Dagatron Auto Stainer AT-2000GGRAM

Stop hard Manual staining. Exact results from all medical laboratories in the world!

Specimens according to GRAM staining method by automated system control.

This new innovated stainer features advanced functions and performances over manual

staining or automated dip-type stainers, include simplicity and convenience.

It can be provide safety and comfortable environment of test lab.

Accurate and precision Stain

This GRAM Auto Stainer provides fast, easy and stable staining process for staining clinical

Can be used by simple operation and it can be available to obtain accurate and precision stain.


  • No cross-contamination in all of process.
  • Reduction in labor costs.
  • Self cleaning system to clean tray
  • Checking and Warning for lower level of reagents.
  • Minimize personal variation during staining.


AT-2000GGRAM Stainer  
Slide Trey Capacity   1 slide ~10 slides(1 to 20 slides by adding Optional Tray) 
Tray Rotation Speed   Approximately, 6RPM (Stain Mode) / Approximately, 200RPM(DRY Mode) 
Display  4 Line by 20 character alpha-numeric LCD dot-matrix 
Key Button Controls   6 Mode Key(Stain, Prime, Clean, Dry, Reset, Slide up/down)  6 Function selection 
Used Reagent / Consumption(Typical)    Crystal Violet / Gram-lodine / Acetone Alcohol / Safranine 1.2ml~1.8ml 
1 Cycle Stain time(Typical)   10 slides : 13 min. / 20 slides: 18 min.(Option)
Dimensions   480(W) x 445(D) x 265(H)mm. Clearance Height(Lid open): Max. 565mm 
Weight   Approx. 17 kgs
Electrical Requirements   100~240VAC~(Auto selection)@50 to 60 Hz
Power Consumption   Max.50 Watts
Drain Connection   Nipple on rear Panel
Safety   Lid interlock : Lid must be closed, andis locked down during operation 
Standard Accessies   1L Reagent Bottle(1set), 5L Waterbottle(1), Reagent Container(1) Reagent Container cable(1), Powercord(1), Drain hose(1) Ragent connection Tube(1 set), User’smanual(1) Quick installation and user’s guide(1),Spare fuse(1), Carbon filer(5) 
Optional Accessaries   Additional slide for 10 slides


Kronos HT WSL-1565 with Brochure 2019

NEW WSL-1565 Kronos HT Brochure 2019

Download (PDF, 84.55MB)


Kronos HT main unit, Control software (for Windows PC), CO2gas mixer, Humidifying unit, 24 well plate adapter

  • High throughput live cell realtime reporter assay
  • Measuring with temperature and CO2 controlled incubation chamber
  • 24 well plate x 2 or 96 well plate x 2 (option)
  • Data display with real-time
  • Detectors scan each well, so culture plates don’t move.
  • Lower noise by PMT cooling
  • Dual-color luciferase assay by optical filter auto-changing

Detector: Photomultiplier tube (10oC cooling) x 2 units, X-Y actuating
Measurement: Photon counting method
Measurement time: Integral time: 1 – 60 s/well, Measurement term: 1 h – 30 days
Plate format: Clear bottom 24 well plate x 2 (Standard)
Clear bottom 96 well plate x 2 (Option), 35 mm dish x 12 (Option)
48 samples (24 well plate x 2)
192 samples (96 well plate x 2, option)
12 samples (35 mm dish x 12, option)
Incubation temperature control: Room temperature + 5oC to 45oC at room temperature 20 – 28oC
CO2 gas control: Control to 5% by CO2 gas mixer
Setting of water reservoir in incubator and humidified 5% CO2 gas flowing intermittently by
humidifying unit
Maintaining >90%RH
Multi-color assay: Measurement with automatically selected optical filter up to 2 colors
PC requirements OS: Windows 10 / 8.1 / 7, 64 / 32 bit, Memory: 4 GB, HDD: more than 20 GB free space
Interface: USB2.0 x 1 port
Dimensions, Weight:
Main unit: 650 (W) x 520 (D) x 340 (H) mm, 40 kg
CO2 gas mixer: 160 (W) x 300 (D) x 200 (H) mm, 4.8 kg
Humidifying unit: 170 (W) x 140 (D) x 115 (H) mm, 1.6 kg
Main unit: AC 100 – 240 V, 50 / 60 Hz, 400 W (max)
CO2 gas mixer: AC 100 – 240 V, 50 / 60 Hz, 100 W (max)
Humidifying unit: AC 100 – 240 V, 50 / 60 Hz, 24W (max)

