, and dynamic cryptic properties. There is a significant difference between their core structures and orthosteric pockets — allosteric pockets are mostly dynamic grooves formed by protein conformational changes, subunit interface clefts, or shallow depressions, rather than the rigid "keyhole" structure of orthosteric sites. With looser spatial constraints, allosteric sites have the advantages of high selectivity and low off-target risk, and have become an important direction in new drug discovery.

Based on the dynamic, hydrophobic, and narrow-long spatial characteristics of allosteric pockets, MCE has performed targeted modification and screening of fragments. The screening criteria strictly conform to the requirements of allosteric binding: molecular weight is controlled at 120–280 Da (to meet the core needs of small molecules in fragment libraries and high derivatization), hydrogen bond donors (HBD ≤ 2), hydrogen bond acceptors (HBA ≤ 3), polar surface area (PSA = 30–80 Å²), rotatable bonds (≤ 2), moderate hydrophobicity (cLogP = 1–3.5), no strongly ionizable groups, and both appropriate rigidity and conformational flexibility to adapt to the dynamic changes of the pocket. Meanwhile, combined with the results of principal moment of inertia (PMI) analysis, fragments with high 3D diversity were obtained. Such fragments have good shape complementarity with allosteric pockets, ensuring that the fragments can smoothly enter the allosteric pockets and form stable binding, while providing room for subsequent optimization and derivation.

This library contains 1,800 structurally diverse fragment molecules with excellent drug-like properties, suitable for allosteric drug development and the design and optimization of allosteric sites. It combines the

HY-L941

Allosteric Modulator Lead‑like Compound Library	4315 compounds
Owing to the high conservation of orthosteric sites, conventional orthosteric drugs frequently suffer from poor subtype selectivity, off-target toxicity, and drug resistance, severely restricting their clinical application. In contrast, allosteric sites feature low conservation, high hydrophobicity, weak polarity, confined spatial geometry, and dynamic cryptic properties. These characteristics endow allosteric modulators with distinct advantages including high selectivity, functional tunability, and improved safety, making allosteric therapy a key direction in modern drug discovery. MCE has curated nearly 1,000 structurally disclosed clinical-stage allosteric modulators. By analyzing allosteric protein–ligand complex structures from the PDB database, we extracted core pharmacophores and privileged scaffolds. Adopting a rational design strategy of “scaffold derivation + allosteric physicochemical filtering”, we performed secondary screening on the derived compounds strictly following the optimal physicochemical principles for allosteric binding based on universal allosteric pocket properties: molecular weight 300–500 Da, HBD ≤ 3, HBA = 3–8, PSA = 70–120 Å², rotatable bonds ≤ 6, highly rigid scaffolds, cLogP = 1.0–3.8, and no strongly ionizable groups. The selected compounds exhibit high rigidity and shape complementarity, making them well-suited for targeting shallow, dynamic, and hydrophobic-dominated allosteric pockets. This allosteric modulator library contains 4,315 structurally diverse, lead-like compounds dedicated to allosteric drug development, allosteric site targeting, and allosteric modulator screening. It is suitable for kinases, GPCRs, and other important drug targets. All compounds are analogs of clinical-stage allosteric modulators with a similarity score > 0.6, combining excellent druggability and allosteric binding potential. It provides a highly efficient tool for early-stage allosteric drug discovery.

Allosteric Modulator Lead‑like Compound Library

4315 compounds

Owing to the high conservation of orthosteric sites, conventional orthosteric drugs frequently suffer from poor subtype selectivity, off-target toxicity, and drug resistance, severely restricting their clinical application. In contrast, allosteric sites feature low conservation, high hydrophobicity, weak polarity, confined spatial geometry, and dynamic cryptic properties. These characteristics endow allosteric modulators with distinct advantages including high selectivity, functional tunability, and improved safety, making allosteric therapy a key direction in modern drug discovery.

MCE has curated nearly 1,000 structurally disclosed clinical-stage allosteric modulators. By analyzing allosteric protein–ligand complex structures from the PDB database, we extracted core pharmacophores and privileged scaffolds. Adopting a rational design strategy of “scaffold derivation + allosteric physicochemical filtering”, we performed secondary screening on the derived compounds strictly following the optimal physicochemical principles for allosteric binding based on universal allosteric pocket properties: molecular weight 300–500 Da, HBD ≤ 3, HBA = 3–8, PSA = 70–120 Å², rotatable bonds ≤ 6, highly rigid scaffolds, cLogP = 1.0–3.8, and no strongly ionizable groups. The selected compounds exhibit high rigidity and shape complementarity, making them well-suited for targeting shallow, dynamic, and hydrophobic-dominated allosteric pockets.

