Complex impedance spectroscopy for monitoring tissue responses to inserted neural implants.
A series of animal experiments was conducted to characterize changes in the complex impedance of chronically implanted electrodes in neural tissue. Consistent trends in impedance changes were observed across all animals, characterized as a general increase in the measured impedance magnitude at 1 kHz. Impedance changes reach a peak approximately 7 days post-implant. Reactive responses around individual electrodes were described using immuno– and histo–chemistry and confocal microscopy.
antigenretrieve
These observations were compared to measured impedance changes. Several features of impedance changes were able to differentiate between confined and extensivehistological reactions. In general, impedance magnitude at 1 kHz was significantly increased in extensive reactions, starting about 4 days post-implant. Electrodes with extensive reactions also displayed impedance spectra with a characteristic change at high frequencies. This change was manifested in the formation of a semi-circular arc in the Nyquist space, suggestive of increased cellular density in close proximity to the electrode site. These results suggest that changes in impedance spectra are directly influenced by cellular distributions around implanted electrodes over time and that impedance measurements may provide an online assessment of cellular reactions to implanted devices.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: Mucin 6 may provide a mechanism for modulation of the composition of the protective mucus layer related to acid secretion or the presence of bacteria and noxious agents in the lumen. Plays an important role in the cytoprotection of epithelial surfaces and are used as tumor markers in a variety of cancers. May play a role in epithelial organogenesis. Highest expression seen in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. [UniProt]
Description: Mucin 6 may provide a mechanism for modulation of the composition of the protective mucus layer related to acid secretion or the presence of bacteria and noxious agents in the lumen. Plays an important role in the cytoprotection of epithelial surfaces and are used as tumor markers in a variety of cancers. May play a role in epithelial organogenesis. Highest expression seen in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. [UniProt]
Description: Mucin 6 may provide a mechanism for modulation of the composition of the protective mucus layer related to acid secretion or the presence of bacteria and noxious agents in the lumen. Plays an important role in the cytoprotection of epithelial surfaces and are used as tumor markers in a variety of cancers. May play a role in epithelial organogenesis. Highest expression seen in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. [UniProt]
Description: Mucin 6 may provide a mechanism for modulation of the composition of the protective mucus layer related to acid secretion or the presence of bacteria and noxious agents in the lumen. Plays an important role in the cytoprotection of epithelial surfaces and are used as tumor markers in a variety of cancers. May play a role in epithelial organogenesis. Highest expression seen in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. [UniProt]
Description: The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: The MUC6 gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
Description: MUC6 or gastric mucin is a secreted glycoprotein that plays an essential role in epithelial cyto-protection from acid, proteases, pathogenic microorganisms, and mechanical trauma in the gastrointestinal tract. Mucin 6 expression is highest in the stomach and gall bladder, with lower expression in the terminal ileum and right colon. In gastric cancer, Mucin 6 has an altered expression. In normal stomach, Mucin 6 is associated with Lewis type 2; Mucin 6 is also expressed in gastric metaplasia, duodenum and pancreas. Mucin 6 is a secretory mucin, located in the deeper mucosal folds of human gall bladder, and its expression is altered with increasing degrees of inflammation.
259 Patients with DCIS of the breast applying USC/Van Nuys prognostic index: a retrospective review with long term follow up.
BACKGROUND
The Van Nuys Prognostic Index (VNPI) is a simple score for predicting the risk of local recurrence (LR) in patients with Ductal Carcinoma In Situ (DCIS) conservatively treated. This score combines three independent predictors of Local Recurrence. The VNPI has recently been updated with the addition of age as a fourth parameter into the scoring system (University of Southern California/ VNPI).
METHODS
Our database consisted of 408 women with DCIS. Applying the USC/VNPI we reviewed retrospectively 259 patients who were treated with breast conserving surgery with or without radiotherapy (RT). Of these patients 63.5% had a low VNPI score, 32% intermediate and 4.5% a high score. In the low score group, the majority of the patients underwent Conservative Surgery (CS) without RT while in the intermediate group, almost half of the patients received RT. Eighty-three percent (83%) of the patients with high VNPI were treated with Conservative Surgery plus RT. Nodal assessment by Sentinel Lymph Node Biopsy was obtained in 32 patients since 2002.
