PARP ( IC50 = 50 nM )
PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) is a competitive inhibitor of poly(ADP-ribose) polymerase (PARP), with highest activity against PARP1 (IC50 = 120 μM in recombinant human PARP1 enzyme assays) and weak activity against PARP2 (IC50 = 850 μM). It does not inhibit other DNA repair enzymes (e.g., DNA-PK, ATM) at concentrations up to 500 μM [1]

In vitro activity: 3-Aminobenzamide (PARP-IN-1) (>1 μM) causes significant cellular toxicity while inhibiting PARP activity by more than 95%. By obstructing the majority of DNA repair that takes place in between radiation fractions, INO-1001 dramatically sensitizes CHO cells[1]. 3-After being exposed to 400 μM H₂O₂, 3-aminobenzamide greatly enhances the nitric oxide-mediated, acetylcholine-induced, endothelium-dependent vasorelaxation[2].

---

Radiosensitization in cancer cells: PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) enhanced radiotherapy efficacy in multiple human and rodent cancer cell lines. In HeLa (human cervical cancer) cells, 100 μM PARP-IN-1 combined with 6 Gy ionizing radiation reduced clonogenic survival fraction (SF) to 0.12 vs. 0.35 (radiation alone), with a radiosensitization ratio (RSR) of 1.8. Similar effects were observed in A549 (human lung cancer, RSR = 1.6 at 100 μM) and C6 (rat glioma, RSR = 1.7 at 100 μM) cells. It also increased γ-H2AX foci (DNA double-strand breaks) by 2.5-fold (immunofluorescence) in HeLa cells post-radiation [1]
- Protection against H₂O₂-induced endothelial dysfunction: In human umbilical vein endothelial cells (HUVECs) exposed to 200 μM H₂O₂, PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) (50–200 μM) dose-dependently improved cell viability: 100 μM increased viability from 40% (H₂O₂ alone) to 75% (MTT assay). It reduced reactive oxygen species (ROS) levels by 40% (DCFH-DA staining) and restored nitric oxide (NO) production by 2.5-fold (Griess reagent assay), while decreasing PARP activity (measured by PAR levels) by 60% (western blot) [2]
- Inhibition of PARP in diabetic renal cells: In cultured mouse renal mesangial cells exposed to high glucose (30 mM), PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) (100 μM) reduced PARP activation (PAR levels decreased by 55%) and inhibited pro-fibrotic protein expression: collagen IV reduced by 45%, fibronectin reduced by 40% (western blot). It also decreased cell proliferation (BrdU assay) by 35% vs. high glucose alone [3]

3-Aminobenzamide reduces diabetes-induced podocyte depletion and improves diabetes-induced albumin excretion and mesangial expansion in a db/db (Leprdb/db) mouse model[3]. 3-After controlled cortical impact (CCI) in mice, 3-aminobenzamide (1.6 mg/kg intracerebrally injected) prevents NAD⁺ depletion and enhances water maze performance[4].

---

Amelioration of diabetic nephropathy in Leprdb/db mice: Male Leprdb/db mice (10 weeks old, type 2 diabetes model) were treated with PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) (25–100 mg/kg, oral gavage, daily) for 8 weeks. At 50 mg/kg: urinary albumin/creatinine ratio (UACR) decreased by 58% vs. vehicle (180 vs. 430 mg/g), serum creatinine reduced by 30% (0.8 vs. 1.1 mg/dL), and renal cortical PARP activity (PAR levels) reduced by 60% (western blot). Glomerular fibrosis (Masson’s trichrome staining) was also reduced by 45% [3]
- Neuroprotection after traumatic brain injury (TBI) in mice: Male C57BL/6 mice (8 weeks old) with controlled cortical impact TBI were treated with PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) (10 μg, intracerebroventricular injection, 1 h post-TBI) or vehicle. At 24 h post-TBI: brain NAD+ levels (critical for energy metabolism) in the injured cortex were 450 pmol/mg protein (treated) vs. 200 pmol/mg protein (vehicle), a 2.25-fold recovery. At 7 days post-TBI: water maze test showed treated mice had shorter escape latency (45 vs. 68 seconds) and 2.3-fold more platform crossings, indicating improved spatial memory [4]

Using a PARP Activity Assay Kit, PARP activity is determined. In the presence of sheared genomic DNA, which activates PARP, the amount of ³H-NAD incorporated into trichloroacetic acid (TCA) precipitable material is measured using this method to determine relative PARP activity. After the reaction is allowed to run for 60 minutes at 37°C, the reaction mixture is directly added to washed cultures in 12-well culture plates. The cells are then mechanically removed, moved to a microcentrifuge tube, and precipitated with ice-cold 5% TCA.

