VetPlus Acrylic Syrup 500ml for Dogs & Cats

FOR ANIMAL USE ONLY — Administer as directed by a veterinarian or as per the VetPlus label instructions. VetPlus Acrylic Syrup is a veterinary nutraceutical multi-vitamin, mineral, and amino acid supplement — not a veterinary medicine. Acrylic Syrup is indicated as a nutritional supplement to support immunity, energy, and overall wellness in dogs and cats of all breeds and life stages. It is not a substitute for veterinary diagnosis or treatment of any underlying medical condition. Pets showing signs of illness, weakness, chronic lethargy, persistent poor appetite, or weight loss require veterinary assessment to identify and treat the underlying cause — Acrylic Syrup is a supportive nutritional supplement, not a therapeutic medicine. Keep out of reach of children. Store in a cool, dry place away from direct sunlight; shake well before use and close the bottle securely after each use.

VetPlus Acrylic Syrup 500ml for Dogs & Cats | Multi-Vitamin, Mineral & Amino Acid Syrup | Immunity, Energy, Metabolism & Overall Wellness Support | All Breeds & Life Stages

VetPlus Acrylic Syrup 500ml is a veterinary nutraceutical multi-vitamin, mineral, and amino acid supplement manufactured by VetPlus Ltd (UK), formulated for daily nutritional support in dogs and cats of all breeds and life stages. Acrylic Syrup provides a comprehensive blend of fat-soluble vitamins (A, D3, E), water-soluble B-complex vitamins (B1 thiamine, B2 riboflavin, B6 pyridoxine, B12 cyanocobalamin, niacin/niacinamide, pantothenic acid, folic acid, biotin), vitamin C (ascorbic acid), essential minerals (calcium, phosphorus, zinc, manganese, iodine), and the essential amino acids lysine and methionine — all in a palatable liquid syrup format for easy oral administration. The 500ml value-pack format provides an extended supply for multi-pet households, large breeds, or sustained daily supplementation programmes. Acrylic Syrup is indicated for general nutritional support in healthy pets, during periods of increased physiological demand (growth, pregnancy, lactation, recovery from illness or surgery, seasonal stress, high activity), and as a palatable micronutrient supplement for pets with reduced dietary intake.

Why Multi-Micronutrient Supplementation Matters in Dogs & Cats

• Nutritional gaps in commercial pet diets and high-demand life stages: while complete and balanced commercial pet foods are formulated to meet minimum AAFCO (Association of American Feed Control Officials) or FEDIAF (European Pet Food Industry Federation) nutrient profiles, several factors can create relative micronutrient insufficiency in individual animals: (a) home-cooked or raw diets: home-prepared diets (increasingly popular among Indian pet owners as an alternative to commercial kibble) frequently fail to meet micronutrient requirements — vitamin D3 (no meaningful UV-synthesised cholecalciferol in carnivores fed organ/muscle meat without UV-irradiated skin or fortified food), riboflavin (B2 — degraded by light exposure and cooking), folic acid (heat-labile), and iodine (absent in most meat without iodised salt or seafood) are the most commonly deficient micronutrients in home-cooked pet diets; (b) high-demand life stages: growth (puppies/kittens — skeletal mineralisation [calcium/phosphorus/D3/vitamin K2] and rapid cell proliferation [folic acid, B12, zinc] have proportionally higher micronutrient demands than maintenance; a 20kg puppy growing to adult weight in 12 months requires approximately 2–3x the weight-adjusted calcium and phosphorus of an adult dog), pregnancy and lactation (the fetal/neonatal calcium/phosphorus demand on the dam’s skeleton and colostrum/milk immunoglobulin synthesis [requiring lysine and methionine as immunoglobulin heavy/light chain structural amino acids and for hepatic immunoglobulin synthesis (N-glycosylation of IgG asparagine residues requires adequate methionine as the methyl donor via SAM [S-adenosylmethionine] for the methylation steps of N-glycan maturation)] are substantial micronutrient loads); (c) illness and recovery: acute febrile illness (each 1°C rise in body temperature increases metabolic rate by approximately 7–10% via Q10 thermodynamic effect on enzymatic reaction rates — particularly the rate-determining mitochondrial OXPHOS enzymes [Complex I–V] whose substrate consumption increases with temperature → increased B-vitamin cofactor turnover [particularly thiamine [TPP], riboflavin [FAD/FMN], niacin [NAD+], and pantothenic acid [CoA]]); surgical recovery (accelerated protein synthesis for wound healing [collagen synthesis requires vitamin C as prolyl/lysyl hydroxylase cofactor; lysine is required as a collagen structural amino acid − the lysine-derived hydroxylysine cross-links of mature collagen fibres provide tensile strength; methionine is the methyl donor for proline N-methylation in collagen]); (d) senior pets: ageing reduces nutrient absorption efficiency (B12 absorption from the ileum requires intrinsic factor [IF – gastric parietal cell glycoprotein – IF secretion declines with age-related gastric mucosal atrophy → reduced B12 absorption]; fat-soluble vitamin absorption from the small intestinal enterocyte requires adequate bile salt secretion and pancreatic lipase – both decline with age-related pancreatic exocrine insufficiency [PEI in senior dogs and cats is under-recognised])

