protein

Mouse CD105/Endoglin, soluble

MBS692095

0.025 mg

345 USD

Recombinant Protein

Mouse CD105/Endoglin, soluble

[CD105/Endoglin, soluble]

[Recombinant Mouse Soluble CD105/Endoglin; Cell surface MJ7/18 antigen; CD105; Endoglin]

[endoglin isoform 1; Endoglin; endoglin; transmembrane glycoprotein; cell surface MJ7/18 antigen; endoglin; Cell surface MJ7/18 antigen]

[CD105/Endoglin]

[Eng; Eng; Endo; CD105; AI528660; AI662476; S-endoglin; Edg]

EGLN_MOUSE

Insect Cells

Mouse

558

SHLELTLQASKQNGTETQEVFLVLVSNKNVFVKFQAPEIPLHLAYDSSLV IFQGQPRVNITVLPSLTSRKQILDWAATKGAITSIAALDDPQSIVLQLGQ DPKAPFLCLPEAHKDMGATLEWQPRAQTPVQSCRLEGVSGHKEAYILRIL PGSEAGPRTVTVMMELSCTSGDAILILHGPPYVSWFIDINHSMQILTTGE YSVKIFPGSKDKGVELPDTPQGLIAEARKLNASIVTSFVELPLVSNVSLR ASSCGGVFQTTPAPVVTTPPKDTCSPVLLMSLIQPKCGNQVMTLALNKKH VQTLQCTITGLTFWDSSCQAEDTDDHLVLSSAYSSCGMKVTAHVVSNEVI ISFPSGSPPLRKKVQCIDMDSLSFQLGLYLSPHFLQASNTIELGQQAFVQ VSVSPLTSEVTVQLDSCHLDLGPEGDMVELIQSRTAKGSCVTLLSPSPEG DPRFSFLLRVYMVPTPTAGTLSCNLALRPSTLSQEVYKTVSMRLNIVSPD LSHHHHHH
ERVGCDLQPVDPTRGEVTFTTSQVSEGCVAQAANAVREV
HVLFLDFPGML

> 90% by SDS-PAGE & silver stain

Lyophilized

Lyophilized samples are stable for greater than six months at -20 degree C to -70 degree C. Reconstituted sCD105 should be stored in working aliquots at -20 degree C.

Testing Data

Gene: Egn. Stabilizer: None. Reconstitution: The lyophilized sCD105 is soluble in water and most aqueous buffers. The lyophilized sCD105 should be reconstituted in PBS or medium to a concentration not lower than 50ug/ml.

Buffer: PBS. Biological Activity: Not tested so far

Soluble Receptors

A DNA sequence encoding the extracellular domain of mouse Endoglin (Met 1 - Gly 581) was expressed in insect cells. Mouse Endoglin is a disulfide-linked homodimeric protein. Based on N-terminal sequence analysis, the primary structure of recombinant mature Endoglin starts at Glu 26. Endoglin has a calculated monomeric molecular mass of 61 kDa but as a result of glycosylation, migrates at approximately 75 - 85 kDa under reducing conditions in SDS-PAGE. Endoglin, also known as CD105, is a Type I integral membrane glycoprotein with a large, disulfide-linked, extracellular region and a short, constitutively phosphorylated, cytoplasmic tail. Two splice variants of human endoglin, the S-endoglin and L-endoglin that differ in the length of their cytoplasmic tails have been identified. Endoglin is highly expressed on vascular endothelial cells, chondrocytes, and syncytiotrophoblasts of term placenta. It is also found on activated monocytes, bone marrow pro-erythroblasts, and leukemic cells of lymphoid and myeloid lineages. Human and mouse endoglin share approximately 70% and 97 % amino acid sequence identity in their extracellular and intracellular domains, respectively. In common with betaglycan (also named TbetaRIII), a proteoglycan that shares regions of sequence similarity, endoglin is an accessory receptor for the TGF- superfamily ligands. Endoglin does not bind ligands by itself, but does so by associating with a ligand-binding serine/threonine kinase receptor. Endoglin binds TGF-1 and TGF-3 but not TGF-2 efficiently by associating with TGF- type II receptor (TbetaRII). It interacts with activin-A and BMP-7 using either the activin type II or type IIB receptors. In the case of BMP-2 which binds directly to the type I but not the type II BMP receptor, endoglin binds via either BMPR-IA (ALK-3) or BMPR-1B (ALK-6). Although the consequence of endoglin interactions on the functions of TGF- family ligands is poorly understood, endoglin has clearly been shown to be required for angiogenesis and to play a key role in heart development. Mutations in human endoglin or ALK-1 (another type I serine/threonine receptor) lead to the vascular disorder hereditary hemorrhagic telangiectasia (HHT). Mice heterozygous for endoglin have been developed as disease models for HHT. Endoglin has been shown to be a powerful marker of neovascularization. It is also useful as a functional marker that defines long-term repopulating hematopoietic stem cells.

1. Cheifetz et al., J Biol Chem 267:19027, 1992 2. Parker et al., J Bone Miner Res 18:289, 2003 3. Barbara et al., J Biol Chem 274:584, 1999 4. McAllister et al., Nature Genet 8:345, 1994 5. Chen et al., Proc Natl Acad Sci 99:15468, 2002

226437647

NP_031958.2

NM_007932.2

Q63961

70-75 kDa

TGF Beta Signaling Pathway (198393); TGF-beta Receptor Signaling Pathway (198330); XPodNet - Protein-protein Interactions In The Podocyte Expanded By STRING Pathway (755427)

Function: Major glycoprotein of vascular endothelium. Involved in the regulation of angiogenesis. May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors. Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade. Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells. Ref.7. Subunit structure: Homodimer that forms a heteromeric complex with the signaling receptors for transforming growth factor-beta: TGFBR1 and/or TGFBR2. It is able to bind TGF-beta 1, and 3 efficiently and TGF-beta 2 less efficiently. Interacts with TCTEX1D4. Interacts with ARRB2. Interacts with GDF2 . By similarity. Subcellular location: Membrane; Single-pass type I membrane protein. Tissue specificity: Endoglin is restricted to endothelial cells in all tissues except bone marrow and is also found in stromal cells within the connective tissue of intestine, stomach, heart, skeletal muscle, uterus, ovary, oviduct, testis and thymus.

0.025 mg

345 USD