We use analytics and advertising cookies, which you can accept or reject; see our privacy policy.

Current choice:

Fig. 1 · Structure
Cat. No.
A10789
CAS No.
83-88-5
Formula
C17H20N4O6
Mol. Weight
376.36

Documents & Downloads

Riboflavin

Vitamin B2

Riboflavin, also known as Vitamin B2, is a vital micronutrient and a precursor to the coenzymes flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). These coenzymes play essential roles in various enzymatic reactions, facilitating key metabolic functions by mediating electron transfer in biological oxidation-reduction processes. Riboflavin is significant in research involving energy metabolism, antioxidant defense, and cellular respiration, making it crucial for various biochemical studies.

In Stock

Notify me when the price drops

For laboratory research use only. We do not sell to patients.

Free Aliquoting for Your Order

Tell us your preferred amount per vial. We’ll confirm the options.

Biological Activity

Bioactivity / Mechanism

Riboflavin availability supports cellular redox metabolism. In HepG2 cultures, four days at 3.1 nmol/L riboflavin reduced glutathione reductase activity below detection compared with 300 nmol/L supplemented medium. This nutrient-deprivation experiment does not establish a direct inhibitory potency. [1]

Riboflavin also acts as a photosensitizer. In cell-free HBSS under UVA, adding folic acid or selected amino acids to riboflavin increased peroxide production relative to riboflavin alone, while most other tested components did not significantly increase it. The effect depends on light exposure and the chemical environment. [2]

Literature-reported observations and conditions; not Adooq-tested protocols or general treatment recommendations.

In Vitro Studies

Riboflavin-deficient HepG2 cultures showed greater DNA strand-break-associated comet tail moments and a higher G0/G1 fraction than supplemented cultures after four days. These findings concern a transformed cell line under defined nutrient conditions; they do not establish a therapeutic concentration. [1]

Riboflavin deprivation and redox stress in HepG2 cells

Cell-based study · Human HepG2 hepatocarcinoma cells; customized RPMI-1640 with 10% dialyzed, riboflavin-depleted bovine growth serum [1]

Four-day comparison of deficient and supplemented cultures linked riboflavin availability to glutathione reductase activity, DNA integrity and cell-cycle distribution. This is one culture-comparison study with several readouts.

Measured endpoints — not treatment concentrations
EndpointReported resultReference
Glutathione reductase activityAbsorbance-based activity 3.1 nmol/L: not detectable; 300 nmol/L: 0.09 ± 0.02 units of absorbance at 340 nm/(mg protein x 12 min); P < 0.05; n = 3; mean ± SD[1]
DNA strand-break-associated comet tail momentTail moment 3.1 nmol/L: 5.2 ± 1.5 arbitrary units; 300 nmol/L: 1.6 ± 0.5 arbitrary units; P < 0.05; n = 50 cells per group; mean ± SD. H2O2 positive control: 5.7 ± 1.8 arbitrary units.[1]
Cells in G0/G1 phasePercent distribution 3.1 nmol/L: 78 ± 3.8%; 300 nmol/L: 63 ± 3.1%; P < 0.05; n = 3; mean ± SD[1]

Literature-Reported Treatment Conditions

Treatment concentration
3.1 nmol/L (deficient) versus 300 nmol/L (supplemented)
Exposure duration
4 days
Method
Riboflavin availability varied in customized culture medium
Vehicle
Customized RPMI-1640 plus 10% dialyzed, riboflavin-depleted bovine growth serum
Reported limits
Riboflavin stock vehicle, supplier, purity and analytical stereochemical confirmation are not specified in the selected cell-culture description.
Methods and source locations

Compound reported in the paper: Riboflavin; Compound label in the paper: Vitamin B2

Nutrient-availability comparison in one transformed cell line; concentrations are culture conditions, not IC50 values.

