SRP6015
Endoglin human
recombinant, expressed in Sf9 cells, ≥95% (SDS-PAGE), ≥95% (HPLC)
Synonym(s):
CD105, END, ENG, HHT1, ORW
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About This Item
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This Item | SRP6016 | SRP3007 | SRP3025 |
|---|---|---|---|
| technique(s) cell culture | mammalian: suitable | technique(s) - | technique(s) cell culture | mammalian: suitable | technique(s) cell culture | mammalian: suitable |
| biological source human | biological source mouse | biological source human | biological source human |
| recombinant expressed in Sf9 cells | recombinant expressed in Sf9 cells | recombinant expressed in HeLa cells | recombinant expressed in HEK 293 cells |
| mol wt 90.0 kDa | mol wt 75-85 kDa | mol wt 60.0-70.0 kDa | mol wt 57.0-60.0 kDa |
| form lyophilized | form lyophilized | form lyophilized | form lyophilized |
General description
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.
Physical form
Lyophilized from PBS pH 7.4.
Reconstitution
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.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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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
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
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
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
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
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