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A KCC2 agonist restores stepping ability in paralyzed mice

Posted by star on 2018-08-27 19:19:22
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On July 19,Cell published Reactivation of Dormant Relay Pathways in Injured Spinal Cord by KCC2 Manipulations. The studies have shown that when administered systemically, a small molecule compound activates these neural circuits in paralyzed mice, thereby restoring their ability to walk.

The researchers injected the CLP290 compound intraperitoneally into paralyzed mice with spinal cord injuries. Each group of mice received treatment for 8 to 10 weeks. The results showed that the paralyzed mice restores stepping ability after four to five weeks of treatment. Electromyography recordings showed that the two groups of related hind limb muscles actively moved in the paralyzed mice. After two weeks of stopping treatment, the walking scores of these mice were still higher than those of the control group.

These neurons produced a significant decrease in KCC2 after spinal cord injury. CLP290 is capable of activating the KCC2 protein in the cell membrane, enabling inhibitory neurons to again receive inhibitory signals from the brain. This causes the spinal circuit to turn to excitation, making it more sensitive to input signals from the brain. This has the effect of reviving the spinal cord circuit that loses its function due to spinal cord injury. A KCC2 agonist restores stepping ability in paralyzed mice and can be combined with epidural electrical stimulation to maximize the patient's function after suffering from spinal cord injury.

Wuhan EIAab Science Co., Ltd has developed KCC2 protein, antibody and ELISA kit. Welcome scientific research workers to choose and purchase.



STAT3 inhibitors can treat tumor brain metastasis

Posted by star on 2018-08-27 01:40:09
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On June 11, a study published STAT3 labels a subpopulation of reactive astrocytes required for brain metastasis in Nature Medicine showed that there is a subpopulation of reactive astrocytes expressing STAT3 in the brain, which can accelerate brain metastasis of tumor cells. The study also found that the STAT3 inhibitor has a good anti-tumor effect and does not cause any adverse effects. This treatment is also effective for brain metastasis of any type of cancer, regardless of the primary tumor that produced it.

It is estimated that 10%-40% of primary tumors will metastasize in the brain, which makes the patient's prognosis significantly worse. Little progress has been made in the treatment, and current brain metastases still rely on surgery and/or radiation therapy. In recent years, there have been some alternatives in targeted therapy or immunotherapy, but in the best case, the percentage of patients who may benefit from these treatments is only 20%.

After good results in blocking STAT3signaling in mice by using silibinin, the authors established 18 studies of patients with lung cancer with brain metastases, which combined the use of this drug with standard treatment. Seventy-five percent of patients were positive for brain metastases. Three patients (20%) showed complete response and 10 (55%) responded partially. The mean survival rate was 15.5 months, while the control group was 4 months.

This treatment focuses on the brain environment that has been metastasized, a new concept of treatment that addresses changes that occur only when the brain is metastasized, and that these changes are necessary for survival.

Wuhan EIAab Science Co., Ltd has developed STAT3 protein, antibody and ELISA kit.

Welcome scientific research workers to choose and purchase.



DNA polymerase III holoenzyme

Posted by star on 2018-08-27 01:37:03
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We now consider DNA polymerase III holoenzyme, the bacterial replication machine, in greater detail. The first clue to this enzyme's existence came in 1969 when Paula Delucia and John cairns isolated an E. coli mutant that lacked DNA polymerase I activity but continued to synthesize DNA and grow normally. This mutant was considered to be very remarkable at the time of its discovery because investigators had assumed that DNA polymerase I was the only polymerase required for DNA synthesis. The possibility that the mutant might have a low level of DNA polymerase I activity that allowed it to synthesize DNA was ruled out when an E. coli mutant with a deletion in polA (the structural gene for DNA polymerase I) was shown to also synthesize DNA.

The most likely explanation for the polA mutant is ability to synthesize DNA is that some other DNA polymerase is present and that enzyme is responsible for DNA synthesis. In support of this hypothesis, two new enzymes-DNA polymerase II and DNA polymerase Ⅲ-were detected in polA mutant extracts when gapped DNA (created by partial hydrolysis of nicked DNA with an exonuclease) was used as a template. The two new polymerases add nucleotides to the 3'-end of the primer chain in the order specified by the template chain, Neither enzyme had been detected in bacterial extracts before because DNA polymerase I is so active that it masks their activity.

