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Legumain Recombinant Protein | LGMN recombinant protein

Legumain Protein, Sus scrofa (Pig), Recombinant (His Tag)

Purity
>95% as determined by SDS-PAGE
Synonyms
Legumain; Legumain Protein; Sus scrofa (Pig); Recombinant (His Tag); Sus scrofa (Pig) Legumain/LGMN/AEP Protein (His Tag); legumain; LGMN recombinant protein
Ordering
For Research Use Only!
Host
HEK293 Cells
Purity/Purification
>95% as determined by SDS-PAGE
Form/Format
Lyophilized from sterile 20mM Tris, 50mM NaCl, pH8.0. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Sequence
Val18-Tyr433
Species
Sus scrofa (Pig)
Endotoxin
<1.0EU per ug of the protein as determined by the LAL method
Predicted N Terminal
His
Tag
N-His
Protein Construction
A DNA sequence encoding the sus scrofa(Pig) LGMN (XP_001927117.4)(Val18-Tyr433) was expressed with a polyhistidine tag at the N-terminus.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Preparation and Storage
Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.
They are shipped out with blue ice.

SDS-Page

SDS-Page
Related Product Information for LGMN recombinant protein
Background: The Mammalian Legumain, also known as LGMN, also called asparaginyl endopeptidase (AEP), is a cysteine protease belonging to peptidase family C13 with strict specificity for hydrolysis of asparaginyl bonds. Known previously only from plants and invertebrates, Legumain is discovered as a lysosomal endopeptidase in mammals. Mammalian Legumain is a cysteine endopeptidase, inhibited by iodoacetamide and maleimides, but unaffected by compound E64. The Mammalian Legumain is involved in the processing of bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Legumain has been observed to be highly expressed in several types of solid tumors. It was demonstrated in membrane-associated vesicles concentrated at the invadopodia of tumor cells and on cell surfaces where it colocalized with integrins. Legumain was demonstrated to activate progelatinase A. Cells overexpressing Legumain possessed increased migratory and invasive activity in vitro and adopted an invasive and metastatic phenotype in vivo, inferring significance of Legumain in tumor invasion and metastasis. Also, Legumain is expressed in both murine and human atherosclerotic lesions. The macrophage-specific expression of Legumain in vivo and the ability of Legumain to induce chemotaxis of monocytes and endothelial cells in vitro suggest that Legumain may play a functional role in atherogenesis.
References
Schwarz G, et al. (2002) Characterization of legumain. Biol Chem. 383(11): 1813-6.Liu C, et al. (2003) Overexpression of legumain in tumors is significant for invasion/metastasis and a candidate enzymatic target for prodrug therapy. Cancer Res. 63(11): 2957-64.Murthy RV, et al. (2005) Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer. Clin Cancer Res. 11(6): 2293-9.Gawenda J, et al. (2007) Legumain expression as a prognostic factor in breast cancer patients. Breast Cancer Res Treat. 102(1): 1-6.Clerin V, et al. (2007) Expression of the cysteine protease legumain in vascular lesions and functional implications in atherogenesis. Atherosclerosis. 201(1): 53-66.Lewen S, et al. (2008) A Legumain-based minigene vaccine targets the tumor stroma and suppresses breast cancer growth and angiogenesis. Cancer Immunol Immunother. 57(4): 507-15.

NCBI and Uniprot Product Information

Molecular Weight
The recombinant sus scrofa (Pig) LGMN consists of 435 amino acids and has a predicted molecular mass of 49.7kDa. The apparent molecular mass of it is approximately 52.5kDa in SDS-PAGE under reducing conditions.
Protein Family

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Product Notes

The LGMN (Catalog #AAA8123283) is a Recombinant Protein produced from HEK293 Cells and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: Val18-Tyr4 33. It is sometimes possible for the material contained within the vial of "Legumain, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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