Secreted Protein Acidic & Rich in Cysteine Recombinant Human
Recombinant Human Secreted Protein Acidic & Rich in Cysteine, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 286 amino acids, with a molecular weight of 32.7 kDa. The purification of SPARC is achieved using proprietary chromatographic methods.
Escherichia Coli.
Sterile Filtered White lyophilized (freeze-dried) powder.
Secreted Protein acidic & Rich in Cysteine Human Recombinant, His Tag
SPARC Like 1 Mouse Recombinant
Secreted Protein Acidic & Rich in Cysteine Human Recombinant, Sf9
Recombinant Human SPARC, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 295 amino acids (residues 18-303). With a molecular weight of 33.8 kDa, it features a 9 amino acid His-tag at the C-terminus. Purification is achieved through proprietary chromatographic techniques.
Secreted Protein Acidic & Rich in Cysteine Mouse Recombinant
Recombinant Mouse SPARC protein, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 291 amino acids (18-302a.a) with a molecular weight of 33.3kDa. This protein includes a 6 amino acid His-tag fused at the C-terminus and is purified using proprietary chromatographic techniques.
Sf9, Baculovirus cells.
SPARC (Secreted Protein Acidic and Rich in Cysteine), also known as osteonectin or BM-40, is a matricellular glycoprotein involved in various cellular processes. It is encoded by the SPARC gene located on chromosome 5q31-q33 in humans . SPARC is classified as a non-collagenous extracellular matrix (ECM) protein that plays a regulatory role in cell-matrix interactions .
Key Biological Properties: SPARC is a 32-35 kDa protein composed of three structural domains: an acidic N-terminal domain, a follistatin-like domain, and a Ca²⁺-binding extracellular domain . It is known for its anti-adhesive properties, disrupting cell-matrix interactions and inhibiting cell cycle progression .
Expression Patterns and Tissue Distribution: SPARC is expressed in a variety of tissues, particularly those undergoing remodeling, repair, or development . It is abundantly found in bone, where it is secreted by osteoblasts, and in other tissues such as the skin, heart, and kidneys .
Primary Biological Functions: SPARC regulates cell growth, differentiation, and migration by modulating interactions between cells and the ECM . It plays a crucial role in bone mineralization, collagen binding, and ECM organization .
Role in Immune Responses and Pathogen Recognition: SPARC is involved in immune responses by modulating the activity of cytokines and growth factors, thereby influencing inflammation and tissue repair .
Mechanisms with Other Molecules and Cells: SPARC interacts with various ECM components, including collagen, thrombospondin, and vitronectin . It binds to growth factors such as PDGF and VEGF, modulating their activity and influencing cell behavior .
Binding Partners and Downstream Signaling Cascades: SPARC’s binding to ECM components and growth factors triggers downstream signaling pathways that regulate cell adhesion, migration, and proliferation . It also affects the expression of matrix metalloproteinases (MMPs), which are involved in ECM remodeling .
Regulation of Expression and Activity: SPARC expression is regulated at both transcriptional and post-transcriptional levels . Transcription factors such as SP1 and AP-1 play a role in its gene regulation .
Post-Translational Modifications: SPARC undergoes various post-translational modifications, including phosphorylation and glycosylation, which influence its stability and activity .
Biomedical Research: SPARC is a valuable biomarker in cancer research due to its role in tumor progression and metastasis . It is also studied for its involvement in tissue repair and fibrosis .
Diagnostic Tools and Therapeutic Strategies: SPARC’s expression levels can serve as diagnostic markers for various diseases, including cancer and fibrosis . Therapeutically, targeting SPARC or its pathways holds potential for treating these conditions .