COMP Human, HEK

Cartilage Oligomeric Matrix Protein Human Recombinant, HEK
Cat. No.
BT1150
Source
HEK293
Synonyms
Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5.
Appearance
Purity
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.
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Description

COMP HEK Protein is a 82.4 kDa protein containing 750 aa fused to a 13 aa N-Terminal
FLAG-tag.

Product Specs

Introduction
Cartilage Oligomeric Matrix Protein (COMP), a prominent member of the thrombospondin family, is a large, non-collagenous glycoprotein exceeding 500kDa. Primarily recognized for its presence in the extracellular matrix of cartilage tissues like articular, nasal, and tracheal cartilage, COMP also exists in other tissues like synovium and tendon. Its complex structure consists of five identical subunits, forming a pentameric arrangement. The carboxy-terminal globular domain of COMP exhibits binding affinity to collagens I, II, and IX, underscoring its crucial role in maintaining the structural integrity and properties of the collagen network. Beyond its structural contribution, COMP serves as a reservoir and transporter for hydrophobic signaling molecules such as vitamin D. Genetic mutations affecting the COMP gene have been linked to skeletal dysplasias like pseudoachondroplasia and certain forms of multiple epiphyseal dysplasia, highlighting the importance of COMP in normal skeletal development and function. Notably, serum COMP levels provide valuable insights into metabolic alterations occurring within cartilage.
Description
Recombinant human COMP protein, encompassing 750 amino acids with a molecular weight of 82.4 kDa, is expressed in HEK293 cells and features a 13 amino acid N-terminal FLAG-tag.
Formulation
Human COMP, produced in HEK cells, is subjected to filtration (0.4µm) and lyophilization from a solution containing 20mM TRIS and 50mM NaCl at a pH of 7.5. The lyophilized protein is supplied at a concentration of 0.5 mg/ml.
Solubility
To generate a working solution, reconstitute the lyophilized COMP HEK Human by adding deionized water to achieve an approximate concentration of 0.5mg/ml. Allow sufficient time for the lyophilized pellet to dissolve completely. Note that the product is not sterile. Prior to cell culture applications, it is essential to filter the reconstituted protein through an appropriate sterile filter.
Stability
Lyophilized COMP HEK Human should be stored at -20°C. To maintain protein stability, it is recommended to aliquot the reconstituted product into smaller volumes and avoid repeated freeze-thaw cycles. Following reconstitution, COMP HEK can be stored at 4°C for a limited duration. Storage at 4°C for two weeks has not been observed to cause any noticeable changes in protein quality.
Synonyms
Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5.
Source
HEK293
Amino Acid Sequence
HVDYKDDDDK PAGQGQSPLG SDLGPQMLRE LQETNAALQD VRELLRQQVR EITFLKNTVM ECDACGMQQS VRTGLPSVRP LLHCAPGFCF PGVACIQTES GARCGPCPAG FTGNGSHCTD VNECNAHPCF PRVRCINTSP GFRCEACPPG YSGPTHQGVG LAFAKANKQV CTDINECETG QHNCVPNSVC INTRGSFQCG PCQPGFVGDQ ASGCQRRAQR FCPDGSPSEC HEHADCVLER DGSRSCVCAV GWAGNGILCG RDTDLDGFPD EKLRCPERQC RKDNCVTVPN SGQEDVDRDG IGDACDPDAD GDGVPNEKDN CPLVRNPDQR NTDEDKWGDA CDNCRSQKND DQKDTDQDGR GDACDDDIDG DRIRNQADNC PRVPNSDQKD SDGDGIGDAC DNCPQKSNPD QADVDHDFVG DACDSDQDQD GDGHQDSRDN CPTVPNSAQE DSDHDGQGDA CDDDDDNDGV PDSRDNCRLV PNPGQEDADR DGVGDVCQDD FDADKVVDKI DVCPENAEVT LTDFRAFQTV VLDPEGDAQI DPNWVVLNQG REIVQTMNSD PGLAVGYTAF NGVDFEGTFH VNTVTDDDYA GFIFGYQDSS SFYVVMWKQM EQTYWQANPF RAVAEPGIQL KAVKSSTGPG EQLRNALWHT GDTESQVRLL WKDPRNVGWK DKKSYRWFLQ HRPQVGYIRV RFYEGPELVA DSNVVLDTTM RGGRLGVFCF SQENIIWANL RYRCNDTIPE DYETHQLRQA

Product Science Overview

Structure and Function

COMP is a pentameric protein, meaning it consists of five identical subunits. Each subunit is composed of several domains, including an N-terminal coiled-coil domain, four EGF-like domains, seven TSP type 3 repeats, and a C-terminal globular domain . This structure allows COMP to interact with various matrix components and cell surface receptors, facilitating the assembly and stabilization of the cartilage matrix.

Expression and Production

Recombinant human COMP is often produced using HEK293 cells, a human embryonic kidney cell line. This expression system is preferred due to its ability to perform post-translational modifications similar to those in human cells, ensuring the recombinant protein’s functionality and stability . The recombinant protein is typically purified to a high degree of purity (>90%) and is suitable for various applications, including SDS-PAGE and Western blotting .

Biological Significance

COMP is essential for cartilage homeostasis and is involved in several physiological processes:

  • Matrix Assembly: COMP interacts with collagen fibers, promoting their assembly and stabilization within the cartilage matrix .
  • Cell-Matrix Interactions: COMP binds to cell surface integrin receptors, mediating the interaction between chondrocytes (cartilage cells) and the extracellular matrix .
  • Mechanical Properties: By contributing to the structural integrity of cartilage, COMP helps maintain the tissue’s mechanical properties, which are crucial for joint function .
Clinical Relevance

Alterations in COMP expression or mutations in the COMP gene can lead to various skeletal disorders, including:

  • Pseudoachondroplasia: A genetic disorder characterized by short stature and joint abnormalities due to mutations in the COMP gene .
  • Multiple Epiphyseal Dysplasia: A condition affecting the growth and development of the epiphyses (ends of long bones), also linked to COMP mutations .
Research and Applications

Recombinant human COMP is widely used in research to study cartilage biology and related diseases. It serves as a valuable tool for:

  • Investigating Cartilage Disorders: Understanding the molecular mechanisms underlying cartilage-related diseases and developing potential therapeutic strategies .
  • Drug Development: Screening and evaluating compounds that may modulate COMP function or expression, offering potential treatments for cartilage disorders .

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