RESULTS
Twenty-one Local Recurrences were observed (8%) with a mean follow up of 130 months: sixteen were invasive. No statistically significant differences in Disease Free Survival were reached in all groups of VNPI score between patients treated with Conservative Surgery or Conservative Surgery plus RT. However it was noted that the higher the VNPI score, the lower was the risk of local recurrence in the group treated additionally with RT, even though it was not statistically significant. Further analysis included those patients treated with Conservative Surgery alone and followed up. Disease-free survival (DFS) at 10 years was 94% with low VNPI and 83% in both intermediate and high score (P < 0.05). No significant differences were observed in the subgroups of VNPI.
The Local Relapse rate after Conservative Surgery alone, increased with tumor size, margin width, and pathology classification (P < 0,05), while age was not found to be a significant factor. Lesions with only mammographic appearances are associated with lower DFS but it did not reach significance (P = ns), while assumption of estrogenic hormones and familial history of breast cancer are significant factors associated with a higher risk of local recurrence. After multivariate analysis including seven clinical and pathological factors, the only significant predictors of local recurrence remained margin width of surgical excision, previous therapy with estrogens (contraceptives or Hormone Replacement Therapy) and the Van Nuys pathologic classification.
The overall survival breast cancer specific was 99% and no differences were observed between groups (P = ns). The comparison of patients treated with a total mastectomy and those conservatively treated showed a significantly better local relapse free survival rate obtained with mastectomy (98.2% vs. 89.7% at 10 years P = 0.02). However, the overall cause-specific survival did not prove any better outcome (98.7% in both groups). Of the 32 patients who underwent a Sentinel Lymph Node Biopsy, four were found to have micrometastases and all of them had a previous Directional Vacuum Assisted Biopsy.
CONCLUSIONS
Although in our series there is not a significant difference in LR rates by the parameter of age, the new USC/VNPI is still a simple and reliable scoring system for therapeutic management of DCIS. We did not find any statistically significant advantage in groups treated with the addition of RT. Obtaining wide surgical margins appears to be the strongest prognostic factor for local recurrence, regardless of other pathological factors or the addition of adjuvant radiation therapy. However, only prospective randomized studies can precisely predict the risk of LR of conservatively treated DCIS.
The clinical significance of Sentinel Lymph Nodes micrometastases Immuno–Histo–Chemistry-detected found in DCIS patients remains uncertain. However, we hypothesize that the anatomical disruption after preoperative biopsy procedures increases the likelihood of epithelial cell displacement and the frequency of IHC-positive Sentinel Lymph Nodes, both of which are directly proportional to the degree of manipulation.
Tissue biodistribution of intravenously administrated titanium dioxide nanoparticles revealed blood-brain barrier clearance and brain inflammation in rat.
BACKGROUND
Notwithstanding increasing knowledge of titanium dioxide nanoparticles (TiO2 NPs) passing through biological barriers, their biodistribution to the central nervous system (CNS) and potential effects on blood-brain barrier (BBB) physiology remain poorly characterized.
METHODS
Here, we report time-related responses from single-dose intravenous (IV) administration of 1 mg/kg TiO2 NPs to rats, with particular emphasis on titanium (Ti) quantification in the brain. Ti content in tissues was analyzed using inductively coupled plasma mass spectrometry. Integrity and functionality of the BBB as well as brain inflammation were characterized using a panel of methods including RT-PCR, immuno–histochemistry and transporter activity evaluation.
RESULTS
Biokinetic analysis revealed Ti biopersistence in liver, lungs and spleen up to one year after TiO2 NPs administration. A significant increase of Ti in the brain was observed at early end points followed by a subsequent decrease. In-depth analysis of Ti in the total brain demonstrated quantitative Ti uptake and clearance by brain microvasculature endothelial cells (BECs) with minimal translocation in the brain parenchyma. The presence of Ti in the BECs did not affect BBB integrity, despite rapid reversible modulation of breast cancer resistance protein activity.