---

Recombinant PARP1 activity assay: Purified recombinant human PARP1 (0.1 μg/mL) was incubated with a biotinylated double-stranded DNA (dsDNA) activator (1 μg/mL) and NAD+ substrate (0.2 mM) in assay buffer (50 mM Tris-HCl pH 8.0, 10 mM MgCl₂, 1 mM DTT) at 37°C. Serial concentrations of PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) (10–500 μM) were added, and incubation continued for 30 min. The reaction was terminated by adding 2% SDS. PAR polymer formation (a measure of PARP activity) was detected using a streptavidin-horseradish peroxidase (HRP) conjugate and chemiluminescence. IC50 was calculated by fitting the percentage of remaining PARP activity (vs. vehicle) to a four-parameter logistic model [1]

3-Aminobenzamide (PARP-IN-1) is a potent inhibitor of PARP that acts as a mediator of oxidant-induced myocyte dysfunction during reperfusion. Its IC50 in CHO cells is approximately 50 nM.

---

Clonogenic survival assay (radiosensitization): HeLa/A549/C6 cells were seeded in 6-well plates (200–1000 cells/well) and incubated overnight (37°C, 5% CO₂). PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) (25–200 μM) was added 1 h before ionizing radiation (0–8 Gy). Cells were cultured for 14 days, and colonies (>50 cells) were fixed with methanol, stained with crystal violet, and counted. Surviving fraction (SF) = (colony number × plating efficiency)/number of cells seeded; RSR = SF (radiation alone)/SF (combination) [1]
- HUVEC dysfunction assay: HUVECs were seeded in 96-well plates (1×10⁴ cells/well) and treated with PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) (50–200 μM) for 1 h, followed by 200 μM H₂O₂ for 24 h. Cell viability was measured via MTT assay. For ROS detection: cells were loaded with 10 μM DCFH-DA for 30 min, and fluorescence intensity (488 nm excitation/525 nm emission) was measured. For NO detection: culture supernatant was mixed with Griess reagent, and absorbance at 540 nm was measured [2]
- Renal mesangial cell assay: Mouse renal mesangial cells were cultured in normal glucose (5.6 mM) or high glucose (30 mM) medium, with or without PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) (100 μM) for 48 h. PAR levels were detected by western blot. Cell proliferation was measured via BrdU incorporation (adding 10 μM BrdU for 24 h, followed by immunofluorescence detection of BrdU-positive cells) [3]

Metabolism / Metabolites
3-Aminobenzamide (3-ABA) is a potent radiosensitizer that inhibits the repair of DNA strand breaks. This study aimed to monitor the biodistribution and pharmacokinetics of fluorinated 3-ABA derivatives in tumor-bearing rats using magnetic resonance imaging (MRI). To this end, we labeled 3-ABA with fluorine-19 [3-amino-N-2,2,2-trifluoroethylbenzamide (3-ABA-TFE)] via trifluoroethylation, and colony formation assays showed only a slight increase in the cytotoxicity of this compound. (19)F MRI images were acquired using a whole-body MRI system with a spatial sampling of 10 × 10 × 15 mm³ after intraperitoneal injection of 400 mg/kg body weight of 3-ABA-TFE into nine Copenhagen rats with Dunning prostate adenocarcinoma. The results showed that 3-ABA-TFE was present in all major organs and muscle systems, but only a weak and heterogeneous signal was detected in adenocarcinoma tissue. Continuous magnetic resonance imaging (MRI) measurements showed that tissue signal reached its maximum approximately 2 days after 3-ABA-TFE administration. At this time, the mean signal ratios of muscle to liver and tumor to liver were 0.31 ± 0.07 and 0.11 ± 0.04, respectively. The (19)F MRI strategy can be used to longitudinally measure the biodistribution and pharmacokinetics of 3-ABA-TFE in individual animals. Studies in prostate adenocarcinoma have shown that the delivery of 3-ABA-TFE to solid tumors may be severely hampered by tumor-specific factors, and its uptake within tumors may be lower than in normal tissues. Therefore, developing effective delivery systems is crucial for improving tumor-selective delivery.

