Human Recombinant MMP12 proteinCatalytic Domain (V2LY-0526-LY5612)

Name: Human Recombinant MMP12 proteinCatalytic Domain
SKU: V2LY-0526-LY5612
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

E. coli

Protein Species

Human

Protein Construction

This product is Human Recombinant MMP12 proteinCatalytic Domain consist of Amino Acid: 106-268 and predicts a molecular mass of 18.2 kDa.

Molecule Mass

18.2 kDa

Protein Domain

Catalytic Domain

Sequence

Amino Acid: 106-268

Species

Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity

>90% as determined by SDS-PAGE

Endotoxin

Please contact us for more information.

Format

Lyophilized

Reconstitution

Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.

Buffer

Lyophilized from sterile PBS

Preservative

None

Storage

Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it 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.

More Infomation

Target

Full Name

Matrix Metallopeptidase 12

Function

May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.

Biological Process

Bronchiole development Source: Ensembl
Cellular response to virus Source: Ensembl
Collagen catabolic process Source: GO_Central
Elastin catabolic process Source: ARUK-UCL
Extracellular matrix disassembly Source: Reactome
Extracellular matrix organization Source: GO_Central
Lung alveolus development Source: Ensembl
Negative regulation of endothelial cell-matrix adhesion via fibronectin Source: ARUK-UCL
Negative regulation of transcription by RNA polymerase II Source: Ensembl
Negative regulation of type I interferon-mediated signaling pathway Source: Ensembl
Positive regulation of epithelial cell proliferation involved in wound healing Source: BHF-UCL
Positive regulation of interferon-alpha production Source: Ensembl
Positive regulation of transcription by RNA polymerase II Source: CAFA
Positive regulation of type I interferon-mediated signaling pathway Source: Ensembl
Protein import into nucleus Source: CAFA
Proteolysis Source: CAFA
Regulation of defense response to virus by host Source: Ensembl
Response to amyloid-beta Source: ARUK-UCL
Wound healing, spreading of epidermal cells Source: BHF-UCL

Cellular Location

Extracellular matrix

Kuntschar, S., Cardamone, G., Klann, K., Bauer, R., Meyer, S. P., Raue, R., ... & Schmid, T. (2023). Mmp12 Is Translationally Regulated in Macrophages during the Course of Inflammation. International Journal of Molecular Sciences, 24(23), 16981.

Cárcel-Márquez, J., Cullell, N., Muiño, E., Gallego-Fabrega, C., Lledós, M., Ibañez, L., ... & Fernandez-Cadenas, I. (2021). Causal effect of MMP-1 (matrix metalloproteinase-1), MMP-8, and MMP-12 levels on ischemic stroke: a Mendelian randomization study.

Gao, H., Zhou, X., Li, H., Liu, F., Zhu, H., Song, X., ... & Lu, J. (2021). Role of matrix metallopeptidase 12 in the development of hepatocellular carcinoma. Journal of Investigative Surgery, 34(4), 366-372.

Nighot, M., Ganapathy, A. S., Saha, K., Suchanec, E., Castillo, E. F., Gregory, A., ... & Nighot, P. (2021). Matrix metalloproteinase MMP-12 promotes macrophage transmigration across intestinal epithelial tight junctions and increases severity of experimental colitis. Journal of Crohn's and Colitis, 15(10), 1751-1765.

Mohan, A., Neequaye, N., Malur, A., Soliman, E., McPeek, M., Leffler, N., ... & Thomassen, M. J. (2020). Matrix metalloproteinase-12 is required for granuloma progression. Frontiers in Immunology, 11, 553949.

Yang, H., Zhang, C., Wu, J., Xiao, W., Xie, X., Zeng, Z., ... & Huang, Q. (2020). Association of matrix metalloproteinase-12 polymorphisms with chronic obstructive pulmonary disease risk: A protocol for systematic review and meta analysis. Medicine, 99(31).

Lulińska, E., Gibbon, A., Kaczmarczyk, M., Maciejewska-Skrendo, A., Ficek, K., Leońska-Duniec, A., ... & Sawczuk, M. (2020). Matrix metalloproteinase genes (Mmp1, mmp10, mmp12) on chromosome 11q22 and the risk of non-contact anterior cruciate ligament ruptures. Genes, 11(7), 766.

Toczek, J., Bordenave, T., Gona, K., Kim, H. Y., Beau, F., Georgiadis, D., ... & Devel, L. (2019). Novel matrix metalloproteinase 12 selective radiotracers for vascular molecular imaging. Journal of medicinal chemistry, 62(21), 9743-9752.

Li, B., Hu, L., Xue, Y., Yang, M., Huang, L., Zhang, Z., ... & Deng, G. (2019). Prediction of matrix metal proteinases-12 inhibitors by machine learning approaches. Journal of Biomolecular Structure and Dynamics, 37(10), 2627-2640.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

For research use only. Not intended for any clinical use.

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