Sections 2.1–2.5, 2.8, 3.1–3.5; Fig. 3

Glutathione reductase activity: Glutathione reductase activity in cell lysates — Sections 2.1–2.2, 2.8 and 3.1

DNA strand-break-associated comet tail moment: Comet assay; positive control 100 μmol/L H2O2 for 1 h. The n = 50 denotes scored cells, not 50 independent cultures. — Sections 2.4, 2.8 and 3.3

Cells in G0/G1 phase: Propidium iodide flow cytometry; Fig. 3 inset; representative plots also mark apoptotic cells — Sections 2.5, 2.8 and 3.5; Fig. 3 and inset

Medium components alter riboflavin-dependent UVA peroxide production

Biochemical assay · Cell-free HBSS containing riboflavin, with individual vitamins or amino acids [2]

Riboflavin with folic acid, tryptophan, tyrosine, methionine or histidine produced more H2O2 after UVA than riboflavin alone; most other tested components did not significantly increase the response.

Measured endpoints — not treatment concentrations
EndpointReported resultReference
H2O2 production after UVARelative H2O2 amount versus riboflavin control Folic acid, tryptophan, tyrosine, methionine and histidine combinations increased H2O2 relative to irradiated riboflavin alone (** P < 0.01; Fig. 3 n = 3). Other tested additions were marked N.S.; no exact bar heights extracted.[2]

Literature-Reported Treatment Conditions

Treatment concentration
Riboflavin 1 μM; individual vitamin 10 μM or amino acid 100 μM
Exposure duration
UVA exposure 3.6 J/cm2; lamp spectrum 340–410 nm, 1.0 mW/cm2 for 1 h
Method
Cell-free photosensitization followed by H2O2 assay
Vehicle
HBSS
Co-treatment
Riboflavin plus one vitamin or amino acid per condition; results are combination effects
Reported limits
No IC50 determined. Figure 3 labels n = 3; methods state minimum three independent experiments. The figure does not explicitly define the plotted error-bar type.
Methods and source locations

Compound reported in the paper: Riboflavin; Compound label in the paper: Vitamin B2

Photochemical combination effects in cell-free buffer; not evidence that riboflavin alone is cytotoxic at these concentrations in darkness.

Results 2.2; Fig. 3a–b; methods 4.2, 4.4–4.5 and 4.13

H2O2 production after UVA: ADHP/horseradish-peroxidase fluorescence assay; matched non-exposed solutions and UVA-exposed riboflavin-only comparator; one-way analysis with the authors’ reported Dunnet II test — Results 2.2; Fig. 3a–b; methods 4.2, 4.5 and 4.13

In Vivo Studies

Dietary riboflavin deficiency in mice caused delayed, progressive reductions in retinal electrical responses. Early scotopic responses were preserved, and the later functional deficit preceded detectable loss of counted photoreceptors or cones at P240. This is evidence from dietary deprivation rather than an isolated-compound dosing study. [3]

Switching long-term deficient mice back to riboflavin-containing chow improved retinal responses after 60 days, with no improvement detected after 30 days. Some RPE abnormalities persisted despite functional recovery, so the experiment supports partial phenotypic rescue rather than complete structural normalization. [3]

Longitudinal retinal effects of dietary riboflavin deficiency

Animal study · Both-sex mice on C57BL/6J-129S1/SvImJ background, negative for rd8 and the RPE65 Leu450Met variant [3]

Deficient chow from P30 produced a delayed, progressive decline in ERG responses relative to regular chow. At P240 the functional deficit occurred without significant loss of counted photoreceptors or cones or reduction in outer-segment length.