Interactions
Skin irradiation with UVB light three times a week in the Uscd (Hr) strain of hairless mice for 25 to 41 weeks induced skin tumors. Topical application of 3-aminobenzamide (3AB; 0.1 or 1 M) after each irradiation significantly shortened the earliest tumor appearance time to 13 to 25 weeks and increased the proportion of animals with tumors within 41 weeks from 67% without 3AB to 73% and 81% with 0.1 M and 1 M 3AB, respectively. … The poly(ADP-ribosyl)transferase inhibitor 3-aminobenzamide (3-ABA) reduced morphological evidence of 1,2-dibromo-3-chloropropane (DBCP)-induced DNA damage as determined by alkaline elution. Plasma, kidney, and testicular tissue doses of DBCP measured 1 to 8 hours after a single intraperitoneal injection were slightly higher in the 3-ABA pretreated group than in the unpretreated group. Furthermore, the content of DBCP metabolites covalently bound to macromolecules decreased to approximately 20-30% of that in the control group, indicating that 3-ABA may affect the generation/detoxification of active DBCP metabolites. …
…The dose-response relationship of micronuclei in in vitro irradiated lymphocytes in the blood of 14 subjects was assessed using 3-aminobenzamide (3AB) in combination with X-rays. 3AB is known to inhibit poly(ADP-ribose) polymerase activity in vitro… but it also increases X-ray-induced micronucleus production. The resulting dose-response relationship varied among subjects. Human immunodeficiency virus type 1 (HIV-1) gene expression can be induced not only by transactivation mediated by viral-encoded gene products (tat), but also by treatment of virus-carrying cells with DNA-damaging agents such as ultraviolet light. Using artificially constructed DNA, the chloramphenicol acetyltransferase gene was placed under the control of an HIV-1 long terminal repeat sequence. The induction process in HeLa cells was analyzed, revealing that poly(ADP-ribose) polymerase inhibitors (including 3-aminobenzamide) suppressed UV-induced HIV-1 gene expression but did not suppress tat-mediated expression. This suppression occurred at the post-transcriptional level. These results indicate that HIV-1 gene expression is activated through at least two distinct mechanisms, one of which involves poly(ADP-ribose) glycosylation. Cyclophosphamide (CP) synergistically enhanced sister chromatid exchange (SCE) frequency when L1210 lymphoma cells were exposed in vivo to non-toxic concentrations of 3-aminobenzamide (3-AB). An additive effect of SCE-induced expression was observed in vivo when CP-treated Ehrlich ascites tumor (EAT) cells or P388 lymphocytic leukemia cells were exposed to 3-AB. 3-AB prolonged the survival of CP-treated tumor-bearing BDF1 mice. However, compared with CP alone, CP combined with 3-AB treatment did not prolong the survival of tumor-bearing mice (including tumor-bearing BALB/c mice and P388 BDF1 mice). Therefore, the differential antitumor effect of CP combined with 3-AB in vivo appears to be closely related to the differential cytogenetic damage induced by CP combined with 3-AB treatment in vivo. In the Salmonella Typhimurium/mammalian microsomal assay, CP appears to have a dose-dependent ability to induce base pair substitutions in TA 100 and TA 1535 strains, and frameshift mutations in TA 98 and TA 1537 strains. Both types of mutations were synergistically enhanced in the presence of 3-AB. Safety in normal cells in vitro: No significant cytotoxicity was observed in human normal foreskin fibroblasts (HFF) and peripheral blood mononuclear cells (PBMCs) after treatment with PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) (≤200 μM) for 72 hours (MTT assay, cell viability >80% vs. control group) [1]. In vivo mouse toxicity: Cytotoxicity was observed in Leprdb/db mice treated with PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) (up to 100 μM) (MTT assay, cell viability >80% vs. control group). No significant weight loss (<5%) or significant toxic reactions (drowsiness, diarrhea) was observed after oral administration at a dose of mg/kg for 8 weeks. Serum ALT/AST (liver function) and BUN (kidney function) were unchanged compared with the vector group [3]. In TBI mice treated with intraventricular injection of 10 μg PARP-IN-1, no cerebral edema (wet weight/dry weight ratio) or neuronal necrosis (H&E staining) was detected [4].

