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Py 3-FITC: a new fluorescent probe for live cell imaging of collagen-rich tissues and ionocytes

Polypyrrole-based polyamides are used as sequence-specific DNA probes. Nonetheless, their mobile uptake and distribution are affected by a number of elements and haven’t been extensively studied in vivo. Right here, we generated a collection of fluorescence-conjugated polypyrrole compounds and examined their mobile distribution utilizing reside zebrafish and cultured human cells. Among the many evaluated compounds, Py3-FITC was capable of visualize collagen-rich tissues, such because the jaw cartilage, opercle and bulbus arteriosus, in early-stage residing zebrafish embryos.
Then, we stained cultured human cells with Py3-FITC and located that the staining grew to become extra intense as the quantity of collagen was elevated. As well as, Py3-FITC-stained HR cells, which characterize a kind of ionocyte on the physique floor of residing zebrafish embryos.
Py3-FITC has low toxicity, and collagen-rich tissues and ionocytes may be visualized when soaked in Py3-FITC answer. Due to this fact, Py3-FITC could also be a helpful reside imaging instrument for detecting modifications in collagen-rich tissue and ionocytes, together with their mammalian analogues, throughout each regular growth and illness development.

Gentle Sheet Microscopy Utilizing FITC-Albumin Adopted by Immunohistochemistry of the Identical Rehydrated Brains Reveals Ischemic Mind Damage and Early Microvascular Reworking

Till just lately, the visualization of cerebral microvessels was hampered by the truth that solely brief segments of vessels may very well be evaluated in mind sections by histochemistry. These limitations have been overcome by gentle sheet microscopy, which permits the 3D evaluation of microvasculature in cleared brains. A serious limitation of sunshine sheet microscopy is that antibodies don’t sufficiently penetrate cleared brains.
We herein describe a way of reverse clearing and rehydration, which after microvascular community evaluation permits mind sectioning and immunohistochemistry using a broad set of antibodies. Performing gentle sheet microscopy on brains of mice uncovered to intraluminal center cerebral artery occlusion (MCAO), we present that within the early part of microvascular transforming branching level density was markedly lowered, extra strongly than microvascular size.
Mind infarcts in gentle sheet microscopy have been sharply demarcated by their autofluorescence sign, carefully comparable to mind infarcts revealed by Nissl staining. Neuronal survival, leukocyte infiltration, and astrocytic reactivity may very well be evaluated by immunohistochemistry in rehydrated brains, as proven in direct comparisons with non-cleared brains. Immunohistochemistry revealed microthrombi in ischemic microvessels that have been probably liable for the marked branching level loss. The steadiness between microvascular thrombosis and transforming warrants additional research at later time-points after stroke.

Hyaluronic acid and poly-L-lysine layers on calcium alginate microspheres to modulate the discharge of encapsulated FITC-dextran

Alginate options crosslink into microspheres in calcium alginate, enabling the encapsulation and subsequent launch of organic macromolecules and medicines. Nonetheless, launch from calcium alginate into PBS is comparatively quick as a result of it would decrosslink the gel comparatively rapidly. On this analysis, FITC-dextran (MW 10 kDa) was encapsulated in 2% (w/v) calcium alginate microspheres by electrospraying.
The ensuing microspheres (diameter = 247 ± 13 μm) have been then layered with skinny polyelectrolyte movies of hyaluronic acid (HA) and poly-L-lysine (PLL) to aim to gradual the diffusion of FITC-dextran out of the microspheres and the coating parameters have been modified to modulate diffusion and launch.
Growing the focus of FITC-dextran encapsulated within the microspheres resulted in a rise in its launch over time into PBS. Crosslinking PLL/HA layers on the microspheres didn’t lower the in vitro launch charges of encapsulated FITC-dextran into PBS. Growing the variety of layers on the microspheres from Three to five layers considerably decreased the quantity of encapsulated FITC-dextran launched.
Nonetheless, rising the variety of layers to 7 layers didn’t additional maintain the discharge of FITC-dextran, probably as a result of these microspheres collapsed to a smaller measurement through the coating process, leading to launch managed by each diffusion and swelling. A number of layers of PLL and HA supplied a strong mechanism to maintain and management launch of enormous molecules from calcium alginate.