Model 3510146: 24 well plate adapter
Model 3510147: 96 well plate adapter
Model 3510148: 35 mm dish adapter

Application data

Circadian rhythm of clock gene expression

Transcriptional activity of clock gene, mPer2
mPer2 promoter – Eluc (PEST) expressed fibroblast stable
cell line in 24 well clear bottom plate
Measurement time: 5s / well, Interval time: 10min

Drug response of transcription factor

Dual-color real-time luciferase assay of TNF-a induced NF-kB transcriptional activity

NF-kB response elemnt – TK promoter – SLG (green color emited luciferase) and TK promoter – SLR (red color emitted luciferase)
expressed fibroblast cell line in 96 well clear bottom plate
Measurement time: 5s x 2 color / well, Interval time: 30min
(A), (B) Transcriptional activity of NF-kB and TK promoter for 48h
(C) Normalized by activity of control (TK)
(D) Ratio to NF-kB activity without TNF-a


Kronos HT WSL-1565

High throughput real-time luciferase assay system

  • High throughput live cell realtime reporter assay
  • Measuring with temperature and CO2 controlled incubation chamber
  • 24 well plate x 2 or 96 well plate x 2 (option)
  • Data display with real-time
  • Detectors scan each well, so culture plates don’t move.
  • Lower noise by PMT cooling
  • Dual-color luciferase assay by optical filter auto-changing


Phosphoprotein phosphatase

Phosphoprotein phosphatase (protein phosphatase 1, protein phosphatase 2A, protein phosphatase 2B, protein phosphatase 2C, D protein phosphatase fosfospektrinska phosphatase, casein phosphatase, Aspergillus awamori acid protein phosphatase, calcineurin, phosphatase 2A, phosphatase 2B phosphatase II, IB phosphatase, phosphatase C-II, polikatjonom modulated (PCM) phosphatase, fosfopiruvat dehydrogenase phosphatase, phosphatase SP dehydrogenase phosphatase alpha-keto acids of branched chain BCKDH phosphatase, 3-hydroxy 3-methylglutaryl coenzyme reductase phosphatase , HMG-KoA reductase phosphatase, phosphatase H-II, III phosphatase, and phosphatase, protein phosphatase, phosphatase IV) is an enzyme with the systematic name phosphoprotein phosphohydrolase. [1] [2] [3] [4] This enzyme catalyzes the following chemical reaction.


Structure of the PPP3CA protein. Based on PyMOL rendering of PDB 1aui

This group of enzymes removes the phosphate group linked to serine or threonine with a wide range of phosphoproteins.


1. ^ Deutscher, J., Kessler, U. and Hengstenberg, W. (1985). “Streptococcal phosphoenolpyruvate: sugar phosphotransferase system: purification and characterization of a phosphoprotein phosphatase hydrolyzes Which phosphorylate the bond in seryl-phosphorylated histidine-containing protein.” J. Bacteriol. 163: 1203-1209. PMID 2,993,239th
2. ^ Ingebritsen, TS and Cohen, P. (1983). “The protein phosphatases involved in cellular regulation. 1 Classification and substrate specificities. “Eur. J. Biochem. 132: 255-261. PMID 6,301,824th
3. ^ Sundarajan, TA and Sarma, P.S. (1959). “Substrate specificity of phosphoprotein phosphatase from spleen.” Biochem. J. 71: 537-544. PMID 13,638,262th
4. ^ Tonks, NK and Cohen, P. (1984). “The protein phosphatases involved in cellular regulation. Identification of the inhibitor-2 phosphatases in rabbit skeletal muscle. “Eur. J. Biochem. 145: 65-70. PMID 6,092,084th


A phosphatase is an enzyme that removes a phosphate group from its substrate by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group (see dephosphorylation). This action is directly opposite to that of phosphorylases and kinases, which attach phosphate groups to their substrates by using energetic molecules like ATP. A common phosphatase in many organisms is alkaline phosphatase.
Protein phosphorylation is the most common and important form of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred PKs exist in mammals and are classified into distinct super-families. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 86, 12 and 2% respectively of the phosphoproteome, at least in mammals. In contrast, protein phosphatases (PPs) are the primary effectors of dephosphorylation and can be grouped into three main classes based on sequence, structure and catalytic function. The largest class of PPs is the phosphoprotein phosphatase (PPP) family comprising PP1, PP2A, PP2B, PP4, PP5, PP6 and PP7, and the protein phosphatase Mg2+- or Mn2+-dependent (PPM) family, composed primarily of PP2C. The protein Tyr phosphatase (PTP) super-family forms the second group, and the aspartate-based protein phosphatases the third.