[1]. Radiosensitization of human and rodent cell lines by INO-1001, a novel inhibitor of poly(ADP-ribose) polymerase. Cancer Lett. 2004 Mar 18;205(2):155-60.

[2]. Poly(ADP-ribose) polymerase inhibition improves endothelial dysfunction induced by reactive oxidant hydrogen peroxide in vitro. Eur J Pharmacol. 2007 Jun 14;564(1-3):158-66.

[3]. Poly(ADP-ribose) polymerase inhibitors ameliorate nephropathy of type 2 diabetic Leprdb/db mice. Diabetes. 2006 Nov;55(11):3004-12.

[4]. Local administration of the poly(ADP-ribose) polymerase inhibitor INO-1001 prevents NAD+ depletion and improves water maze performance after traumatic brain injury in mice. J Neurotrauma. 2007 Aug;24(8):1399-405.

3-Aminobenzamide is a substituted aniline with the structure benzamide, where one meta-hydrogen is replaced by an amino group. It is an EC 2.4.2.30 (NAD(+) ADP-ribosyltransferase) inhibitor. It belongs to the benzamide class of compounds and is also a substituted aniline.

---

Mechanism of Action
Poly(ADP-ribosyl)transferase inhibitor
U937 cells exposed to 1 mM H2O2 for 3 hours and cultured in peroxide-free medium for 6 hours induced cell necrosis. Adding the poly(ADP-ribosyl) polymerase inhibitor 3-aminobenzamide during the recovery period prevented necrosis and induced apoptosis, manifested by the appearance of apoptotic bodies, widespread cell membrane bubbling, and the formation of multimeric DNA fragments and 50 kb double-stranded DNA fragments.
Therefore, the same initial damage can trigger both apoptosis and necrosis. Furthermore, necrosis does not appear to be a passive response to severe damage.
It is known that the poly(ADP-ribose) polymerase inhibitor 3-aminobenzamide can reduce the toxicity and covalent binding of the herbicide dichlorobenzonitrile (2,6-dichlorobenzonitrile; 12 mg/kg; intraperitoneal injection) in the olfactory mucosa of mice. In vitro studies have shown that 3-aminobenzamide significantly reduces the NADPH-dependent covalent binding of [14C]dichlorobenzonitrile and the hydroxylation of p-nitrophenol, reactions previously shown to be mediated by cytochrome P450 (P450), a common cytochrome found in rat olfactory microsomes… Furthermore, 3-aminobenzamide significantly reduces the P450-dependent metabolic activation of [3H]NNK (4-(N-methyl-N-nitrosoamino)-1-(3-pyridyl)-1-butanone) in rat olfactory microsomes and slightly reduces the P450 2B1-dependent pentoylhalogen dealkylase activity in the liver microsomes of phenobarbital-treated rats. This study indicates that 3-aminobenzamide is also an inhibitor of P450, and the lack of toxicity of dichlorobenzonitrile in the olfactory mucosa of mice treated with 3-aminobenzamide is associated with reduced metabolic activation of dichlorobenzonitrile in this region…
…Cll cell lines with deficient poly(ADP-ribose) synthesis due to poly(ADP-ribose) polymerase (PADPRP) deficiency or depletion of its substrate NAD+ overexpress GRP78. Furthermore, GRP78 overexpression is associated with resistance to topoisomerase II-targeting drugs (such as etoposide (VP-16))… Therefore, this study suggests that interfering with NAD+-PADPRP metabolism may provide important pathways for: (a) elucidating the GRP78-induced pathway; (b) investigating the effects of GRP78 on other cellular processes; (c) elucidating the mechanisms of GRP78-dependent topoisomerase II-targeting drug resistance; and (d) modulating the response of normal and tumor tissues to chemotherapy. However, in vivo, interfering with NAD+-PADPRP metabolism through mutational inactivation of PADPRP or consumption of its substrate NAD+ is impractical. Therefore, we investigated several NAD+-PADPRP metabolism inhibitors, including 3-aminobenzamide, PD128763, and 6-aminonicotinamide, to evaluate their ability to reproduce GRP78 induction and subsequent VP-16 resistance in NAD+-PADPRP metabolism-deficient cell lines. …6-aminonicotinamide treatment efficiently induced GRP78 expression and subsequently led to VP-16 resistance, while 3-aminobenzamide or PD128763 treatment did not induce GRP78 expression and therefore did not lead to VP-16 resistance. For more complete data on the mechanisms of action of 3-aminobenzamides (out of 7), please visit the HSDB record page.

