Recombinant Human Leukocyte Cell-Derived Chemotaxin 1 (CNMD) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-08198P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Leukocyte Cell-Derived Chemotaxin 1 (CNMD) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-08198P
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Product Overview

Description Recombinant Human Leukocyte Cell-Derived Chemotaxin 1 (CNMD) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb O75829
Target Symbol CNMD
Synonyms BRICD3; BRICHOS domain containing 3; CH-SP; CHM I; ChM-I; CHM1; chondromodulin; Chondromodulin I; Chondromodulin-1; Chondromodulin-I; Chondrosurfactant protein; LECT 1; Lect1; LECT1_HUMAN; Leukocyte cell derived chemotaxin 1; Multiple myeloma tumor suppressor 1; MYETS1
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence EVVRKIVPTTTKRPHSGPRSNPGAGRLNNETRPSVQEDSQAFNPDNPYHQQEGESMTFDPRLDHEGICCIECRRSYTHCQKICEPLGGYYPWPYNYQGCRSACRVIMPCSWWVARILGMV
Expression Range 215-334aa
Protein Length Partial
Mol. Weight 29.8kDa
Research Area Cancer
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Bifunctional growth regulator that stimulates the growth of cultured chondrocytes in the presence of basic fibroblast growth factor (FGF) but inhibits the growth of cultured vascular endothelial cells. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage by bone during endochondral bone development. Inhibits in vitro tube formation and mobilization of endothelial cells. Plays a role as antiangiogenic factor in cardiac valves to suppress neovascularization.
Subcellular Location [Chondromodulin-1]: Secreted, extracellular space, extracellular matrix. Note=Accumulated in the inter-territorial matrix of cartilage.; [Chondrosurfactant protein]: Endomembrane system; Single-pass membrane protein.
Protein Families Chondromodulin-1 family
Database References

HGNC: 17005

OMIM: 605147

KEGG: hsa:11061

STRING: 9606.ENSP00000367198

UniGene: PMID: 28983591

  • CHM1 seems to have pleiotropic functions in Ewing sarcoma. PMID: 28319320
  • The results of the present study indicated that ChMI was able to inhibit the growth of breast cancer cells; thus suggesting that ChM-I may have potential clinical applications in the treatment of breast cancer. PMID: 27035228
  • Data suggest ChM1 as potential tumor suppressor in gastric cancer and useful biomarker for the treatment and prognosis. Its expression was downregulated in cancer tissue, and correlated with advanced stages, lymph node metastasis, and poorer prognosis. PMID: 26165347
  • intact 20-25 kDa ChM-I is stored as a component of extracellular matrix in the avascular cartilage zones, but it is inactivated by a single N-terminal proteolytic cleavage in the hypertrophic zone of growth-plate cartilage PMID: 24710035
  • the inner meniscus contained larger amounts of ChM-I, and that the inner meniscus-derived ChM-I inhibited endothelial cell proliferation. PMID: 23143879
  • Degenerative intervertebral disc cells express ChM-I. Administration of bFGF down-regulates the expression of ChM-I. Expression is correlated with the degree of degeneration. PMID: 22041680
  • Inhibition of YY1 in combination with forced expression of p300 and Sp3 restored the expression of ChM-I in cells with a hypomethylated promoter region, but not in cells with hypermethylation. PMID: 20663886
  • Data suggest that chondromodulin-I impairs the VEGF-A-stimulated motility of endothelial cells by destabilizing lamellipodial extensions. PMID: 20026108
  • Methylation in the core-promoter region of the chondromodulin-I gene determines the cell-specific expression by regulating the binding of transcriptional activator Sp3 PMID: 15107420
  • chondromodulin-I has a pivotal role in maintaining valvular normal function by preventing angiogenesis that may lead to valvular heart diseases PMID: 16980969
  • Cell-specific epigenetic regulation of ChM-I gene expression PMID: 17980151
  • new hypoxia-inducible and SOX9-regulated genes, Gdf10 and Chm-I. In addition, Mig6 and InhbA were induced by hypoxia, predominantly via HIF-2alpha PMID: 18077449
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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