Recombinant Human ADAMTSL1/PUNCTIN Protein (His Tag) | PKSH030600

Recombinant Human ADAMTSL1/PUNCTIN Protein (His Tag) | PKSH030600 | Gentaur US, UK & Europe Disrtribition

Synonyms: ADAMTSL-1;ADAMTSR1;C9orf94;PUNCTIN

Active Protein: N/A

Activity: A DNA sequence encoding the human ADAMTSL1 (Met 1-His439) (Q8N6G6-2) was expressed, with a C-terminal polyhistidine tag.

Protein Construction: A DNA sequence encoding the human ADAMTSL1 (Met 1-His439) (Q8N6G6-2) was expressed, with a C-terminal polyhistidine tag.

Fusion Tag: C-His

Species: Human

Expressed Host: Baculovirus-Insect Cells

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

Purity: > 97 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg 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: 47 kDa

Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4

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

Background: ADAMTSL1 is a secreted molecule resembling members of the ADAMTS protein family of matrix metalloproteinases. Both ADAMTS proteins and ADAM protein family contain a disintegrin and a metalloprotease domain. Metallospondins is collective term for members of ADAMTS protein family. ADAMTS proteins lack the EGF-like domain found normally in members of the ADAM protein family. They also do not possess the canonical disintegrin sequence found in the ADAM protein family. It contains the domains found in members of the ADAMTS protein family with the exception of the pro-metalloprotease and the disintegrin-like domain typical of this family. ADAMTSL1 gene is expressed in adult skeletal muscle. ADAMTSL1 may play an important role in the extracellular matrix as it is deposited in the cell substratum in a punctate fashion and is excluded from focal contacts.

Research Area: N/A