The next task was to determine what role, if any the new DNA polymerases play in DNA replication. Once again, a genetic approach helped to provide the answer Mutants lacking DNA polymerase ∏ synthesize DNA normally indicating that this enzyme is not essential for bacterial DNA replication. In contrast, temperature-sensitive DNA polymerase III mutants replicate DNA at 30 ° C but not at 42 ° C, indicating that DNA polymerase Ⅲ is required for bacterial DNA synthesis.

Although genetic studies indicated that DNA polymerase Ⅲ plays an essential role in bacte......

Several enzymes act together at the replication fork

Posted by star on 2018-08-24 01:29:24
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DNA elongation is a complex process involving cooperative interactions among many different proteins. These proteins synthesize two new DNA chains at an astonishing rate. Tania Baker and Stephen Bell provide the following insightful analogy to illustrate the astonishing job that the E.coli replication enzymes perform while synthesizing DNA. They begin by changing the scale so that the DNA duplex is 1 m in diameter. At this scale, the replication fork would move at about 600 km/h (375 mph) and the replication machinery would be about the size of a FedEx® delivery truck.

Baker and Bell's analogy underscores the enormous complexity and incredible speed of the DNA replication process. DNA polymefase Ⅲ holoenzyme, the bacterial counterpart of the FedEx delivery truck, acts as the replication machine. It extends the leading strand by continuous nucleotide attachment to the 3'-hydroxy terminus, while helping to form the lagging strand by extending the primer until the resulting Okazaki fragment reaches the 5'-end of the adjacent fragment. Although DNA polymerase Ⅲ holoenzyme is a remarkable replication machine, it does not act alone. Several additional proteins assist in DNA synthesis at the replication fork. These events, which are summarized, are as follows:

1. DnaB, a homohexameric helicase, use energy supplied by ATP hydrolysis to unwind double-stranded DNA as the helicase moves 5'→3'along the lagging template strand. Unwinding at the replication fork leads to tighter winding ahead of the replication fork because the bacterial chromosome is a double-stranded circular DNA molecule. Helicase also activates RNA primase (see below) to make the RNA primers.

2. DNA gyrase and topoisomerase I  act cooperatively to relieve the resulting torsional strain, allowing the replication fork to continue moving along the bacterial chromosome.

3. Single-stranded binding protein (SSB) coats......

Experimental Steps of Plasmid DNA Extration

Posted by star on 2018-08-23 18:52:50
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1. Isolate a single colony from a freshly streaked selective plate, and inoculate a culture of 5mL LB medium containing the appropriate selective antibiotic. Incubate for12~16 hours at 37℃ with vigorous shaking(180rpm). Centrifuge at 13,000 x g for 1 minute at room temperature.

2. Add 250μL Solution I, vortex or pipet up down to mix thoroughly.

3. Add 250μL Solution II, invert and gently rotate the tube several times to obtain a clear lysate. A 2-3 minute incubation may be necessary.

4. Add 350μL Solution III, immediately invert several times until a flocculent white precipitate forms I.

5. Centrifuge at maximum speed(13,000 x g) for 10 minutes. A compact white pellet will form. Promptly proceed to the next step. Insert a HiBind DNA Mini Column into a 2mL Collection Tub.

6. Transfer the cleared supernatant from Step 5 by carefully aspirating it into the HiBind DNA Mini Column. Be careful not to disturb the pellet and that no cellular debris is transferred to the HiBind DNA Mini Column. Centrifuge at maximum speed for 1 minute. Discard the filtrate and reuse the collection tube.

7. Add 500μL HBC Buffer.Centrifuge at maximum speed for 1 minute. Discard the filtrate and reuse collection tube.

8. Add 700μL DNA Wash Buffer. Centrifuge at maximum speed for 1 minute. Discard the filtrate and reuse the collection tube.

9. Centrifuge the empty HiBind DNA Mini Column for 2 minutes at maximum speed to dry the column matrix.

10. Transfer the HiBind DNA Mini Column to a clean 1.5mL microcentrifuge tube. Add 30μL Elution Buffer or sterile deionized water directly to the center of the column membrane.

11. Store DNA at -20°C.



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