Mouse ADAM9 Protein 3360

$300.00 – $1,000.00

Summary

Expression: HEK293
Active: Yes (catalytic)
Amino Acid Range: Gly30-Asp697

SKU: 3360parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	Q61072
express system	HEK293
product tag	C-His
purity	> 90% as determined by Tris-Bis PAGE;> 90% as determined by HPLC
background	A disintegrin and metalloproteinase 9 (ADAM9) is a member of the transmembrane ADAM family. It is expressed in different types of solid cancer and promotes tumor invasiveness. ADAM9 may be a prognostic marker for vestibular schwannomas (VS), and ADAM9 inhibition might have the potential as a systemic approach for the treatment of VS.
molecular weight	The protein has a predicted MW of 77.61 kDa. Due to furin cleavage site, the protein migrates to 65-115 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Mouse ADAM9 Protein 3360

protein

Size and concentration 100, 500µg and liquid
Form Liquid
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped with dry ice.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
A disintegrin and metalloproteinase 9 (ADAM9) is a member of the transmembrane ADAM family. It is expressed in different types of solid cancer and promotes tumor invasiveness. ADAM9 may be a prognostic marker for vestibular schwannomas (VS), and ADAM9 inhibition might have the potential as a systemic approach for the treatment of VS.
Protein names Disintegrin and metalloproteinase domain-containing protein 9 (ADAM 9) (EC 3.4.24.-) (Meltrin-gamma) (Metalloprotease/disintegrin/cysteine-rich protein 9) (Myeloma cell metalloproteinase)
Gene names Adam9,Adam9 Kiaa0021 Mdc9 Mltng
Mass 10090Da
Function Metalloprotease that cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5 (PubMed:19273593, PubMed:9920899). May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins (PubMed:10825303).
Catalytic activity BINDING 347; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 351; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"; BINDING 357; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="catalytic"; /evidence="ECO:0000250"
Subellular location Cell membrane ; Single-pass type I membrane protein .
Structure Interacts with SH3GL2 and SNX9 through its cytoplasmic tail (PubMed:10531379). Interacts with ITGA6 (PubMed:10825303).
Post-translational modification Proteolytically cleaved in the trans-Golgi network before it reaches the plasma membrane to generate a mature protein. The removal of the pro-domain occurs via cleavage at two different sites. Processed most likely by a pro-protein convertase such as furin, at the boundary between the pro-domain and the catalytic domain. An additional upstream cleavage pro-protein convertase site (Arg-56/Glu-57) has an important role in the activation of ADAM9.; Phosphorylation is induced in vitro by phorbol-12-myristate-13-acetate (PMA) (PubMed:9920899).
Target Relevance information above includes information from UniProt accession: Q61072
The UniProt Consortium

Measured by its ability to cleave a fluorogenic peptidesubstrate Mca-PLAQAV-Dpa-RSSSR-NH The specificactivity is > 1.0 pmol/min/ug.

The purity of Mouse ADAM9 is greater than 90% as determined by SEC-HPLC.

Mouse ADAM9 on Tris-Bis PAGE under reduced condition. The purity is greater than 90%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.