Endoglin Human, Sf9

Endoglin Human Recombinant, Sf9
Cat. No.
BT21925
Source
Sf9 Insect Cells.
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, 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.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
Endoglin is a transmembrane glycoprotein found on cell surfaces, belonging to the TGF beta receptor complex. It forms a homodimer with a molecular weight of 180 kDa, linked by disulfide bonds. Endoglin is expressed on various cell types, including endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. It participates in the TGF-beta1 receptor complex, suggesting a role in binding TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Besides TGF-beta signaling, endoglin might be involved in cytoskeletal organization, influencing cell shape and movement. It plays a crucial role in cardiovascular system development and vascular remodeling, with its expression regulated during heart development. Mice lacking the endoglin gene experience cardiovascular abnormalities and die.
Description
Recombinant human CD105, expressed in baculovirus, is a glycosylated homodimeric polypeptide. It consists of 586 amino acids, with a predicted molecular weight of 61 kDa. Due to glycosylation, it migrates at approximately 90 kDa under reducing conditions in SDS-PAGE. The CD105 protein is engineered with a C-terminal His-tag (6xHis) for purification using specialized chromatographic methods.
Physical Appearance
White, sterile-filtered powder obtained by lyophilization (freeze-drying).
Formulation
Endoglin is supplied as a lyophilized powder, prepared from a sterile solution at a concentration of 1 mg/ml in 1xPBS.
Solubility
To reconstitute 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 extended storage, it is recommended to store it desiccated at -18°C or below. Once reconstituted, CD105 should be stored at 4°C and used within 2-7 days. For long-term storage, adding a carrier protein such as 0.1% HSA or BSA is advised. Avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 95%, as determined by: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) and (b) SDS-PAGE analysis.
Biological Activity
The biological activity of the protein is determined by its ability to bind to recombinant human TGF-beta receptor II (rhTGF-beta RII) fused to the Fc region of immunoglobulin G (IgG) in a functional ELISA. The optimal dilutions for specific applications should be determined by each laboratory.
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Source
Sf9 Insect Cells.
Amino Acid Sequence
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.

Product Science Overview

Structure and Function

Endoglin is a homodimeric protein, meaning it consists of two identical subunits linked by disulfide bonds. Each subunit has a molecular weight of approximately 90 kDa due to glycosylation, although the polypeptide chain itself is around 61 kDa . The protein contains a zona pellucida (ZP) domain and an orphan domain (OD) at its N-terminal extracellular region, which is unique and does not have homology to any other known protein .

Endoglin is involved in the binding of various ligands, including TGF-β1, TGF-β3, Activin-A, BMP-2, and BMP-7. It modulates cellular responses to Bone Morphogenetic Protein (BMP)-9 and BMP-10 by interacting with the type I TGF-β signaling receptor activin receptor-like kinase (ALK)1 . This interaction is crucial for the regulation of angiogenesis, the process of new blood vessel formation, and vascular remodeling .

Clinical Significance

Mutations in the endoglin gene (ENG) are associated with hereditary hemorrhagic telangiectasia (HHT), a genetic disorder that leads to abnormal blood vessel formation. Endoglin is also implicated in preeclampsia, a pregnancy-related condition characterized by high blood pressure and damage to other organs .

Recombinant Production in Sf9 Cells

The recombinant form of human endoglin is produced using the Sf9 insect cell expression system. Sf9 cells, derived from the fall armyworm Spodoptera frugiperda, are commonly used for the production of recombinant proteins due to their high expression levels and ability to perform post-translational modifications similar to those in mammalian cells .

The recombinant endoglin produced in Sf9 cells is typically fused to a C-terminal His-tag (6xHis) to facilitate purification. The protein is purified using proprietary chromatographic techniques to achieve a purity of ≥95% as determined by SDS-PAGE and HPLC .

Applications

Recombinant endoglin is used in various research applications, including studies on angiogenesis, vascular biology, and related diseases. It serves as a valuable tool for understanding the molecular mechanisms underlying these processes and for developing potential therapeutic interventions.

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