Recombinant Human LECT1 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-3164

Recombinant Human LECT1 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLPSN-3164
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Product Overview

Tag Fc
Host Species Human
Accession NP_001011705.1
Description A DNA sequence encoding the human LECT1 (NP_001011705.1) (Glu215-Val333) was expressed with the Fc region of human IgG1 at the N-terminus.
Source HEK293
Predicted N Terminal Glu
AA Sequence Glu215-Val333
Molecular Weight The recombinant human LECT1 consists 379 a.a. and predicts a molecular mass of 42.1 kDa.
Purity >(81.7+13.6)% as determined by SDS-PAGE.
Endotoxin < 1.0 EU per μg protein as determined by the LAL method.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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
Tissue Specificity Detected in cartilage and cardiac valves (at protein level). Detected in the laminae fibrosa, spongiosa and ventricularis layers of normal cardiac valves (at protein level). Expression is decreased cardiac valves of patients with valvular heart disease (a

Gene Functions References

  1. ChMI directly suppressed the proliferation and growth of osteosarcoma cells. PMID: 28983591
  2. CHM1 seems to have pleiotropic functions in Ewing sarcoma. PMID: 28319320
  3. 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
  4. 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
  5. 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
  6. the inner meniscus contained larger amounts of ChM-I, and that the inner meniscus-derived ChM-I inhibited endothelial cell proliferation. PMID: 23143879
  7. 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
  8. 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
  9. Data suggest that chondromodulin-I impairs the VEGF-A-stimulated motility of endothelial cells by destabilizing lamellipodial extensions. PMID: 20026108
  10. 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
  11. chondromodulin-I has a pivotal role in maintaining valvular normal function by preventing angiogenesis that may lead to valvular heart diseases PMID: 16980969
  12. Cell-specific epigenetic regulation of ChM-I gene expression PMID: 17980151
  13. 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


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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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