Measured endpoints — not treatment concentrations
EndpointReported resultReference
Scotopic and photopic ERG amplitudesRelative decrease versus age-matched regular-chow mice No scotopic difference at P90/P120; significant scotopic decline from P180. At P300, scotopic a-wave reduced by 40% and photopic response by ~44% (text-reported).[3]
Photoreceptor/cone counts, outer-segment length and IPL thickness at P240Direction and significance No significant reduction in photoreceptor nuclei, cone count or mean outer-segment length; IPL thinning was detected.[3]

Conditions shared by the study groups

Route
Dietary, ad libitum
Frequency
Continuous access to assigned chow
Vehicle
AIN-93G-based chow (Envigo)
Study groups and reported outcomes
Group / doseComparatorObserved resultReference
Regular chow
6 ppm riboflavin in RC		Age-matched riboflavin-deficient chowReference retinal function and structure[3]
Riboflavin-deficient chow
RF-deficient AIN-93G; numerical riboflavin content not specified		Age-matched regular chowDelayed ERG decline with P240 IPL thinning; no significant P240 photoreceptor/cone loss or outer-segment shortening[3]
Regular chow
Model: Mice on C57BL/6J-129S1/SvImJ background; both sexes
Treatment course: Regular chow from birth through assessment
Reported limits: Food consumption and achieved mg/kg/day exposure are not provided for these comparisons; no dose conversion made.
Riboflavin-deficient chow
Model: Mice on C57BL/6J-129S1/SvImJ background; both sexes
Treatment course: RDC from P30 through assessment, up to P300
Reported limits: Food consumption and achieved mg/kg/day exposure are not provided for these comparisons; no dose conversion made.
Methods and source locations

Compound reported in the paper: Riboflavin; Compound label in the paper: Vitamin B2

Nutritional deficiency in mice, not pharmacological inhibition or treatment of a disease with an isolated riboflavin dose.

Sections 2.1, 2.7–2.8, 2.11, 2.13, 3.1–3.2; Fig. 2

Scotopic and photopic ERG amplitudes: Longitudinal full-field ERG; Fig. 2, n = 6–11 animals/age/group; points average both eyes from one animal; means ± SEM; two-way ANOVA with Sidak post-hoc test — Section 3.2; Fig. 2A–D and caption; methods 2.1 and 2.11

Photoreceptor/cone counts, outer-segment length and IPL thickness at P240: Retinal histology, morphometry and PNA cone labeling; Fig. 2F–J; no exact values estimated from graphs. Caption gives n = 3 for H–J and also n = 3–4 for I–J, an unresolved replicate-count inconsistency. — Section 3.2; Fig. 2E–J and caption; methods 2.7–2.8

Regular chow · Sections 2.1 and 3.1–3.2; Fig. 2

Riboflavin-deficient chow · Sections 2.1 and 3.1–3.2; Fig. 2

Late dietary repletion restores ERG responses but leaves RPE abnormalities

Animal study · Same mouse background; deficient chow P30–P240 followed by regular chow until P270 or P300 [3]

After 30 days of repletion ERG amplitudes did not improve versus continued deficiency. After 60 days, scotopic a-/b-wave and photopic b-wave amplitudes were statistically indistinguishable from regular-chow controls. Some enlarged multinucleated RPE cells and cytoplasmic β-catenin persisted.

Measured endpoints — not treatment concentrations
EndpointReported resultReference
Scotopic a-/b-wave and photopic b-wave amplitudesRecovery versus dietary controls At P270: no improvement versus RDC; at P300: responses statistically indistinguishable from RC. This is not an equivalence test.[3]
RPE morphology after 60 days of repletionPersistent abnormalities Enlarged multinucleated RPE cells and cytoplasmic β-catenin persisted in the RDC > RC group. RPE cell number was only partially rescued.[3]

