SPARC Human, His

Secreted Protein acidic & Rich in Cysteine Human Recombinant, His Tag
Cat. No.
BT3043
Source
Escherichia Coli.
Synonyms
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec'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.
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Description

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.

Product Specs

Introduction
SPARC, which stands for 'secreted protein, acidic and rich in cysteine', is also called osteonectin or BM-40. It belongs to a family of secreted matricellular proteins that share a similar domain structure. This protein is 303 amino acids long with a molecular weight of 43 kDa. It consists of a 17 amino acid signal sequence, an acidic region at the N-terminus that can bind calcium, a follistatin domain with Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain containing two EF-hand motifs. Fibroblasts, capillary endothelial cells, platelets, and macrophages produce SPARC, particularly in areas where tissues are being formed and remodeled. SPARC's effects vary depending on the context, but it usually hinders cell adhesion, spreading, and proliferation while promoting the formation of collagen matrix. In endothelial cells, SPARC disrupts focal adhesions and binds to and sequesters PDGF and VEGF. Bone tissue expresses high levels of SPARC, where it encourages the differentiation of osteoblasts and suppresses adipogenesis.
Description
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.
Physical Appearance
White lyophilized (freeze-dried) powder that has been sterile filtered.
Formulation
Following extensive dialysis against 20mM PBS at pH 7.4, the SPARC (at a concentration of 1 mg/ml) was lyophilized.
Solubility
It is advised to reconstitute the lyophilized SPARC in sterile 18MΩ-cm H2O to a concentration of at least 100 µg/ml. This solution can then be further diluted into other aqueous solutions.
Stability
Lyophilized Osteonectin, while stable at room temperature for 3 weeks, should be stored in a dry environment below -18°C. Once reconstituted, BM-40 should be stored at 4°C for 2-7 days. For future use, it should be stored below -18°C. To ensure long-term storage, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeding 95.0% as determined by: (a) RP-HPLC analysis. (b) SDS-PAGE analysis.
Synonyms
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
Source
Escherichia Coli.
Amino Acid Sequence
MSYYHHHHHHPQQEALPDETEVVEETVAEVTEVSVGANPVQVEVGEFD
DGAEETEEEVVAENPCQNHHCKHGKVCELDENNTPMCVCQDPTSCP
APIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCK
YIPPCLDSELTEFPLRMRDWLKNVLVTLYERDEDNNLLTKQKLRVKKI
HENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGY
LSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALDEWAGCFGIKQK
DIDKDLVI.

Product Science Overview

Structure and Domains

SPARC is a 40 kDa protein consisting of a single polypeptide chain that can be divided into four distinct domains :

  1. Domain I: A calcium-binding domain near the glutamic acid-rich region at the amino terminus.
  2. Domain II: A cysteine-rich domain.
  3. Domain III: A hydrophilic region.
  4. Domain IV: An EF-hand motif at the carboxy terminus.

These domains enable SPARC to interact with various components of the ECM, including collagen and hydroxyapatite, facilitating its role in bone mineralization and cell-matrix interactions .

Functions

SPARC is involved in several biological processes, including:

  • Bone Mineralization: SPARC binds to calcium and collagen, promoting the formation of mineral crystals in the bone .
  • Cell-Matrix Interactions: It modulates cell attachment, spreading, and migration by interacting with ECM components .
  • Angiogenesis: SPARC plays a role in the formation of new blood vessels, which is essential for tissue repair and tumor growth .
  • Regulation of Cell Cycle: It can delay the cell cycle in the G1 phase, affecting cell proliferation .
Expression and Regulation

SPARC is predominantly expressed in non-epithelial cells, including endothelial and smooth muscle cells, osteoblasts, and platelets . Its expression is regulated by various factors, including retinoic acid and dexamethasone, which can stimulate SPARC transcription through specific promoter elements .

Clinical Significance

Overexpression of SPARC has been associated with several types of cancer, including breast, prostate, colon, and pancreatic cancers . Its role in promoting angiogenesis and cell migration makes it a potential target for cancer therapy . Additionally, SPARC is involved in wound healing and tissue remodeling, making it a critical protein for maintaining tissue homeostasis .

Recombinant SPARC (Human, His Tag)

Recombinant SPARC proteins, such as the human recombinant SPARC with a His tag, are produced using recombinant DNA technology. These proteins are used in various research applications to study the functions and interactions of SPARC in vitro. The His tag facilitates the purification and detection of the recombinant protein, making it a valuable tool for biochemical and structural studies .

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