Cysteine-dependent phosphatases (CDPs) catalyse the hydrolysis of a phosphoester bond via a phospho-cysteine intermediate.

Mechanism of Tyrosine dephosphorylation by a CDP
The free cysteine nucleophile forms a bond with the phosphorus atom of the phosphate moiety, and the P-O bond linking the phosphate group to the tyrosine is protonated, either by a suitably positioned acidic amino acid residue (Asp in the diagram below) or a water molecule. The phospho-cysteine intermediate is then hydrolysed by another water molecule, thus regenerating the active site for another dephosphorylation reaction.
Metallo-phosphatases (e.g. PP2C) co-ordinate 2 catalytically essential metal ions within their active site. There is currently some confusion of the identity of these metal ions, as successive attempts to identify them yield different answers. There is currently evidence that these metals could be Magnesium, Manganese, Iron, Zinc, or any combination thereof. It is thought that a hydroxyl ion bridging the two metal ions takes part in nucleophilic attack on the phosphorus ion.

Physiological relevance
Phosphatases act in opposition to kinases/phosphorylases, which add phosphate groups to proteins. The addition of a phosphate group may activate or de-activate an enzyme (e.g., kinase signalling pathways[7]) or enable a protein-protein interaction to occur (e.g., SH2 domains [8]); therefore phosphatases are integral to many signal transduction pathways. It should be noted that phosphate addition and removal do not necessarily correspond to enzyme activation or inhibition, and that several enzymes have separate phosphorylation sites for activating or inhibiting functional regulation. CDK, for example, can be either activated or deactivated depending on the specific amino acid residue being phosphorylated. Phosphates are important in signal transduction because they regulate the proteins to which they are attached. To reverse the regulatory effect, the phosphate is removed. This occurs on its own by hydrolysis, or is mediated by protein phosphatases.
Protein phosphorylation plays a crucial role in biological functions and controls nearly every cellular process, including metabolism, gene transcription and translation, cell-cycle progression, cytoskeletal rearrangement, protein-protein interactions, protein stability, cell movement, and apoptosis. These processes depend on the highly regulated and opposing actions of PKs and PPs, through changes in the phosphorylation of key proteins. Histone phosphorylation, along with methylation, ubiquitination, sumoylation and acetylation, also regulates access to DNA through chromatin reorganisation.
One of the major switches for neuronal activity is the activation of PKs and PPs by elevated intracellular calcium. The degree of activation of the various isoforms of PKs and PPs is controlled by their individual sensitivities to calcium. Furthermore, a wide range of specific inhibitors and targeting partners such as scaffolding, anchoring, and adaptor proteins also contribute to the control of PKs and PPs and recruit them into signalling complexes in neuronal cells. Such signalling complexes typically act to bring PKs and PPs in close proximity with target substrates and signalling molecules as well as enhance their selectivity by restricting accessibility to these substrate proteins. Phosphorylation events, therefore, are controlled not only by the balanced activity of PKs and PPs but also by their restricted localisation. Regulatory subunits and domains serve to restrict specific proteins to particular subcellular compartments and to modulate protein specificity. These regulators are essential for maintaining the coordinated action of signalling cascades, which in neuronal cells include short-term (synaptic) and long-term (nuclear) signalling. These functions are, in part, controlled by allosteric modification by secondary messengers and reversible protein phosphorylation.
It is thought that around 30% of known PPs are present in all tissues, with the rest showing some level of tissue restriction. While protein phosphorylation is a cell-wide regulatory mechanism, recent quantitative proteomics studies have shown that phosphorylation preferentially targets nuclear proteins. Many PPs that regulate nuclear events, are often enriched or exclusively present in the nucleus. In neuronal cells, PPs are present in multiple cellular compartments and play a critical role at both pre- and post-synapses, in the cytoplasm and in the nucleus where they regulate gene expression.