Endoglin Mouse

Endoglin Mouse Recombinant
Cat. No.
BT21993
Source
Insect Cells.
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Cell surface MJ7/18 antigen, Endoglin.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

CD105 Mouse Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 581 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 75-85 kDa under reducing conditions in SDS-PAGE. Based on N-terminal sequence analysis, the primary structure of recombinant mature Endoglin starts at Glu 26. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Endoglin, a type I membrane glycoprotein found on cell surfaces, is an integral part of the TGF beta receptor complex. This protein exists as a homodimer with a molecular weight of 180 kDa, interconnected by disulfide bonds. Its presence has been observed in endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Functionally, endoglin participates in the TGF-beta1 receptor complex, suggesting its involvement in binding TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beyond TGF-beta signaling, endoglin may contribute to cytoskeletal organization, influencing cell morphology and migration. It plays a critical role in cardiovascular system development and vascular remodeling, with its expression being regulated during heart development. Notably, experimental mice lacking the endoglin gene exhibit cardiovascular abnormalities and do not survive.
Description
Recombinant Mouse Endoglin, encompassing the extracellular domain, is produced in a baculovirus expression system. This homodimeric glycoprotein consists of 581 amino acids, resulting in a molecular mass of 61 kDa. However, due to glycosylation, it migrates at 75-85 kDa under reducing conditions in SDS-PAGE. The primary structure of the mature recombinant Endoglin, as determined by N-terminal sequence analysis, commences at Glu 26. This protein is engineered with a C-terminal His-tag (6xHis) and purified using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
Endoglin is lyophilized from a sterile solution at a concentration of 1 mg/ml, without any additional additives.
Solubility
To reconstitute the lyophilized CD-105, it is recommended to dissolve it in sterile PBS at a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Endoglin remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is advisable to store it desiccated below -18°C. After reconstitution, CD105 can be stored at 4°C for 2-7 days. For extended storage, freezing below -18°C is recommended. To ensure optimal stability during long-term storage, consider adding a carrier protein like HSA or BSA (0.1%). It's crucial to avoid repeated freeze-thaw cycles.
Purity
The purity of Endoglin is greater than 95.0%, as determined by: (a) Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) analysis, and (b) SDS-PAGE analysis.
Biological Activity
The biological activity of Endoglin is evaluated based on its ability to bind with recombinant human TGF-beta RII/Fc using a functional ELISA. It is recommended that each laboratory determine the optimal dilutions for their specific applications.
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Cell surface MJ7/18 antigen, Endoglin.
Source
Insect Cells.
Amino Acid Sequence
MDRGVLPLPITLLFVIYSFVPTTGLAERVGCDLQPVDPTRGEVT FTTSQVSEGCVAQAANAVREVHVLFLDFPGMLSHLELTLQASKQNGTETQEVF LVLVSNKNVFVKFQAPEIPLHLAYDSSLVIFQGQPRVNITVLPSLTSRKQILDWA ATKGAITSIAALDDPQSIVLQLGQDPKAPFLCLPEAHKDMGATLEWQPRAQTP VQSCRLEGVSGHKEAYILRILPGSEAGPRTVTVMMELSCTSGDAILILHGPPYVS WFIDINHSMQILTTGEYSVKIFPGSKVKGVELPDTPQGLIAEARKLNASIVTSFV ELPLVSNVSLRASSCGGVFQTTPAPVVTTPPKDTCSPVLLMSLIQPKCGNQVMT LALNKKHVQTLQCTITGLTFWDSSCQAEDTDDHLVLSSAYSSCGMKVTAHVV SNEVIISFPSGSPPLRKKVQCIDMDSLSFQLGLYLSPHFLQASNTIELGQQAFVQV SVSPLTSEVTVQLDSCHLDLGPEGDMVELIQSRTAKGSCVTLLSPSPEGDPRFSF LLRVYMVPTPTAGTLSCNLALRPSTLSQEVYKTVSMRLNIVSPDLS.

Product Science Overview

Structure and Function

Endoglin is a 180 kDa protein that functions as a co-receptor for ligands of the TGF-β superfamily . It is composed of an extracellular domain, a single transmembrane domain, and a short cytoplasmic tail. The extracellular domain contains a zona pellucida (ZP) domain and an orphan domain (OD), which is unique and does not have homology to any other known protein .

Endoglin interacts with the type I TGF-β signaling receptor activin receptor-like kinase (ALK)1 and modulates cellular responses to Bone Morphogenetic Protein (BMP)-9 and BMP-10 . This interaction is essential for the regulation of angiogenesis, particularly during development and in response to injury .

Recombinant Endoglin

Recombinant endoglin, including mouse recombinant endoglin, is produced using various expression systems to study its structure and function in vitro. These recombinant proteins are often used in research to understand the molecular mechanisms underlying endoglin’s role in vascular biology and its involvement in diseases such as hereditary hemorrhagic telangiectasia (HHT) and preeclampsia .

Applications in Research

Recombinant endoglin is utilized in various experimental setups, including surface plasmon resonance (SPR) and cellular assays, to study its binding properties and interactions with other proteins . These studies have provided insights into the recognition and binding ability of endoglin to BMP-9 and its role in dimerization, which is crucial for its function .

Clinical Relevance

Endoglin’s role in angiogenesis makes it a potential therapeutic target for diseases characterized by abnormal blood vessel formation. Understanding the molecular details of endoglin’s interactions and functions can lead to the development of novel therapeutic strategies for conditions such as cancer, cardiovascular diseases, and fibrotic disorders .

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