This allosteric modulator library contains 4,315 structurally diverse, lead-like compounds dedicated to allosteric drug development, allosteric site targeting, and allosteric modulator screening. It is suitable for kinases, GPCRs, and other important drug targets. All compounds are analogs of clinical-stage allosteric modulators with a similarity score > 0.6, combining excellent druggability and allosteric binding potential. It provides a highly efficient tool for early-stage allosteric drug discovery.

Cat. No.	Product Name	Type

HY-NP002H

Porcine Serum Albumin (globulin free)	Biochemical Assay Reagents
Porcine Serum Albumin (globulin free) is a serum albumin protein containing a flexible C-terminal region. Porcine Serum Albumin (globulin free) induces the production of anti-PSA IgG antibodies in rats and triggers severe immune responses upon secondary administration .

HY-40156

5-Fluoroindole	Biochemical Assay Reagents
5-Fluoroindole is an orally active fluorinated indole derivative and antibacterial agent. 5-Fluoroindole induces ROS accumulation and triggers Apoptosis. 5-Fluoroindole inhibits the growth of pan-susceptible Mycobacterium tuberculosis (Mtb) H37Rv strains. 5-Fluoroindole has significant bactericidal activity against Pseudomonas syringae pv. actinidiae (Psa) with an EC₅₀ of 15.34 μg/mL. 5-Fluoroindole introduces fluorine labeling for protein research. 5-Fluoroindole can be used in the study of tuberculosis and kiwifruit bacterial canker .

5-Fluoroindole

Biochemical Assay Reagents

5-Fluoroindole is an orally active fluorinated indole derivative and antibacterial agent. 5-Fluoroindole induces ROS accumulation and triggers Apoptosis. 5-Fluoroindole inhibits the growth of pan-susceptible Mycobacterium tuberculosis (Mtb) H37Rv strains. 5-Fluoroindole has significant bactericidal activity against Pseudomonas syringae pv. actinidiae (Psa) with an EC₅₀ of 15.34 μg/mL. 5-Fluoroindole introduces fluorine labeling for protein research. 5-Fluoroindole can be used in the study of tuberculosis and kiwifruit bacterial canker .

Cat. No.	Product Name	Target	Research Area	Image

HY-P99554

Topsalysin PRX-302	PSMA	Cancer
Topsalysin is a PSA-activated protoxin, a pore-forming protein (synthetic proaerolysin) fusion protein with human prostate-specific antigen. Topsalysin has tumor suppression effect in mice modle .

Cat. No.	Product Name	Category	Target	Chemical Structure

HY-N7045

Isosilybin B 2 Publications Verification	Flavanonols Flavonoids Glycine soya Classification of Application Fields Phenols Polyphenols Cyamopsis tetragonoloba (L.) Taub. Plants Compositae Disease Research Fields Source Classification Cancer	Androgen Receptor Apoptosis CDK Caspase PSMA
Isosilybin B is a flavonolignan. Isosilybin B can be isolated from Silybum marianum. Isosilybin B can regulate cell cycle-related proteins (e.g., reduce cyclins (D3, D1, A, E), Cdk4, Cdk2, Cdc25A), and activate Caspases (Caspase-9 and Caspase-3). Isosilybin B can promote Apoptosis, reduce androgen receptor (AR) and *PSA*. Isosilybin B has anticancer activity against prostate cancer .

HY-N7045R

Isosilybin B (Standard)	Flavanonols Structural Classification Flavonoids Glycine soya Phenols Polyphenols Cyamopsis tetragonoloba (L.) Taub. Plants Compositae Source Classification	Reference Standards Androgen Receptor Apoptosis CDK Caspase PSMA
Isosilybin B (Standard) is the analytical standard of Isosilybin B (HY-N7045). This product is intended for research and analytical applications. Isosilybin B is a flavonolignan. Isosilybin B can be isolated from Silybum marianum. Isosilybin B can regulate cell cycle-related proteins (e.g., reduce cyclins (D3, D1, A, E), Cdk4, Cdk2, Cdc25A), and activate Caspases (Caspase-9 and Caspase-3). Isosilybin B can promote Apoptosis, reduce androgen receptor (AR) and *PSA*. Isosilybin B has anticancer activity against prostate cancer .

Species:	Human (3)
Tag:	His (2)
Source:	HEK293 (2) E. coli (1)

Cat. No.	Compare	Product Name	Species	Source	Image

HY-P70606A

	*Kallikrein-3/PSA* Protein, Human (HEK293, His)** Prostate-specific antigen; PSA; Gamma-seminoprotein; Kallikrein-3; P-30 antigen; Semenogelase; KLK3; APS	Human	HEK293
	Kallikrein-3 (PSA) protein, pivotal in the male reproductive system, hydrolyzes semenogelin-1, a seminal vesicle protein. This enzymatic activity initiates seminal coagulum liquefaction, crucial for sperm mobility and fertility. PSA's cleavage of semenogelin-1 highlights its importance in the complex processes of semen physiology and male reproductive function. Kallikrein-3/PSA Protein, Human (HEK293, His) is the recombinant human-derived Kallikrein-3/PSA protein, expressed by HEK293 , with C-6*His labeled tag.