Transdermal supply of FITC-Dextrans with totally different molecular weights utilizing radiofrequency microporation

Background: Transdermal supply is of nice significance for the efficient supply of bioactive or therapeutic brokers right into a physique. The microporation machine based mostly on radiofrequency can be utilized to boost supply effectivity by eradicating the dermis layer.
Strategies: The micropores have been developed on pig pores and skin and human cadaver pores and skin with dermal and epidermal layers by the microporation machine. The regeneration of micropores within the human cadaver pores and skin attributable to microporation was confirmed utilizing an optical microscope and haematoxylin/eosin (H&E) staining.
The permeability of fluorescein isothiocyanate-dextrans (FITC-dextrans) with totally different molecular weights by way of the pig and human cadaver skins have been measured utilizing Franz diffusion cell.
Outcomes: The optical picture and histological evaluation confirmed that the micropores on the pores and skin have been recovered over time. The improved permeability by way of micropores was confirmed by Franz diffusion cell. The decrease molecular weight of FITC-dextran permeated extra on each human and pig pores and skin. As well as, the permeation fee was increased in pig pores and skin than in human pores and skin.
teitell-lab
teitell-lab

DNA-crosslinked alginate and layered microspheres to modulate the discharge of encapsulated FITC-dextran

Alginate may be gently crosslinked by calcium into hydrogels and microspheres for the encapsulation and launch of proteins and medicines. Nonetheless, the discharge is commonly over brief durations except alginate can be covalently modified or crosslinked. This analysis goals to maintain the discharge of encapsulated mannequin drug FITC-dextran by covalently crosslinking alginate with brief oligomers DNA as a result of proof means that DNA can also work together with alginate to additional enhance efficient crosslinking. Moreover, modulating the discharge of medicine from alginate in response to particular proteins might tailor launch profiles to enhance affected person remedy.
  • This analysis develops a DNA-crosslinked alginate hydrogel and layered alginate microspheres to encapsulate after which maintain the discharge FITC-dextran (mannequin drug). An aptamer sequence to hen egg-white lysozyme is included in a single DNA strand to permit for the disruption of the crosslinks by interactions with human lysozyme.
  • Alginate was covalently modified with complementary strands of DNA to crosslink the alginate into hydrogels, which had elevated crosslinking density when re-swollen (compared to controls crosslinked with PEG) and will sustained the discharge of encapsulated FITC-dextran.
  • When an aptamer sequence for hen lysozyme was included within the DNA crosslinks, the hydrogels decrosslinked when incubated in human lysozyme for 60 days. As well as, calcium alginate microspheres have been coated with Three alternating layers of poly-Lysine, DNA-crosslinked alginate, and poly-L-lysine.
  • FITC-dextran loaded into the microspheres launched in a sustained method previous 30 days (into PBS at 37°C) and would probably proceed to launch for a lot longer had the research continued. When incubated with Three μM of human lysozyme, a burst launch of FITC-dextran happens from each the hydrogels and microspheres, with no modifications within the controls.
  • The elevated launch was in bursts adopted by related sustained launch charges suggesting that the human lysozyme quickly disrupted the DNA crosslinks which have been then re-established or have been influenced by interactions between DNA and alginate.
  • Importantly, covalently certain complementary strands of DNA might crosslink the alginate and extra interactions appeared to additional maintain the discharge of encapsulated therapeutics.

MOUSE ANTI HUMAN PODOPLANIN

MBS212743-01mg 0.1mg
EUR 450

MOUSE ANTI HUMAN PODOPLANIN

MBS212743-5x01mg 5x0.1mg
EUR 1840

Mouse anti Podoplanin (human)

101-M40 100ug
EUR 297.6

Anti- Podoplanin Human Antibody

GWB-F131C7 0.2 mg Ask for price

Mouse anti Podoplanin-Biotin (human)