Active Ingredients & Mechanisms of Action

• Vitamin A (retinol/retinyl esters) — the fat-soluble vitamin for immune function, epithelial integrity, and vision: vitamin A (all-trans retinol; MW 286.45 g/mol; the parent alcohol form; stored as retinyl esters [retinyl palmitate, retinyl stearate] in hepatic stellate cells [Ito cells] in lipid droplets; mobilised as retinol bound to retinol-binding protein 4 [RBP4] complexed with transthyretin [TTR] in plasma; the RBP4–TTR complex prevents glomerular filtration of the small RBP4 molecule [21 kDa]; delivered to target cells via STRA6 [stimulated by retinoic acid 6] receptor-mediated retinol uptake) functions via its active metabolites: (a) 11-cis retinal — the visual chromophore: retinal is the aldehyde form of vitamin A; 11-cis retinal is covalently bound to opsin (the apoprotein of rhodopsin in rod photoreceptors and of the three cone opsins in cone photoreceptors) via a protonated Schiff base between the aldehyde and Lys296 of the opsin seventh transmembrane helix → rhodopsin; photon absorption → 11-cis → all-trans isomerisation of retinal → conformational change in rhodopsin → metarhodopsin II → G-protein transducin (Gt) activation → cGMP phosphodiesterase activation → cGMP hydrolysis → cGMP-gated Na+ channel closure → rod cell hyperpolarisation → the visual signal; vitamin A deficiency → night blindness (nyctalopia) − the classic early sign of vitamin A deficiency, particularly in cats (cats have a high rod photoreceptor density relative to cones and high retinal turnover); (b) all-trans retinoic acid (ATRA) — the transcriptional regulator: retinol → retinaldehyde (via alcohol dehydrogenase ADH1B/ADH1C or retinol dehydrogenase RDH10 [the primary retinol → retinaldehyde enzyme in most tissues]) → ATRA (via retinaldehyde dehydrogenase ALDH1A1/1A2/1A3 [RALDH enzymes]); ATRA → nuclear retinoic acid receptors (RARα/β/γ – NR1B family of ligand-activated nuclear receptors; RAR forms obligate heterodimers with RXRα/β/γ [retinoid X receptors]; RAR–RXR heterodimers bind retinoic acid response elements [RAREs: direct repeats of the core AGGTCA motif with 1–5 bp spacing] in the promoters of ATRA-target genes); ATRA’s immune targets: (i) innate immunity: ATRA drives differentiation of monocytes → dendritic cells (DCs) and macrophages (ATRA induces IRF4 and C/EBPβ expression → monocyte–DC differentiation); ATRA activates NK cell cytotoxicity (upregulates NKG2D expression on NK cells); (ii) adaptive immunity: ATRA is essential for T-helper cell (Th) differentiation: ATRA → RARα → Foxp3+ regulatory T cell (Treg) generation (ATRA promotes TGF-β-driven Foxp3 induction in naive CD4+ T cells in the gut-associated lymphoid tissue [GALT] → mucosal immune tolerance − relevant to reducing food allergy and inflammatory bowel disease risk); ATRA also promotes Th2 differentiation and suppresses Th17 differentiation; IgA class switching: ATRA promotes B-cell class switch recombination to IgA (via ATRA-driven upregulation of APRIL [a proliferation-inducing ligand] and BAFF [B-cell activating factor] in DCs → IgA+/α-chain B-cell differentiation → IgA secretion by intestinal plasma cells → secretory IgA [sIgA] — the primary immunoglobulin of mucosal immunity); (c) epithelial integrity: ATRA maintains the differentiation of stratified squamous epithelium → vitamin A deficiency → squamous metaplasia of columnar and transitional epithelia (respiratory tract, urinary tract, conjunctiva, and salivary gland ductal epithelium undergo keratinising squamous metaplasia under vitamin A deficiency → reduced mucociliary clearance, reduced urinary tract antibacterial protection, and reduced tear film quality)