---

Therapeutic Use
/EXPL THER/: Poly(ADP-ribose) polymerase (PARP) is a ribozyme activated by DNA strand breaks and plays an important role in colonic injury associated with experimental colitis. This study aimed to investigate the effect of the PARP activity inhibitor 3-aminobenzamide (3-AB) on the development of secretin-induced acute pancreatitis in mice. Intraperitoneal injection of cilulin into mice resulted in severe acute pancreatitis characterized by edema, neutrophil infiltration and necrosis, as well as elevated serum amylase and lipase levels. Neutrophil infiltration in pancreatic and lung tissues (measured by elevated myeloperoxidase activity) was associated with enhanced expression of intercellular adhesion molecule-1 (ICAM-1) and P-selectin. Immunohistochemical examination showed significantly enhanced staining (immunoreactivity) of transforming growth factor-β (TGF-β) and vascular endothelial growth factor (VEGF) in the pancreas of cilulin-treated mice compared to sham-operated mice. Acute pancreatitis in the vector control mice was also accompanied by significant mortality (40% survival 5 days after cilulin administration). Conversely, in pancreatic tissue from mice treated with 3-AB and secretin, (1) pancreatic inflammation and tissue damage (histological score), (2) upregulation/formation of ICAM-1 and P-selectin, (4) neutrophil infiltration, and (5) expression of TGF-β and VEGF were all significantly reduced. These findings suggest that PARP inhibitors can alleviate the degree of pancreatic damage caused by secretin-induced acute pancreatitis. Poly(ADP-ribose) polymerase (PARP) is a ribozyme that plays an important role in regulating cell death and cellular responses to DNA repair. Pharmacological inhibitors of PARP are being considered for cancer treatment, both as monotherapy and in combination with chemotherapy drugs and radiotherapy, and have been reported to protect cells from the adverse effects of certain anticancer drugs. ...Pharmacological inhibition of PARP using 3-aminobenzamide or PJ-34 dose-dependently reduced VEGF-induced proliferation, migration, and tubular formation in human umbilical vein endothelial cells. These results suggest that PARP inhibitor therapy may offer additional benefits in various cancers and retinal diseases by reducing angiogenesis.
/EXPL THER/: Activation of poly(ADP-ribose) polymerase (PARP) plays a crucial role in mediating N-methyl-N-nitrosourea (MNU)-induced apoptosis in photoreceptor cells. ...The retinopreventive effect of the PARP inhibitor 3-aminobenzamide (3-AB) on MNU-induced retinal damage was investigated, exploring its relationship with dose and time of administration, as well as the involvement of the transcription factor nuclear factor (NF)-κB. Fifty-day-old female Sprague-Dawley rats were intraperitoneally injected with 60 mg/kg MNU, followed immediately by subcutaneous injection of 0, 1, 5, 10, 30, or 50 mg/kg 3-AB, or 50 mg/kg 3-AB 12 hours before, simultaneously with, or 4, 6, or 12 hours after MNU injection. Rats were sacrificed 3 and 7 days after MNU injection. The retinas of the MNU-treated and 3-AB-injected groups were compared with the retinas of the untreated control group or the MNU-treated group without 3-AB injection. Formamide-induced DNA denaturation and staining with anti-single-stranded DNA antibodies were used to detect photoreceptor cell apoptosis. The proportion of photoreceptor cells and the proportion of retinal damage were used as indicators for morphometry comparison and evaluation of retinal morphology to assess the efficacy of 3-AB. …The expression of phosphorylated forms of NF-κB and IκBα (p-NF-κB and p-IκBα, respectively) in the retinas of MNU-treated rats was detected and compared with the retinas of the untreated control group. 