Recombinant Mouse Cartilage oligomeric matrix protein(Comp)

Code CSB-YP005778MO
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Source Yeast
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Code CSB-EP005778MO
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Source E.coli
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Code CSB-EP005778MO-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP005778MO
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Source Baculovirus
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Code CSB-MP005778MO
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names Comp
Uniprot No. Q9R0G6
Alternative Names CompCartilage oligomeric matrix protein; COMP
Species Mus musculus (Mouse)
Expression Region 20-755
Target Protein Sequence Q GQIPLGGDLA PQMLRELQET NAALQDVREL LRQQVKEITF LKNTVMECDA CGMQPARTPG LSVRPVPLCA PGSCFPGVVC SETATGARCG PCPPGYTGNG SHCTDVNECN AHPCFPRVRC INTSPGFHCE ACPPGFSGPT HEGVGLTFAK SNKQVCTDIN ECETGQHNCV PNSVCVNTRG SFQCGPCQPG FVGDQTSGCQ RRGQHFCPDG SPSPCHEKAN CVLERDGSRS CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED VDRDGIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDSD KWGDACDNCR SKKNDDQKDT DLDGRGDACD DDIDGDRIRN VADNCPRVPN FDQSDSDGDG VGDACDNCPQ KDNPDQRDVD HDFVGDACDS DQDQDGDGHQ DSRDNCPTVP NSAQQDSDHD GKGDACDDDD DNDGVPDSRD NCRLVPNPGQ EDNDRDGVGD ACQGDFDADK VIDKIDVCPE NAEVTLTDFR AFQTVVLDPE GDAQIDPNWV VLNQGMEIVQ TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG YQDSSSFYVV MWKQMEQTYW QANPFRAVAE PGIQLKAVKS STGPGEQLRN ALWHTGDTAS QVRLLWKDPR NVGWKDKTSY RWFLQHRPQV GYIRVRFYEG PELVADSNVV LDTAMRGGRL GVFCFSQENI IWANLRYRCN DTIPEDYESH RLQRV
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Data

Function May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity).
Gene References into Functions
  1. COMP could normally have a protective role against PASMC phenotype switching PMID: 28860005
  2. these findings revealed the essential role of COMP in retarding the development of vascular aging and vascular smooth muscle cell senescence. PMID: 27498005
  3. COMP deficiency drove macrophages toward the atherogenic phenotype and thereby aggravated atherosclerotic calcification. PMID: 27151399
  4. COMP forms a complex with collagens intracellularly that is a prerequisite for collagen secretion. PMID: 26746240
  5. The accumulation and thereby the functionality of thrombospondin in extracellular matrix is controlled by concentration-dependent, intermolecular "matrix trapping" mechanism. PMID: 25995382
  6. COMP deficiency shortened tail-bleeding and clotting time and accelerated ferric-chloride-induced thrombosis. COMP specifically inhibited thrombin-induced platelet aggregation, activation, and retraction and the thrombin-mediated cleavage of fibrinogen. PMID: 26045608
  7. COMP immunoreactivity was observed in about half of the investigated plaques from the ApoE null mice, mainly located along the intima-medial border. Plaques in the brachiocephalic artery from ApoE mice lacking COMP were increased in size with 54%. PMID: 25133350
  8. study will facilitate better awareness of the differential diagnoses that might be associated with the PSACH/MED spectrum and subsequent care of PSACH/MED patients PMID: 24312420
  9. The lack of arthritis, together with high levels of COMP-specific antibodies, in COMP-deficient mice indicates that susceptibility to arthritis is COMP specific and that endogenous expression of COMP in wild-type mice tolerizes B cells in vivo. PMID: 23754310
  10. results imply that COMP is not a key upstream mediator of the anabolic effects of ML on the skeleton. PMID: 23098652
  11. Lack of COMP and matrilin 3 leads to increased deposition of TIMP-3, which causes partial inactivation of matrix metalloproteinases in bone, including MMP-13. PMID: 22378539
  12. A novel form of chondrocyte stress triggered by the expression of a human-like mutation in COMP is central to the pathogenesis of pseudoachondroplasia. PMID: 22006726
  13. reducing steady state levels of COMP mRNA alleviates intracellular retention of other extracellular matrix proteins associated with the pseudoachondroplasia cellular pathology PMID: 20421976
  14. Data show that cartilage oligomeric matrix protein (COMP) promotes cell attachment via independent mechanisms involving cell surface CD47 and alphaVbeta3 integrin and that cell attachment to COMP induces formation of fascin-stabilized actin microspikes. PMID: 20033473
  15. Cartilage oligomeric matrix protein-deficient mice have normal skeletal development. PMID: 12024046
  16. Comp was expressed in tendon clone cells. PMID: 12837285
  17. Negative regulation of transcription is an important mechanism for chondrocyte-specific expression of the COMP gene PMID: 15183430
  18. ADAMTS-7 is the first metalloproteinase found to bind directly to and degrade COMP PMID: 16585064
  19. COMP appears to be required for granulin PC cell-derived growth factor-mediated chondrocyte proliferation PMID: 17307734
  20. a mutation in the C-terminal domain of COMP exerts a dominant-negative effect on both intra- and extracellular processes. PMID: 17588960
  21. contribution of COMP to the phenotype of mice deficient in both collagen IX and COMP appears minor, even though clear differences in the deposition of matrilin-3 were detected PMID: 18191556
  22. COMP-deficient mice develop an early onset collagen-induced arthritis and more severe arthritis during the chronic phase. PMID: 19014566

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Subcellular Location Secreted, extracellular space, extracellular matrix
Protein Families Thrombospondin family
Tissue Specificity Expressed only in cartilage, including nasal, knee epiphyseal and rib tissues.
Database Links

KEGG: mmu:12845

STRING: 10090.ENSMUSP00000003659

UniGene: Mm.45071

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