• Vitamin D3 (cholecalciferol) — the secosteroid for calcium/phosphorus homeostasis and immune modulation: (a) dogs and cats do NOT synthesise adequate vitamin D3 from sun exposure (unlike humans and most other mammals, the skin of dogs and cats has minimal 7-dehydrocholesterol [7-DHC] content in the stratum spinosum relative to the stratum basale, and the thick hair coat further reduces UV-B penetration − dogs and cats are therefore dietary vitamin D-dependent [they cannot rely on UV-B cutaneous synthesis for adequate D3 status]; this is a critical difference from dogs’ and cats’ ancestral diet [organ meat and whole prey, which provides liver vitamin D3 stores] and explains why home-cooked diets without vitamin D supplementation or UV-irradiated mushroom/fish sources lead to vitamin D deficiency); (b) bioactivation: cholecalciferol [D3] → hepatic CYP2R1 [the primary hepatic 25-hydroxylase] → 25-hydroxyvitamin D3 [25(OH)D3; calcidiol − the major circulating form and the clinical measure of vitamin D status] → renal CYP27B1 [1α-hydroxylase, expressed predominantly in the proximal tubule] → 1,25-dihydroxyvitamin D3 [1,25(OH)2D3; calcitriol − the biologically active hormone]; (c) calcitriol acts via the vitamin D receptor (VDR; NR1I1 − a nuclear receptor of the NR1 subfamily; forms obligate heterodimers with RXRα; binds vitamin D response elements [VDREs: direct repeats of AGGTCA with 3 bp spacing in the DR3 configuration] in the promoters of VDR-target genes); VDR target genes in mineral homeostasis: intestinal TRPV6 (the apical calcium channel of duodenal enterocytes − mediates transcellular Ca2+ absorption), calbindin-D9k (the cytosolic Ca2+ ferry protein that shuttles Ca2+ from TRPV6 to the basolateral PMCA1b Ca2+-ATPase for export into portal blood), NPT2b (the intestinal Na+-phosphate cotransporter for phosphate absorption); (d) VDR immune functions: VDR is expressed in virtually all immune cells (monocytes, macrophages, T cells, B cells, DCs, NK cells); 1,25(OH)2D3 → VDR in macrophages → upregulation of cathelicidin (CAMP [LL-37 in humans; CRAMP in dogs] − the cationic antimicrobial peptide that disrupts bacterial membranes) and defensin-β4 → innate antimicrobial defence; 1,25(OH)2D3 in T cells: promotes Treg differentiation (Foxp3 upregulation) and suppresses Th17 differentiation (RORγt downregulation → reduced IL-17A/F) → immune balance; anti-inflammatory: 1,25(OH)2D3 inhibits NF-κB activity (VDR competes with NF-κB p65 for CBP/p300 coactivator binding at inflammatory gene promoters) and promotes IL-10 production (by Tregs and tolerogenic DCs)
• Vitamin E (d-alpha-tocopherol) — the lipid-soluble chain-breaking antioxidant and immune activator: as described for Aktivait; specifically in the immunity context: vitamin E at supplemental doses (above the AAFCO minimum requirement) enhances: (a) lymphocyte proliferation in response to mitogen stimulation (PHA [phytohemagglutinin] and ConA [concanavalin A] proliferation assays in dogs: vitamin E supplementation increases lymphocyte proliferation index); (b) NK cell cytotoxicity (vitamin E upregulates perforin and granzyme B expression in NK cells); (c) IgG antibody titres following vaccination in dogs and cats (vitamin E is the most consistently immunopotentiating vitamin across species at supplemental doses; the mechanism involves vitamin E’s effect on macrophage prostaglandin E2 [PGE2] synthesis − macrophage-derived PGE2 [via arachidonic acid → COX-2 → PGH2 → microsomal PGE2 synthase 1 (mPGES-1)] suppresses T-cell proliferation and IL-2 production; vitamin E inhibits COX-2 expression in macrophages [via Nrf2-mediated HO-1 upregulation and NF-κB inhibition] → reduced macrophage PGE2 → disinhibited T-cell and B-cell responses)
