Recombinant Mouse ADAM9 Protein (His Tag) | PKSM040887

Recombinant Mouse ADAM9 Protein (His Tag) | PKSM040887 | Gentaur US, UK & Europe Disrtribition

Synonyms: AU020942;MDC9;mKIAA0021;Mltng

Active Protein: N/A

Activity: A DNA sequence encoding the mouse ADAM9 (Q61072) extracellular domain (Met 1-Asp 697) was expressed with a C-terminal polyhistidine tag.

Protein Construction: A DNA sequence encoding the mouse ADAM9 (Q61072) extracellular domain (Met 1-Asp 697) was expressed with a C-terminal polyhistidine tag.

Fusion Tag: C-His

Species: Mouse

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 87 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 74.9 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: ADAM9 (A disintegrin and metallopeptidase domain 9, MDC9, meltrin gamma), is a type 1 transmembrane protein that has been associated with cancer development and metastases. ADAM9 is consistently overexpressed in various human cancers, and plays a role in tumorigenesis in mouse models. ADAM9 cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as EGF, FGFR2iiib, Tie-2, Flk-1, EphB4, CD40, VCAM-1, and VE-cadherin, and could represent a potential therapeutic target in tumors where it is highly expressed. ADAM9 belongs to a family of transmembrane, disintegrin-containing metalloproteinases involved in protein ectodomain shedding and cell-cell and cell-matrix interactions. ADAM-9 adhesive domain plays a role in regulating the motility of cells by interaction with beta1 integrins and modulates MMP synthesis.

Research Area: N/A