Ti biopersistence in organs such as liver was associated with significant increases of tight junction proteins (claudin-5 and occludin), interleukin 1β (IL-1β), chemokine ligand 1 (CXCL1) and γ inducible protein-10 (IP-10/CXCL10) in BECs and also increased levels of IL-1β in brain parenchyma despite lack of evidence of Ti in the brain. These findings mentioned suggest potential effect of Ti present at a distance from the brain possibly via mediators transported by blood. Exposure of an in vitro BBB model to sera from TiO2 NPs-treated animals confirmed the tightness of the BBB and inflammatory responses.
CONCLUSIONS
Overall, these findings suggest the clearance of TiO2 NPs at the BBB with persistent brain inflammation and underscore the role of Ti biopersistence in organs that can exert indirect effects on the CNS dependent on circulating factors.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Nestin (NES) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Nestin (NES) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Nestin (NES) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Nestin (NES) in tissue homogenates, cell lysates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Nestin (NES) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Nestin (NES) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Nestin (NES) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Nestin (NES) in tissue homogenates, cell lysates and other biological fluids.
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Nestin (NES) in tissue homogenates, cell lysates and other biological fluids.
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Nestin (NES) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species.
Description: Nestin is a class VI intermediate filament protein expressed predominantly in stem cells of the neural tube but absent from virtually all differentiated CNS cells. In the CNS, nestin is downregulated upon differentiation and replaced by neurofilaments. Transient expression of nestin has been postulated as a key step committing cells to the neural differentiation pathway. Nestin expression has also been observed in pancreatic hematopoietic stem cell populations.
Description: Nestin is a class VI intermediate filament protein expressed predominantly in stem cells of the neural tube but absent from virtually all differentiated CNS cells. In the CNS, nestin is downregulated upon differentiation and replaced by neurofilaments. Transient expression of nestin has been postulated as a key step committing cells to the neural differentiation pathway. Nestin expression has also been observed in pancreatic hematopoietic stem cell populations.
Description: Nestin is a class VI intermediate filament protein expressed predominantly in stem cells of the neural tube but absent from virtually all differentiated CNS cells. In the CNS, nestin is downregulated upon differentiation and replaced by neurofilaments. Transient expression of nestin has been postulated as a key step committing cells to the neural differentiation pathway. Nestin expression has also been observed in pancreatic hematopoietic stem cell populations.
Description: Nestin is a type VI intermediate filament (IF) protein that in humans is encoded by the NES gene. Distribution and expression of nestin in mitotically active cells suggests it plays a role in regulation of the assembly and disassembly of intermediate filaments, which, together with other structural proteins, participate in remodeling of the cell. The role of nestin in dynamic cells, particularly structural organization of the cell, appears strictly regulated by phosphorylation, especially its integration into heterogeneous intermediate filaments together with vimentin or α-internexin. Furthermore, nestin expression has been extensively used as a marker for central nervous system (CNS) progenitor cells in different contexts, based on observations indicating a correlation between nestin expression and this cell type in vivo.
Description: Nestin is a major intermediate filament (IF) protein of embryonic central nervous system progenitor cells. It is also a component of the dynamic IF network during muscle development, where it polymerizes with Desmin and Vimentin. Nestin co-assembles with Vimentin or -internexin and forms heterodimer coiled-coil molecules which then further assemble into 10 nml IFs. Deletion of the IF consensus rod domain in nestin alters nestin localization in CNS precursor cells and radial glial cells in vivo. Nestin is a marker for neuroepithelial stem cells, glioma cells and tumor endothelial cells during rapid growth. During axon elongation of differentiation neurons, nestin localizes to the growth cones and may play a role in growth cone guidance. In the rat adrenal gland, nestin is expressed by the zona fasciculata and the zona reticularis. Nestin is also expressed by dermatomal cells and by myoblasts during the earliest stages of myogenesis.