• B-complex vitamins — the metabolic enzyme cofactor family essential for energy production, immune cell proliferation, and neurotransmitter synthesis: (a) Thiamine (B1/TPP) — pyruvate dehydrogenase (PDH) complex cofactor for neuronal glucose oxidation; cats are at higher risk of thiamine deficiency than dogs (higher dietary protein–to–carbohydrate ratio in feline metabolism → higher thiaminase exposure from raw fish diets; higher thiamine turnover from the obligate carnivore’s high taurine/thiamine metabolic flux); (b) Riboflavin (B2/FAD/FMN) — FAD is the prosthetic group of Complex I (NADH:FMN → FMNH2 → FeS clusters → CoQ10), Complex II (FADH2 → CoQ10), and the electron-transfer flavoprotein (ETF → fatty acid β-oxidation); FMN is the immediate electron acceptor from NADH at Complex I’s FMN-binding site (ND1/ND2 subunit interface); riboflavin is light-sensitive and heat-labile — the first vitamin to degrade in stored commercial pet food; (c) Niacin (B3/NAD+) — cats cannot synthesise niacin from tryptophan (unlike dogs and humans, cats have very high hepatic picolinic acid carboxylase [ACMSD] activity that diverts tryptophan → picolinic acid [a dead-end metabolite] instead of quinolinate → NAD+ — this enzyme difference makes cats entirely dietary-niacin-dependent; this is the mechanistic basis of the AAFCO feline niacin requirement being approximately 4x higher than the canine requirement on a per-kg metabolic weight basis); (d) Pantothenic acid (B5/CoA) — CoA (coenzyme A; 3’-phospho-ADP conjugated to pantothenate via 4’-phosphopantetheine) is the universal acyl carrier: acetyl-CoA (TCA cycle entry; cholesterol/fatty acid synthesis), succinyl-CoA (TCA cycle; heme synthesis), and malonyl-CoA (fatty acid chain elongation); (e) Pyridoxine (B6/PLP) — GAD65/67 GABA synthesis cofactor; AADC serotonin/dopamine cofactor; transaminase [AST/ALT] cofactor (PLP is the Schiff base-forming cofactor for all amino acid transaminases — the pyridoxamine phosphate [PMP] form is the cofactor in the second half-reaction of transamination); (f) Cyanocobalamin (B12/cobalamin) — methylcobalamin cofactor for methionine synthase (5-methyltetrahydrofolate [5-MTHF] + homocysteine → methionine + tetrahydrofolate [THF]; the methylcobalamin methyl transfer reaction regenerates THF for the folate cycle → dTMP synthesis → DNA replication in proliferating cells including lymphocytes); adenosylcobalamin cofactor for methylmalonyl-CoA mutase (the mitochondrial isomerisation of methylmalonyl-CoA [from odd-chain fatty acid β-oxidation and branched-chain amino acid catabolism] → succinyl-CoA [TCA cycle entry]); (g) Folic acid (B9) — after reduction to dihydrofolate [DHF] and tetrahydrofolate [THF] by dihydrofolate reductase [DHFR], THF becomes the C1 carrier for: dTMP synthesis (5,10-methylene-THF + dUMP → dTMP + DHF [thymidylate synthase reaction] — the rate-limiting step of pyrimidine nucleotide synthesis for DNA replication); purine synthesis (10-formyl-THF as the C2 and C8 donor in the purine ring de novo synthesis pathway); methionine cycle (5-MTHF + homocysteine → methionine [via B12/methionine synthase]); rapidly proliferating lymphocytes (the cells of the adaptive immune response) have a high demand for folic acid (lymphocyte blast transformation and clonal expansion require extensive DNA replication); (h) Biotin (B7/biocytin) — the covalently bound cofactor of the biotin-dependent carboxylases: pyruvate carboxylase [PC: pyruvate + CO2 + ATP → oxaloacetate − the anaplerotic TCA cycle entry for gluconeogenesis], acetyl-CoA carboxylase [ACC1/2: acetyl-CoA + CO2 → malonyl-CoA − fatty acid synthesis initiation], propionyl-CoA carboxylase [PCC: propionyl-CoA + CO2 → methylmalonyl-CoA − odd-chain fatty acid and branched-chain amino acid catabolism], and β-methylcrotonyl-CoA carboxylase [MCC: in leucine catabolism]