Conditions shared by the study groups

Route
Dietary, ad libitum
Frequency
Continuous access to assigned chow
Vehicle
AIN-93G-based chow (Envigo)
Study groups and reported outcomes
Group / doseComparatorObserved resultReference
Continuous regular chow
6 ppm riboflavin in RC		Continued RDC and RDC > RCRegular-chow reference responses[3]
Continued deficiency
RF-deficient chow; numerical content not specified		Continuous RCPersistent functional deficit and RPE abnormalities[3]
Late repletion
Switch from deficient chow to RC containing 6 ppm riboflavin		Continuous RC and continued RDCNo 30-day ERG recovery; 60-day ERG recovery with residual RPE abnormalities[3]
Continuous regular chow
Model: Mice on C57BL/6J-129S1/SvImJ background; both sexes
Treatment course: RC through P300
Reported limits: Food consumption and achieved mg/kg/day exposure are not provided for these comparisons; no dose conversion made.
Continued deficiency
Model: Mice on C57BL/6J-129S1/SvImJ background; both sexes
Treatment course: RDC P30–P300
Reported limits: Food consumption and achieved mg/kg/day exposure are not provided for these comparisons; no dose conversion made.
Late repletion
Model: Mice on C57BL/6J-129S1/SvImJ background; both sexes
Treatment course: RDC P30–P240; then RC to P270 or P300
Reported limits: Food consumption and achieved mg/kg/day exposure are not provided for these comparisons; no dose conversion made.
Methods and source locations

Compound reported in the paper: Riboflavin; Compound label in the paper: Vitamin B2

Functional recovery and persistent structural abnormalities in a mouse deficiency model. Persistence at 60 days does not establish permanent irreversibility.

Sections 2.1, 2.9, 2.11, 2.13 and 3.6; Fig. 9A–C,G–H

Scotopic a-/b-wave and photopic b-wave amplitudes: Full-field ERG; Fig. 9A–C; n = 4–10, each point averages both eyes from one animal; mean ± SEM; one-way ANOVA with Holm-Sidak comparisons; P240 two-group t-test — Section 3.6, second paragraph; Fig. 9A–C and caption; methods 2.11

RPE morphology after 60 days of repletion: β-catenin/DAPI flatmount imaging and cell counts, Fig. 9G–H; 3 independent animals/cohort, 6 regions per sample; no exact bar values inferred — Section 3.6; Fig. 9G–H and caption; methods 2.9

Continuous regular chow · Sections 2.1, 3.1 and 3.6; Fig. 9

Continued deficiency · Section 3.6; Fig. 9

Late repletion · Section 3.6; Fig. 9A–C,G–H

Specifications

Manufacturer Adooq Bioscience
CAS Number 83-88-5
Applications Vitamin B2
Formula C17H20N4O6
Molecular Weight 376.36
Synonyms Vitamin B2; E101
SMILES
O[C@H]([C@H](O)[C@H](O)CO)CN1C(C=C(C)C(C)=C2)=C2N=C(C(N3)=O)C1=NC3=O

Storage & Solubility

In Vitro Solubility

Reported Solubility

No reported solubility data are available for this product.

Preparing Stock Solutions

Stock preparation is unavailable for this product molecular weight.

Calculated stock concentrations do not establish solvent solubility. Refer to the reported solubility data for experimental guidance.

Storage

Store powder at -20°C, keep desiccated.
In powder form, the chemical is stable for 36 months.
In solution, store at -20°C and use within 1 month to prevent loss of potency. Aliquot to avoid multiple freeze/thaw cycles.

Research References

  1. [1] Manthey KC, Rodriguez-Melendez R, Hoi JT, et al. Riboflavin deficiency causes protein and DNA damage in HepG2 cells, triggering arrest in G1 phase of the cell cycle. The Journal of nutritional biochemistry (2006). PMID: 16109485 DOI: 10.1016/j.jnutbio.2005.05.004 Source material
  2. [2] Yoshimoto S, Kohara N, Sato N, et al. Riboflavin Plays a Pivotal Role in the UVA-Induced Cytotoxicity of Fibroblasts as a Key Molecule in the Production of H2O2 by UVA Radiation in Collaboration with Amino Acids and Vitamins. International journal of molecular sciences (2020). PMID: 31952279 DOI: 10.3390/ijms21020554 Source material
  3. [3] Sinha T, Ikelle L, Makia MS, et al. Riboflavin deficiency leads to irreversible cellular changes in the RPE and disrupts retinal function through alterations in cellular metabolic homeostasis. Redox biology (2022). PMID: 35738087 DOI: 10.1016/j.redox.2022.102375 Source material

Added to your cart

View Cart Checkout
Loading...