101-MBi40 50ug
EUR 297.6

Podoplanin Human, Antibody

GWB-9FF8E1 0.1 mg Ask for price

Mouse Anti Human Podoplanin clone P56F7AT

MBS146676-0005mg 0.005mg
EUR 240

Mouse Anti Human Podoplanin clone P56F7AT

MBS146676-002mg 0.02mg
EUR 310

Mouse Anti Human Podoplanin clone P56F7AT

MBS146676-01mg 0.1mg
EUR 610

Mouse Anti Human Podoplanin clone P56F7AT

MBS146676-5x01mg 5x0.1mg
EUR 2405

Mouse Anti-Human Podoplanin

MBS690117-0025mg 0.025mg
EUR 310

Mouse Anti-Human Podoplanin

MBS690117-5x0025mg 5x0.025mg
EUR 1110

Mouse Anti-Human Podoplanin

MBS690586-01mg 0.1mg
EUR 450

Mouse Anti-Human Podoplanin

MBS690586-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human Podoplanin

MBS690680-0025mg 0.025mg
EUR 310

Mouse Anti-Human Podoplanin

MBS690680-5x0025mg 5x0.025mg
EUR 1110

Mouse Anti-Human Podoplanin

MBS690759-01mg 0.1mg
EUR 450

Mouse Anti-Human Podoplanin

MBS690759-5x01mg 5x0.1mg
EUR 1725

Mouse Anti-Human Podoplanin

MBS690992-005mg 0.05mg
EUR 430

Mouse Anti-Human Podoplanin

MBS690992-5x005mg 5x0.05mg
EUR 1645

Mouse Anti-Human Podoplanin

MBS692357-005mg 0.05mg
EUR 450

Mouse Anti-Human Podoplanin

MBS692357-5x005mg 5x0.05mg
EUR 1725

Mouse Anti-Human Podoplanin

MBS692358-005mg 0.05mg
EUR 450

Mouse Anti-Human Podoplanin

MBS692358-5x005mg 5x0.05mg
EUR 1725

Rabbit Anti-Human Podoplanin

102-PA40 100ug
EUR 240

Anti-Human Podoplanin Antibody

101-M40-FITC 50 µg Ask for price
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody

101-M40-PE 50 µg Ask for price
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody

101-M40S-FITC 25 µg Ask for price
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody

101-M40S-PE 25 µg Ask for price
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody

101-M41 100 µg
EUR 199.5
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207-228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential O-linked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for C-type lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on O-glycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody

102-PA40AG 50 µg
EUR 147
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207-228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential Olinked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver (1). Podoplanin is the ligand for Ctype lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on Oglycans of Podoplanin. Through its association with CLEC2, Podoplanin induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Anti-Human Podoplanin Antibody

102-PA40S 100 µg
EUR 126
Description: Podoplanin, also known as glycoprotein 36 (gp36), PA2.26 antigen, T1alpha (T1A), and aggrus, is a 36 kDa type I transmembrane sialoglycoprotein and member of the Podoplanin family. Podoplanin has three potential splice variants, the longest of which is represented by a 238 amino acid (aa) precursor (NP_006465). It contains an undefined signal sequence, a 22 aa transmembrane segment (aa 207-228) and a short cytoplasmic tail (aa 229-238). The ECD contains abundant Ser/Thr residues that could serve as potential O-linked glycosolation sites. The cytoplasmic tail contains putative sites for protein kinase C phosphorylation. There are two potential alternate start sites at Met 77 (Swiss Prot #: Q86YL7) and Met 119 (EAW51692) that generate short forms. The 162 aa short form Podoplanin precursor shares 47% aa identity with mouse Podoplanin. Podoplanin is expressed on glomerular epithelial cells (podocytes), type I lung alveolar cells, lymphatic endothelial cells, and numerous tumors, including colorectal tumors, squamous cell carcinomas, testicular seminoma, and brain tumors. One study shows high expression of Podoplanin mRNA in placenta, lung, skeletal muscle, and heart, and weaker levels in brain, kidney, and liver. Podoplanin is the ligand for C-type lectin-like receptor 2 (CLEC2). Their association is dependent on sialic acid on O-glycans of Podoplanin. Through its association with CLEC2, Podoplanin-induces platelet aggregation and tumor metastasis. Podoplanin is also necessary for lymphatic vessel formation, normal lung cell proliferation and alveolus formation at birth.

Human Podoplanin, soluble

MBS691538-0005mg 0.005mg
EUR 250

Human Podoplanin, soluble

MBS691538-5x0005mg 5x0.005mg
EUR 835

anti- Podoplanin antibody

FNab06598 100µg
EUR 702
Description: Antibody raised against Podoplanin
Frank Rivera