SRP6015
Endoglin human
recombinant, expressed in Sf9 cells, ≥95% (SDS-PAGE), ≥95% (HPLC)
Sinónimos:
CD105, END, ENG, HHT1, ORW
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About This Item
origen biológico
human
recombinante
expressed in Sf9 cells
Análisis
≥95% (HPLC)
≥95% (SDS-PAGE)
formulario
lyophilized
mol peso
90.0 kDa
envase
pkg of 10 μg
técnicas
cell culture | mammalian: suitable
impurezas
Endotoxin, tested
Nº de acceso NCBI
Nº de acceso UniProt
Condiciones de envío
wet ice
temp. de almacenamiento
−20°C
Información sobre el gen
human ... ENG(2022)
Descripción general
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex. Endoglin consists of a homodimer of 180 kDa with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, Activin-A, BMP-2, and BMP-7. It has been postulated that Endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development. CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, polypeptide containing 586 amino acids and having a molecular mass of 61 kDa, but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.
Forma física
Lyophilized from PBS pH 7.4.
Reconstitución
Centrifuge the vial prior to opening. Reconstitute in sterile PBS to a concentration of ~ 100 μg/ml. This solution can then be diluted into other aqueous buffers.
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Daniel Beiroa et al.
PloS one, 8(1), e54591-e54591 (2013-01-22)
Endoglin is a transmembrane auxiliary receptor for transforming growth factor-beta (TGF-beta) that is predominantly expressed on proliferating endothelial cells. It plays a wide range of physiological roles but its importance on energy balance or insulin sensitivity has been unexplored. Endoglin
Olivier Nolan-Stevaux et al.
PloS one, 7(12), e50920-e50920 (2013-01-10)
Endoglin (ENG), a co-receptor for several TGFβ-family cytokines, is expressed in dividing endothelial cells alongside ALK1, the ACVRL1 gene product. ENG and ACVRL1 are both required for angiogenesis and mutations in either gene are associated with Hereditary Hemorrhagic Telangectasia, a
David M Charytan et al.
International journal of cardiology, 176(1), 99-109 (2014-07-23)
Sudden cardiovascular death is increased in chronic kidney disease (CKD). Experimental CKD models suggest that angiogenesis and nitric oxide (NO) inhibitors induce myocardial fibrosis and microvascular dropout thereby facilitating arrhythmogenesis. We undertook this study to characterize associations of CKD with
Caixia Yuan et al.
Experimental and therapeutic medicine, 17(4), 2547-2556 (2019-03-25)
Bone morphogenetic protein (BMP) expression has been observed in the uterus in previous studies. However, the influence of BMP7 on blastocyst implantation remains unclear. Blastocysts first act on luminal endometrial epithelial cells during implantation. The purpose of the present study
Lee B Rivera et al.
The Journal of cell biology, 193(7), 1305-1319 (2011-06-29)
Pericytes migrate to nascent vessels and promote vessel stability. Recently, we reported that secreted protein acidic and rich in cysteine (SPARC)-deficient mice exhibited decreased pericyte-associated vessels in an orthotopic model of pancreatic cancer, suggesting that SPARC influences pericyte behavior. In
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