This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
Facts about Slit homolog 2 protein.
SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as gruesome signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal chord development may play a role in guiding commissural axons when they reached the floor plate by modulating the response to netrin.
Human | |
---|---|
Gene Name: | SLIT2 |
Uniprot: | O94813 |
Entrez: | 9353 |
Belongs to: |
---|
No superfamily |
FLJ14420; SLIL3; slit (Drosophila) homolog 2; slit homolog 2 (Drosophila); slit homolog 2 protein; Slit2; Slit-2SLIL3
Mass (kDA):
169.87 kDA
Human | |
---|---|
Location: | 4p15.31 |
Sequence: | 4; NC_000004.12 (20251905..20620561) |
Fetal lung and kidney, and adult spinal cord. Weak expression in adult adrenal gland, thyroid, trachea and other tissues examined.
Secreted. The C-terminal cleavage protein is more diffusible than the larger N-terminal protein that is more tightly cell associated.
There are many ways to optimize your experiments with the Boster Bio SLIT2 Marker. For best results, you should refer to the Boster Bio User Guide. There are many flow methods to consider. Check out our optimization tips to get the most from your experiment. You can also find guides and FAQs that will help you optimize your experiment.
There are numerous applications for SLIT2, and this article will highlight a few of them. This gene is expressed by the liver ductular structure and could be used as a therapeutic target for liver wound healing. Endothelial cells that develop near the periportal areas also express SLIT2. Although it is not expressed by endothelial cells in the portal vein and hepatic artery, it is known to interact with ROBO1 receptors in neo-vessels.
SLIT2 can be described as a receptor or gene that regulates a multitude of processes in the body. This gene has been linked with ROBO1 and several other cancers, including head- and neck tumors. SLIT2 was previously reported to be inactivated in some tumors, and this gene is also a significant risk factor for poor patient outcomes.
SLIT2 has been proven to inhibit macropinocytosis within RAS-transformed cells. This cellular adaptation ensures that tumors cells have sufficient amino acid. The SLIT2 protein is found in the DLD-1 cells and is associated to poor prognosis. SLIT2 is expressed on both cell lines. It inhibits macropinocytosis as well as directed migration.
Recent studies also reveal the complex signaling pathways involved with KRAS transformed cells. KRAS-transformed PDAC cell use macropinocytosis to uptake protein in the nutrient-deficient tumor environment. This is a very interesting study as it demonstrated that SLIT2 expression was able to significantly reduce primary tumor size and secondary neuroinvasive in vivo.
SLIT2 can also affect NFkB signaling. These cells might have a higher activity of SLIT2 than NOD2 under inflammatory conditions. Further research is needed before SLIT2 can prove to be of therapeutic value. The current study suggests that it could be used as a therapy for inflammation conditions that involve hyperactivation NOD2 signaling.
In addition to its potential as a therapeutic target, SLIT2 has a significant association with HNSCC. These findings suggest that a greater understanding of the role of SLIT2 in these tumors may improve the chances of treatment. It is important to thoroughly study ROBO1 and SLIT2 in order to determine the key targets for HNSCC and develop therapeutic strategies. This pathway has been associated with the development of numerous types of cancer, including melanoma, prostate and kidney.
It is important to select an antibody with high affinity and specificity when searching for an antibody against VEGF or SLIT2. Boster Bio's robust portfolio of high affinity and specificity antibodies, ELISA kits, and ELISA kits has been transparently validated for use across a range of applications including Flow Cytometry. Boster Bio provides excellent customer service and is committed towards continuous improvement and product expansion.
EphA2-deficient endothelial tissues have elevated levels of SLIT2 expression. Inhibiting Slit activity can restore VEGF-mediated giogenesis in vivo. Slit2 expression inhibits tumorangiogenesis and restores normal activity for Src/Rac. These factors regulate endothelial cell growth and function.
Slit2N prevents L-LEC migration and proliferation. It is also a key regulator for tube formation. It modulates signaling by VEGF C, and VEGFR-3. This is consistent in the fact that LECs incubated with SLIT2N showed decreased VEGF–C-induced lymphangiogenesis.
We used a transwell migration test with a 6.5mm pore filter to evaluate the role of SLIT2 for vascular development. To determine the length of each tube within each field, we used "UTHSCSA ImagingTool" software. The data are the average tube length (+SD), from 3 wells for each condition, with 5 fields per condition.
L-LECs express the protein Slit2N, which inhibits VEGF C-induced activation Akt. L-LECs are more likely to express SLIT2N than other types of cells. Robo4-expressing cell activity is also inhibited by Slit2N. The results of these experiments show that L-LECs secrete Slit2N.