• Vitamin C (ascorbic acid) — the aqueous antioxidant, collagen cofactor, and immune cell activator: dogs and cats synthesise ascorbate endogenously (via the glucuronolactone pathway: glucose → UDP-glucuronate → glucuronolactone → L-gulonolactone → L-gulonolactone oxidase [GULO] → ascorbate; dogs and cats retain functional GULO unlike humans and guinea pigs [who have pseudogenised GULO due to inactivating mutations]); however, GULO-synthesised ascorbate may be insufficient during high oxidative stress states (illness, fever, surgery, intensive training) → supplementary ascorbate supports: (a) collagen synthesis (prolyl hydroxylase [P4H] and lysyl hydroxylase [PLOD1/2/3] require Fe2+-ascorbate for the hydroxylation of proline and lysine residues in nascent collagen chains → hydroxyproline and hydroxylysine → triple helix formation and cross-linking); (b) immune cell function (ascorbate is concentrated 10–100-fold in neutrophils, lymphocytes, and monocytes vs plasma → SVCT2-mediated active uptake; neutrophil ascorbate supports myeloperoxidase [MPO] oxidative burst without depleting intracellular GSH); (c) iron absorption enhancement (ascorbate reduces Fe3+ → Fe2+ in the GI tract → Fe2+ is absorbed by DMT1 [divalent metal transporter 1/SLC11A2] in duodenal enterocytes; Fe3+ is poorly absorbed)
• Minerals (calcium, phosphorus, zinc, manganese, iodine) — essential structural and catalytic elements: (a) calcium and phosphorus — skeletal mineralisation (hydroxyapatite [Ca10(PO4)6(OH)2] − the mineral phase of bone [~65% of bone dry weight]; bone mineral crystal nucleation occurs at matrix vesicles [MV − osteoblast-derived lipid bilayer vesicles enriched in TNAP (tissue-nonspecific alkaline phosphatase), annexin V, and phosphatidylserine; TNAP hydrolyses inorganic pyrophosphate [PPi − the endogenous inhibitor of hydroxyapatite crystal growth] → Pi → Ca2+–Pi supersaturation within the MV → hydroxyapatite crystal nucleation → crystal growth and propagation into the collagen fibril framework of the ECM]); neuromuscular signalling (Ca2+ as the second messenger for muscle contraction [the Ca2+–calmodulin–MLCK pathway for smooth muscle; the Ca2+–troponin C switch for cardiac and skeletal muscle] and for neurotransmitter exocytosis [voltage-gated Ca2+ channel [Cav2.1/Cav2.2] opening at the presynaptic active zone → Ca2+ influx → synaptotagmin 1 [C2A/C2B domain Ca2+/PS cooperative binding] → SNARE complex stabilisation → vesicle fusion]); (b) zinc — the most abundant intracellular trace element and essential catalytic cofactor for >300 metalloenzymes: (i) immune function: zinc is essential for thymulin (the thymic hormone that promotes T-cell maturation − thymulin is a nonapeptide with zinc as an obligate cofactor for its biological activity; zinc deficiency → reduced thymulin activity → impaired T-cell maturation in the thymus → reduced naive T-cell output → impaired adaptive immunity); (ii) antioxidant: zinc is a structural component of Cu/Zn-SOD1 (cytosolic superoxide dismutase 1 − the primary cytosolic •O2− dismutase: 2•O2− + 2H+ → H2O2 + O2; the catalytic mechanism cycles between Cu2+ [oxidised, reduced by •O2−] and Cu+ [reduced, oxidised by the second •O2−]; zinc provides structural stabilisation of the SOD1 homodimer interface); (iii) wound healing (zinc is a cofactor for the matrix metalloproteinases [MMPs − the Zn2+/Ca2+-dependent endopeptidases that remodel the ECM during wound healing: MMP-1 collagenase, MMP-9 gelatinase B, MMP-13 collagenase 3]); (c) manganese — cofactor for MnSOD2 (the mitochondrial matrix superoxide dismutase − the primary defence against mitochondrial •O2−) and for arginase (Arg1/Arg2 − the enzyme that converts L-arginine → L-ornithine + urea in the urea cycle); manganese is also a cofactor for glucosyltransferases and galactosyltransferases involved in proteoglycan synthesis (glycosaminoglycan [GAG] chain initiation: xylosyltransferase, galactosyltransferase I/II, and glucuronosyltransferase I add the core tetrasaccharide [Xyl–Gal–Gal–GlcUA] to the serine of core proteoglycan proteins [aggrecan, versican, decorin, biglycan] before GAG chain extension); (d) iodine — the essential element for thyroid hormone synthesis: iodide (I−) is actively transported into thyroid follicular cells by the sodium-iodide symporter (NIS/SLC5A5) → oxidised