HY-P70266

	*Kallikrein-3/PSA* Protein, Human (244a.a, HEK293, His)** 1 Publications Verification rHuProstate-specific antigen/KLK3, His; Prostate-Specific Antigen; PSA; Gamma-Seminoprotein; Seminin; Kallikrein-3; P-30 Antigen; Semenogelase; KLK3; APS	Human	HEK293
	Kallikrein-3 (PSA) protein, pivotal in the male reproductive system, hydrolyzes semenogelin-1, a seminal vesicle protein. This enzymatic activity initiates seminal coagulum liquefaction, crucial for sperm mobility and fertility. PSA's cleavage of semenogelin-1 highlights its importance in the complex processes of semen physiology and male reproductive function. Kallikrein-3/PSA Protein, Human (244a.a, HEK293, His) is the recombinant human-derived Kallikrein-3/PSA protein, expressed by HEK293 , with C-His labeled tag.

HY-P78999

	*PSAT1 Protein, Human (His)* Phosphoserine aminotransferase; PSAT1; Phosphohydroxythreonine aminotransferase; PSAT; PSA; Phosphoserine Aminotransferase 1	Human	E. coli
	The PSAT1 protein plays a central role in cellular metabolism by catalyzing the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and 3-hydroxy-2-oxo-4-phosphonooxybutyrate to phosphohydroxythreonine. These enzyme activities are key steps in the biosynthetic pathway of the essential amino acids serine and threonine. PSAT1 Protein, Human (His) is the recombinant human-derived PSAT1 protein, expressed by E. coli , with C-6*His labeled tag.

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Host:	Rabbit (2)
Reactivity:	Human (2) Rat (1) Mouse (1)
Application:	IHC-P (1) IP (1) WB (2) FC (1)
Isotype:	IgG (2)
Conjugation:	Non-conjugated (2)
Clonality:	Monoclonal (2) Recombinant (2)
Modification:	Unmodified (2)

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HY-P83174

	Protein S Antibody (YA2919) Preproprotein S; PROS; proS1; PS21; PS22; PS23; PS24; PS25; PS26; PSA; THPH5; THPH6	WB	Human
	Protein S Antibody (YA2919) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Protein S.

HY-P87041

	Phosphoserine aminotransferase Antibody (YA6734) EC 2.6.1.52 antibody; Endometrial progesterone induced protein antibody; EP; IP : antibody; MGC1460 antibody; NLS2 antibody; Phosphohydroxythreonine aminotransferase antibody; phosphoserine aminotransferase 1 antibody; Phosphoserine aminotransferase antibody; PSA antibody; PSAT antibody; EC 2.6.1.52 antibody; Endometrial progesterone induced protein antibody; EP; IP : antibody; MGC1460 antibody; NLS2 antibody; Phosphohydroxythreonine aminotransferase antibody; phosphoserine aminotransferase 1 antibody; Phosphoserine aminotransferase antibody; PSA antibody; PSAT antibody; PSAt1 antibody; PSATD antibody; SERC_HUMAN antibody;	WB, IHC-P, FC, IP	Human, Mouse, Rat
	Phosphoserine aminotransferase Antibody (YA6734) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Phosphoserine aminotransferase.

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Cat. No.	Product Name		Classification

HY-114402

ARD-69		PROTAC Synthesis
ARD-69 is a PROTAC degrader based on the E3 ubiquitin ligase VHL and targeting the androgen receptor, which can induce androgen receptor (AR) protein degradation in AR-positive prostate cancer cells. ARD-69 inhibits AR-regulated gene expression, binds to the AR ligand binding domain at one end and binds to VHL at the other end, prompting AR to be recruited to the E3 ubiquitin ligase complex, triggering proteasome degradation, thereby inhibiting AR signaling pathways and downstream gene expression (such as PSA, TMPRSS2). ARD-69 can be used to study of castration-resistant prostate cancer (mCRPC) . ARD-69 is composed of a target protein ligand (pink part) AR antagonist 14 (HY-172624), a PROTAC linker (black part) tert-Butyl 4-ethynyl-[1,4'-bipiperidine]-1'-carboxylate (HY-W442074), and a VHL-type E3 ubiquitinase ligand (blue part) VH 101, acid (HY-47070); among them, the VHL ligand and the linker can form a conjugate VH 101-amide-piperidine-Pip-alkyne (HY-172625).

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Inhibitors & Agonists

Screening Libraries

Biochemical Assay Reagents

Inhibitory Antibodies

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Recombinant Proteins

Antibodies

Click Chemistry

PSA protein

Inhibitors & Agonists

Screening Libraries

Biochemical Assay Reagents

Inhibitory Antibodies

NaturalProducts

Recombinant Proteins

Antibodies

Click Chemistry

Natural
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