Recombinant Proteins

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SPARC Human

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.

Shipped with Ice Packs
Cat. No.
BT2950
Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

SPARC Human, His

Secreted Protein acidic & Rich in Cysteine Human Recombinant, His Tag

Recombinant Human Osteonectin, fused with a 6X His tag, is produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 295 amino acids, with a molecular weight of 34 kDa. This SPARC protein is expressed with a 6 amino acid His tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3043
Source
Escherichia Coli.
Appearance
White lyophilized (freeze-dried) powder that has been sterile filtered.

SPARCL1 Mouse

SPARC Like 1 Mouse Recombinant

Recombinant SPARCL1 Mouse, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 642 amino acids (17-650 a.a) with a molecular mass of 71.7kDa. It is fused to an 8 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3085
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

SPARC Human, Sf9

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.

Shipped with Ice Packs
Cat. No.
BT3154
Source
Sf9, Baculovirus cells.
Appearance
A sterile, filtered solution appearing colorless.

SPARC Mouse

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.

Shipped with Ice Packs
Cat. No.
BT3215
Source

Sf9, Baculovirus cells.

Appearance
A sterile, filtered solution that is colorless.
Definition and Classification

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 .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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 .

Regulatory Mechanisms

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 .

Applications

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 .

Role in the Life Cycle

Development to Aging and Disease: SPARC is essential during embryogenesis for tissue development and differentiation . Its expression is upregulated in response to injury and during tissue repair . In aging, altered SPARC expression is associated with diseases such as osteoporosis and cancer .

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