Search results for: Rabbit Anti-YWHAE (C-term) Antibodies
#35187520 2022/02/12 To Up
The dynamic nature of the coronavirus receptor, angiotensin-converting enzyme 2 (ACE2) in differentiating airway epithelia.
Once inhaled, SARS-CoV-2 particles enter respiratory ciliated cells by interacting with angiotensin converting enzyme 2 (ACE2). Understanding the nature of ACE2 within airway tissue has become a recent focus particularly in light of the COVID-19 pandemic. Airway mucociliary tissue was generated using primary human nasal epithelial cells and the air-liquid interface (ALI) model of differentiation. Using ALI tissue, three distinct transcript variants of ACE2 were identified. One transcript encodes the documented full-length ACE2 protein. The other two transcripts are unique truncated isoforms, that until recently had only been predicted to exist via sequence analysis software. Quantitative PCR revealed that all three transcript variants are expressed throughout differentiation of airway mucociliary epithelia. Immunofluorescence analysis of individual ACE2 protein isoforms exogenously expressed in cell-lines revealed similar abilities to localize in the plasma membrane and interact with the SARS CoV 2 spike receptor binding domain. Immunohistochemistry on differentiated ALI tissue using antibodies to either the N-term or C-term of ACE2 revealed both overlapping and distinct signals in cells, most notably only the ACE2 C-term antibody displayed plasma-membrane localization. We also demonstrate that ACE2 protein shedding is different in ALI Tissue compared to ACE2-transfected cell lines, and that ACE2 is released from both the apical and basal surfaces of ALI tissue. Together, our data highlights various facets of ACE2 transcripts and protein in airway mucociliary tissue that may represent variables which impact an individual's susceptibility to SARS-CoV-2 infection, or the severity of Covid-19.Vincent J Manna, Hana Choi, Shawna M Rotoli, Salvatore J Caradonna
1479 related Products with: The dynamic nature of the coronavirus receptor, angiotensin-converting enzyme 2 (ACE2) in differentiating airway epithelia.
100ug100ug96 wells (1 kit)100ug100.00 ug1100 ug500 Units100ugRelated Pathways
#22911854 2012/07/24 To Up
Pathogenicity of autoantibodies in anti-p200 pemphigoid.
Recently, the C-terminus of laminin γ1 has been identified as target antigen in anti-p200 pemphigoid and the disease was renamed as anti-laminin γ1 pemphigoid. However, the pathogenic relevance of these autoantibodies has not yet been demonstrated. Therefore, we employed an ex vivo model of autoantibody-mediated leukocyte-dependent neutrophil activation and dermal-epidermal separation (DES) using cryosections of human skin. We showed that anti-p200 pemphigoid sera (n = 7) induced DES in a time-dependent manner, in contrast to sera from healthy controls. Furthermore, laminin γ1-specific IgG and serum depleted from anti-laminin γ1 reactivity were generated using the recombinant C-terminus of laminin γ1 (LAMC1-term; amino acids 1364 to 1609). Interestingly, both fractions labeled the dermal-epidermal-junction (DEJ) by indirect immunofluorescence microscopy on human foreskin and recognized a 200 kDa protein by immunoblotting with dermal extract. Human and rabbit IgG against LAMC1-cterm failed to attract neutrophils at the DEJ and to induce DES. In contrast, patient serum depleted from LAMC1-cterm reactivity led to the same extent of DES as non-depleted IgG. Repeated injection of rabbit anti-murine LAMC1-cterm IgG into both neonatal and adult C57BL/6mice as well as repetitive immunization of various mouse strains with murine LAMC1-cterm failed to induce macro- and microscopic lesions. In all mice, circulating anti-LAMC1-cterm antibodies were present, but only in some mice, IgG deposits were seen at the DEJ. We conclude that autoantibodies in anti-p200 pemphigoid sera are pathogenic while pathogenicity is not mediated by autoantibodies against laminin γ1. Further studies are needed to identify the pathogenically relevant autoantigen in anti-p200 pemphigoid.Katerina Vafia, Stephanie Groth, Tina Beckmann, Misa Hirose, Jenny Dworschak, Andreas Recke, Ralf J Ludwig, Takashi Hashimoto, Detlef Zillikens, Enno Schmidt
1465 related Products with: Pathogenicity of autoantibodies in anti-p200 pemphigoid.
100 100 μg100 μg100 μg100 μg100ug Lyophilized100ug Lyophilized100ul100 μg1 mL100 μg100 μgRelated Pathways
#9823765 // To Up
The murine homolog of the HIN 200 family, Ifi 204, is constitutively expressed in myeloid cells and selectively induced in the monocyte/macrophage lineage.
To examine the expression of Ifi 200 genes in vivo and add new information about their function, polyclonal monospecific rabbit antibodies, designated N-term or C-term, were raised against both the N-terminus and C-terminus of the 204 protein (p204) respectively. Western blotting analysis demonstrated that p204 and D3, another member of the Ifi 200 gene family, are constitutively expressed, though at different degrees, in bone marrow, thymus and lymph nodes, and barely detectable in the spleen. Poly rI:rC treatment did not modulate their expression. Peritoneal resident macrophages (Mphi) from untreated mice were negative, but displayed high levels of both p204 and D3 on poly rI:rC treatment. A significant increase of these proteins is also observed when Mphi are cultured overnight in vitro with IFNs or LPS. Lung, kidney and brain were negative for p204 and D3 expression. These results, together with immunohistochemical analysis, demonstrate that the 204 gene has an expression pattern restricted to cells of the myelomonocytic lineage similar to that observed for the human homolog, the myeloid nuclear differentiation antigen (MNDA) suggesting its potential involvement in the differentiation and maturation of this cell lineage.M Gariglio, M De Andrea, M Lembo, M Ravotto, C Zappador, G Valente, S Landolfo
1335 related Products with: The murine homolog of the HIN 200 family, Ifi 204, is constitutively expressed in myeloid cells and selectively induced in the monocyte/macrophage lineage.
150 ul1 mg50 ulRelated Pathways
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