The cellular distributions for Slit2 were determined in inner nuclear layers, ganglion cells layers, nerve fibre layers, and the inner segment of photoreceptor levels. Similar patterns of Robo1 & SLIT2 were observed in the control groups. They were similar to those seen after a month. Positive staining began in the inner layer of the plexiform, inner segment of photoreceptors, then spread to the outer layer.
Slit2 and Robo1 mRNA expressions in vitreous tissues revealed that patients with DR had significantly higher levels than those in the control group. However, there was no significant difference between the two groups. Slit2 was also significantly higher in the FVMs from PDR patients compared to the DR. This suggests that Robo1 might play a significant role in the treatment and prevention of PDR.
This mouse model of NF-kB signaling is a powerful tool for examining the biological functions of the p50 subunit. Although p50 has no intrinsic ability to activate transcription, it is thought to recruit the coactivator Bcl-3. Interestingly, this molecule is phosphorylated and its activity is partially inhibited. This could mean that it may also inhibit neutrophil recruitment.
NF-kB 'p-p50' is a partially processed version of the precursor p105. This protein is thought be a cotranslational product from partially synthesized molecules by proteasome. It is generated in an ubiquitin-independent manner when fully synthesized p105 is degraded by the 20S proteasome. This can occur in wildtype p105, provided that the C-terminus has at least 25 residues. In vivo mutants without the complete ankyrin repeat domain can be processed incorrectly.
The orchestration of cellular processes is facilitated by NF-kB dimers. Five members of this family are important. NF-kB-p50, the most significant, performs a wide range cellular functions. It is synthesized from p105, then processed by the proteasome for the production of the p50/p52 units.
NFkB serves many functions in our nervous system, including mediating cell death. In particular, it promotes synaptic transmission, learning, and memory. Glutamate growth factors and synaptic transmissio are examples of activators for NF-kB. When phosphorylated, NF-kb dimers can activate transcription of various genes. However, this does in no way guarantee an anti-apoptotic effect.
The Boster Bio Anti-NF-kB p-p50 antibody is part of the Picoband(tm) catalog and reacts with Rat and Human. It contains 5 mg BSA and the recombinant prot. This antibody is a great choice as a research tool for scientists. It's easy to use, and a valuable tool for confirming whether or not it activates NF-kB signaling in cells.
This refolded proteins was loaded onto a Superdex200 gel filtration column under native conditions. The Boster BioNFKB p-50 purified GST-tagged p105 p105 proteins. Glutathione Sepharose 4B columns were used to purify GST-tagged proteins. The purified P50RHR protein is then transferred to SDS/PAGE as a two-ton.
The Slit2 gene carries more than 90% homology among species, including humans. Slit2 expression in the human body is effective, but binding to Robo Receptors is non-selective in vertebrate species. It is therefore an attractive candidate for clinical research in a variety heterogeneous diseases. Slit2 is important for controlling cell growth.
The Slit2 marker prevents platelet adhesion, proliferation, and thrombus formation. It may also inhibit the inflammatory process in blood vessels, which can ultimately lead to occlusion of diseased vessels. Further research is needed to understand the role of Slit2 within the vascular system. Here are some of the best uses for it:
Slit2 acts to regulate new vessel formation. It also interacts with Robo1 and Robo4 proteins. It has also been implicated in cancer, ischemic diseases, and intrahepatic angiogenesis. Slit2 also is upregulated by CDE and DDC cell lines and at similar levels with epitin 19.
Slit2 overexpression is also protective against spatial learning deficits following MI induction. Animal models also show the effects of Slit2 on the brain. It is also associated with better BBB integrity. By decreasing neuroinflammation, stroke severity can be reduced by increasing glymphatic clearance. Slit2 also has protective effects in other areas of our bodies.
In a mouse model of renal fibrosis, Slit2 was found to reduce its progression. It also decreased the risk of developing fibrosis left kidney injury. N-Slit2 reduced blood creatinine (urea) levels in the study. This study suggests that N -Slit2 may be of therapeutic value in chronic kidney injury.
An immunohistochemical staining procedure in mouse kidney tissue is used to analyze the expression of Slit2. This was done using an ELISA kit from cusabio biotech Co. Afterwards, the Slit2 levels were calculated. We can then compare the expression of Slit2 across different tissues. We also compare the mean levels of Slit2 in different groups.
PMID: 9813312 by Itoh A., et al. Cloning and expressions of three mammalian homologues of Drosophila slit suggest possible roles for Slit in the formation and maintenance of the nervous system.
PMID: 10349621 by Holmes G.P., et al. Distinct but overlapping expression patterns of two vertebrate slit homologs implies functional roles in CNS development and organogenesis.