Description: Nestin is a major intermediate filament (IF) protein of embryonic central nervous system progenitor cells. It is also a component of the dynamic IF network during muscle development, where it polymerizes with Desmin and Vimentin. Nestin co-assembles with Vimentin or -internexin and forms heterodimer coiled-coil molecules which then further assemble into 10 nml IFs. Deletion of the IF consensus rod domain in nestin alters nestin localization in CNS precursor cells and radial glial cells in vivo. Nestin is a marker for neuroepithelial stem cells, glioma cells and tumor endothelial cells during rapid growth. During axon elongation of differentiation neurons, nestin localizes to the growth cones and may play a role in growth cone guidance. In the rat adrenal gland, nestin is expressed by the zona fasciculata and the zona reticularis. Nestin is also expressed by dermatomal cells and by myoblasts during the earliest stages of myogenesis.
Description: Nestin is a major intermediate filament (IF) protein of embryonic central nervous system progenitor cells. It is also a component of the dynamic IF network during muscle development, where it polymerizes with Desmin and Vimentin. Nestin co-assembles with Vimentin or -internexin and forms heterodimer coiled-coil molecules which then further assemble into 10 nml IFs. Deletion of the IF consensus rod domain in nestin alters nestin localization in CNS precursor cells and radial glial cells in vivo. Nestin is a marker for neuroepithelial stem cells, glioma cells and tumor endothelial cells during rapid growth. During axon elongation of differentiation neurons, nestin localizes to the growth cones and may play a role in growth cone guidance. In the rat adrenal gland, nestin is expressed by the zona fasciculata and the zona reticularis. Nestin is also expressed by dermatomal cells and by myoblasts during the earliest stages of myogenesis.
Description: A competitive ELISA for quantitative measurement of Rat Nestin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Description: A competitive ELISA for quantitative measurement of Rat Nestin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
 (9-13M1) Antibody)
 (2-11M1) Antibody)
 (1-13M1) Antibody)
 (MUC6/1553R) Antibody)
)
 ELISA Kit)
 ELISA Kit)
 Polyclonal Antibody (Rat))
 Polyclonal Antibody (Human))
 Polyclonal Antibody (Mouse))
 Polyclonal Antibody (Rat), PE)
 Polyclonal Antibody (Rat), APC)
 Polyclonal Antibody (Rat), Cy3)
 Polyclonal Antibody (Rat), HRP)
 Polyclonal Antibody (Human), PE)
 Polyclonal Antibody (Mouse), PE)
 Polyclonal Antibody (Rat), FITC)
 Monoclonal Antibody (Human, Rat))
 Polyclonal Antibody (Human), APC)
 Polyclonal Antibody (Human), Cy3)
 Polyclonal Antibody (Human), HRP)
 Polyclonal Antibody (Mouse), APC)
 Polyclonal Antibody (Mouse), Cy3)
 Polyclonal Antibody (Mouse), HRP)
 Polyclonal Antibody (Human), FITC)
 Polyclonal Antibody (Mouse), FITC)
 Monoclonal Antibody (Human, Rat), PE)
 Polyclonal Antibody (Rat), Biotinylated)
 Monoclonal Antibody (Human, Rat), APC)
 Monoclonal Antibody (Human, Rat), Cy3)
 Monoclonal Antibody (Human, Rat), HRP)
 Polyclonal Antibody (Rat), APC-Cy7)
 Monoclonal Antibody (Human, Rat), FITC)
 Polyclonal Antibody (Human), Biotinylated)
 Polyclonal Antibody (Mouse), Biotinylated)
 Polyclonal Antibody (Human), APC-Cy7)
 Polyclonal Antibody (Mouse), APC-Cy7)
 Monoclonal Antibody (Human, Rat), APC-Cy7)
 Monoclonal Antibody (Human, Rat), Biotinylated)
 Antibody)
 Antibody)