to I0 by thyroid peroxidase (TPO) + H2O2 → iodination of tyrosine residues on thyroglobulin (MIT [3-monoiodotyrosine] and DIT [3,5-diiodotyrosine]) → TPO-catalysed coupling reaction: MIT + DIT → T3 [3,5,3’-triiodothyronine] and DIT + DIT → T4 [thyroxine/tetraiodothyronine]; thyroid hormones regulate basal metabolic rate (BMR) via TRE [thyroid hormone response element]-mediated induction of SERCA1a [skeletal muscle SR Ca2+-ATPase − the ‘thermogenic futile Ca2+ cycle’ − TH drives SERCA1a expression → increased SR Ca2+ cycling → futile ATP hydrolysis → heat generation], UCP1 [thermogenin − via indirect β2-AR/cAMP pathway upregulation], and mitochondrial biogenesis [via PGC-1α – TH upregulates PGC-1α transcription via a TRE in the PGC-1α promoter]); iodine deficiency → hypothyroidism → reduced BMR → weight gain, lethargy, and cold intolerance in dogs and cats (particularly relevant for home-cooked diets without iodised salt or seafood)
• Lysine and methionine — the two essential amino acids of primary nutritional concern in dogs and cats: (a) L-lysine: (i) structural amino acid for collagen (lysine is hydroxylated by lysyl hydroxylase [PLOD1/2/3] → hydroxylysine; hydroxylysine is the site of O-glycosylation [galactose and glucose] and of the allysine-derived cross-links [formed by lysyl oxidase (LOX) − a Cu2+-dependent amine oxidase that converts ε-amino groups of lysine and hydroxylysine to reactive aldehydes [allysine] → spontaneous Schiff base or aldol cross-link formation between adjacent collagen chains → mature collagen fibril tensile strength]); (ii) carnitine synthesis: lysine + methionine → ε-N-trimethyllysine (TML via lysine N-methyltransferase, SAM-dependent) → 3-hydroxy-TML → 4-trimethylaminobutyraldehyde → 4-N-trimethylaminobutyrate [butyrobetaine] → butyrobetaine dioxygenase (BBD/γ-BBD, Fe2+/ascorbate/α-ketoglutarate-dependent) → L-carnitine [the rate-limiting step is butyrobetaine dioxygenase, which requires vitamin C as the Fe2+ reductant]; (iii) lysine is the precursor for glutamate and succinate in the saccharopine pathway (lysine → saccharopine [via α-aminoadipic semialdehyde synthase/AASS] → α-aminoadipate semialdehyde → α-aminoadipate → α-ketoadipate → glutaryl-CoA → acetyl-CoA [TCA cycle]; lysine catabolism’s TCA cycle contribution is relevant during caloric stress); (iv) lysine is the first limiting essential amino acid in plant-based proteins (cereal proteins: low lysine content is the primary nutritional limitation of wheat, corn, and rice proteins − hence the emphasis on lysine supplementation in pet diets that use plant protein sources); (b) L-methionine: (i) SAM [S-adenosylmethionine] synthesis: methionine + ATP → SAM [via MAT1A/MAT2A: methionine adenosyltransferase] → SAM is the universal methyl donor for: DNA methylation (DNMT1/3A/3B: CpG methylation → epigenetic gene regulation), histone methylation (SET domain methyltransferases: H3K4me3 [active transcription mark], H3K27me3 [repressive mark]), RNA methylation (m6A: METTL3/14 writer complex → N6-methyladenosine in mRNA → mRNA stability, translation efficiency, and splicing regulation), catecholamine inactivation (COMT [catechol-O-methyltransferase] → dopamine methylation → 3-methoxytyramine; noradrenaline methylation → normetanephrine), and creatine synthesis (guanidinoacetate N-methyltransferase [GAMT]: guanidinoacetate + SAM → creatine + SAH [S-adenosylhomocysteine]); (ii) cysteine synthesis: methionine → SAH → homocysteine [via SAH hydrolase: SAH + H2O → homocysteine + adenosine] → cystathionine [via CBS: cystathionine β-synthase, PLP-dependent] → cysteine [via CGL: cystathionine γ-lyase, PLP-dependent]; cysteine is the rate-limiting amino acid for GSH synthesis; (iii) methionine is also the first codon (AUG) of every eukaryotic mRNA − methionyl-tRNAiMet is the universal translation initiator charged by MetRS [methionyl-tRNA synthetase]

