Recombinant Proteins
Product List
SPARC Human
Secreted Protein Acidic & Rich in Cysteine Recombinant Human
Secreted Protein Acidic & Rich in Cysteine Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 286 amino acids and having a molecular mass of 32.7kDa.
SPARC is purified by proprietary chromatographic techniques.
Escherichia Coli.
Sterile Filtered White lyophilized (freeze-dried) powder.
SPARC Human, His
Secreted Protein acidic & Rich in Cysteine Human Recombinant, His Tag
Osteonectin Human Recombinant fused with 6X His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 295 amino acids and having a molecular mass of 34 kDa.
SPARC is expressed with a 6 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
SPARCL1 Mouse
SPARC Like 1 Mouse Recombinant
SPARCL1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 642 amino acids (17-650 a.a) and having a molecular mass of 71.7kDa.
SPARCL1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
SPARC Human, Sf9
Secreted Protein Acidic & Rich in Cysteine Human Recombinant, Sf9
SPARC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 295 amino acids (18-303 a.a) and having a molecular mass of 33.8kDa.
SPARC is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
SPARC Mouse
Secreted Protein Acidic & Rich in Cysteine Mouse Recombinant
SPARC Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 291 amino acids (18-302a.a) and having a molecular mass of 33.3kDa.
SPARC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
Introduction
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 .
