SPARC Protein, Cynomolgus (HEK293, His)

SPARC protein is involved in the regulation of cell growth and may play a regulatory role by affecting the interaction of extracellular matrix and cytokines. SPRC protein can bind calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. It has two calcium binding sites: one is an acidic domain that can bind 5-8 Ca²⁺ with low affinity, and the other is an EF-hand loop that can bind Ca²⁺ ions with high affinity. SPARC Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived SPARC protein, expressed by HEK293 , with C-His labeled tag. The total length of SPARC Protein, Cynomolgus (HEK293, His) is 286 a.a., with molecular weight of 43-48 kDa.

SPARC protein is a cysteine-rich acidic secreted protein, also known as osteonectin or BM-40, and is a matricellular protein that regulates cell adhesion, extracellular matrix production, growth factor activity, and cell cycle. SPARC protein does not play a structural function, but has anti-proliferative and anti-adhesive properties that can regulate the interaction between cells and the surrounding extracellular matrix. SPRC protein is able to bind to Ca and Cu, several types of collagen, albumin, thrombospondin, PDGF, and cell membranes. It has two calcium binding sites: one is an acidic domain that can bind 5-8 Ca²⁺ with low affinity, and the other is an EF-hand ring that can bind Ca²⁺ ions with high affinity. SPARC is overexpressed in sites of injury, regeneration, obesity, cancer, and inflammation, and is a potential target and therapeutic indicator for disease treatment and evaluation.

Cynomolgus

HEK293

C-His

G7P8R2 (A18-I303)

101925878  [NCBI]

43-48 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.