Indications

• Daily multi-vitamin and mineral nutritional support for dogs and cats of all breeds and life stages
• Nutritional supplementation during high-demand periods: growth (puppies and kittens), pregnancy, lactation, recovery from illness or surgery
• Supportive supplementation for senior dogs and cats with age-related decline in nutrient absorption
• Nutritional support for pets on home-cooked or raw diets that may be deficient in specific micronutrients
• Adjunctive support during seasonal stress, high activity, or intense training
• Palatability-friendly micronutrient delivery for pets who resist capsule or tablet supplementation

Directions for Use

• Administer as directed by a veterinarian or as per VetPlus label dosing instructions; dose is typically weight- and life-stage-dependent
• Administer orally — directly into the mouth or mixed into food; the palatable syrup formulation is accepted by most dogs and cats
• Shake well before each use; close the bottle securely after administration to prevent contamination
• 500ml value pack; store in a cool, dry place away from direct sunlight

Safety Information

• For animal use only — keep out of reach of children
• Do not exceed the recommended dose; excess fat-soluble vitamins (A and D3) can accumulate to toxic levels — vitamin A toxicity (hypervitaminosis A) causes cervical spondylosis and periosteal new bone formation in cats; vitamin D3 toxicity causes hypercalcaemia and soft tissue mineralisation
• Pets with ongoing medical conditions should receive veterinary guidance before supplementation
• Store in a cool, dry place; discard if the syrup changes colour, odour, or consistency