SPARC Mouse

Secreted Protein Acidic & Rich in Cysteine Mouse Recombinant
Cat. No.
BT3215
Source

Sf9, Baculovirus cells.

Synonyms

Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine

Appearance
Sterile Filtered colorless solution.
Purity

Greater than 95.0% as determined by SDS-PAGE.

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction

Secreted Protein Acidic and Rich in Cysteine (SPARC), also known as osteonectin, is encoded by the SPARC gene in humans. This glycoprotein plays a crucial role in bone mineralization by binding to calcium. SPARC is synthesized by various cells, including fibroblasts, capillary endothelial cells, platelets, and macrophages, primarily in tissues undergoing morphogenesis and remodeling. Besides calcium, SPARC also exhibits binding affinity for collagen.

Description

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.

Physical Appearance
A sterile, filtered solution that is colorless.
Formulation

The SPARC solution is provided at a concentration of 0.25mg/ml and is formulated in Phosphate-Buffered Saline (pH 7.4) with 10% glycerol.

Stability

For short-term storage (2-4 weeks), the SPARC solution should be stored at 4°C. For extended storage, it is recommended to store the solution frozen at -20°C. To ensure stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is advisable. It is important to avoid repeated freeze-thaw cycles to maintain protein integrity.

Purity

The purity of SPARC Mouse Recombinant is determined to be greater than 95.0% as assessed by SDS-PAGE analysis.

Synonyms

Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine

Source

Sf9, Baculovirus cells.

Amino Acid Sequence

APQQTEVAEE IVEEETVVEE TGVPVGANPV QVEMGEFEDG AEETVEEVVA DNPCQNHHCK HGKVCELDES NTPMCVCQDP TSCPAPIGEF EKVCSNDNKT FDSSCHFFAT KCTLEGTKKG HKLHLDYIGP CKYIAPCLDS ELTEFPLRMR DWLKNVLVTL YERDEGNNLL TEKQKLRVKK IHENEKRLEA GDHPVELLAR DFEKNYNMYI FPVHWQFGQL DQHPIDGYLS HTELAPLRAP LIPMEHCTTR FFETCDLDND KYIALEEWAG CFGIKEQDIN KDLVIHHHHH H

Product Science Overview

Structure and Composition

SPARC is a 40 kDa acidic and cysteine-rich glycoprotein consisting of a single polypeptide chain. It can be divided into four domains:

  1. Ca²⁺ Binding Domain: Located near the glutamic acid-rich region at the amino terminus.
  2. Cysteine-Rich Domain: Contains multiple cysteine residues.
  3. Hydrophilic Region: A region that interacts with water molecules.
  4. EF Hand Motif: Located at the carboxy terminus, involved in calcium binding .
Functions

SPARC is involved in several biological processes, including:

  • Bone Mineralization: It binds to calcium and collagen, promoting the formation of mineral crystals in bones .
  • ECM Remodeling: Acts as a matricellular chaperone, mediating the disassembly and degradation of ECM networks .
  • Cell-Matrix Interactions: Modulates interactions between cells and the ECM, influencing cell adhesion, migration, and proliferation .
  • Tumor Biology: Overexpression of SPARC has been linked to various cancers, including breast, prostate, colon, and pancreatic cancers. It promotes angiogenesis, proliferation, and migration of tumor cells .
Mouse Recombinant SPARC

The mouse recombinant version of SPARC is produced using recombinant DNA technology, where the SPARC gene from mice is inserted into a suitable expression system, such as bacteria or yeast. This allows for the production of large quantities of SPARC protein for research and therapeutic purposes.

Research and Applications

SPARC has been extensively studied for its role in tissue remodeling and repair. It has potential therapeutic applications in treating diseases related to ECM dysfunction, such as fibrosis and cancer . Additionally, SPARC’s role in bone mineralization makes it a target for osteoporosis research .

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