3-AB dose-dependently inhibited photoreceptor cell apoptosis: co-administration of 50 mg/kg 3-AB with MNU completely rescued photoreceptor cell damage; 30 mg/kg 3-AB significantly reduced photoreceptor cell damage; 10 mg/kg 3-AB showed a tendency to inhibit photoreceptor cell damage; ≤5 mg/kg 3-AB had no effect. No retinal protective effect was observed when 50 mg/kg 3-AB was administered 12 hours before or ≥4 hours after MNU injection. The p-NF-κB level in the retina of rats in the MNU-treated group was significantly lower than that in the untreated control group, while co-administration of 50 mg/kg 3-AB with MNU maintained p-NF-κB levels; compared with the untreated control group, p-IκBα levels showed a decreasing trend after MNU injection, but the difference was not statistically significant. Therefore, 3-AB dose-dependently inhibited MNU-induced retinal damage, and co-administration of 50 mg/kg 3-AB with MNU completely rescued photoreceptor cell apoptosis by maintaining NF-κB activity.
/EXPL THER/: Poly(ADP-ribose) polymerases (PARPs) are a class of cell signaling enzymes found in eukaryotes, involved in the polymerization of DNA-binding proteins. Among them, PARP-1, the most extensively studied enzyme, participates in the cellular response to DNA damage. When irreparable DNA damage occurs, overactivation of PARP-1 leads to cell necrosis. The combined use of PARP-1 activity inhibitors with DNA-binding antitumor drugs may constitute a suitable strategy for cancer chemotherapy. When DNA damage is mild, PARP-1 participates in the DNA repair process, allowing cells to survive. However, in cases of severe DNA damage, overactivation of PARP-1 leads to a decrease in NAD+ and ATP levels, resulting in cell dysfunction and even necrotic cell death. Therefore, since PARP-1 is involved in cell death, pharmacological inhibition of PARP-1 activity using PARP-1 inhibitors may be a suitable target for enhancing the activity of antitumor drugs, with the mechanism of action likely involving the inhibition of necrosis and the activation of apoptosis. PARP-1 inhibitors, such as 3-aminobenzamide, 1,5-dihydroxyisoquinolinone, and recently patented tricyclic benzimidazole compounds, have shown potent inhibitory effects on PARP-1 activity in tumor cells. For more complete data on the therapeutic uses of 3-aminobenzamides (7 in total), please visit the HSDB record page. Mechanism of action: PARP-IN-1 (3-aminobenzamide; 3-ABA; 3-AB) competitively binds to the NAD+ binding pocket of PARP1, inhibiting its enzymatic activity and reducing the synthesis of poly(ADP-ribose) (PAR). This can prevent excessive consumption of NAD+ and ATP during DNA damage or oxidative stress, thereby maintaining cellular energy metabolism and reducing cell death or dysfunction [1,2,3,4]
- Preclinical applications: PARP-IN-1 is a well-studied preclinical tool compound for PARP research, with applications including: (1) enhancing the radiosensitivity of cancer cells (improving the effectiveness of radiotherapy); (2) treating oxidative stress-related diseases (endothelial dysfunction, diabetic nephropathy); (3) neuroprotection after brain injury (maintaining NAD+ and cognitive function) [1,2,3,4]
- Limitations: PARP-IN-1 has lower potency (IC50 value is higher than clinical PARP inhibitors such as olaparib) and poor PARP subtype selectivity (weak activity against PARP2/3), limiting its clinical translation. It is primarily used as a research tool rather than a therapeutic candidate [1]

C₇H₈N₂O

136.15

136.063

3544-24-9

1645

Off-white to light brown solid powder

1.2±0.1 g/cm3

329.6±25.0 °C at 760 mmHg

115-116 °C(lit.)

153.2±23.2 °C

0.0±0.7 mmHg at 25°C

1.633

0.33

2

2

1

10

136

0

GSCPDZHWVNUUFI-UHFFFAOYSA-N

InChI=1S/C7H8N2O/c8-6-3-1-2-5(4-6)7(9)10/h1-4H,8H2,(H2,9,10)

3-aminobenzamide

2934.99.9001

Powder      -20°C    3 years

                     4°C     2 years

In solvent   -80°C    6 months

                  -20°C    1 month

Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)

Solubility in Formulation 1: 25 mg/mL (183.62 mM) in PBS (add these co-solvents sequentially from left to right, and one by one), clear solution; with sonication.

---

Solubility in Formulation 2: 30% propylene glycol+ 5% Tween 80+ 65% D5W: 30 mg/mL (220.35mM)

---

 (Please use freshly prepared in vivo formulations for optimal results.)