Mouse Recombinant MMP8 protein (V2LY-0526-LY8678)

Name: Mouse Recombinant MMP8 protein
SKU: V2LY-0526-LY8678
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

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

Basic Information

Expressed Host

HEK293 Cells

Protein Species

Mouse

Protein Construction

This product is Mouse Recombinant MMP8 protein consist of Amino Acid: 21-465 and predicts a molecular mass of 52 kDa.

Molecule Mass

52 kDa

Sequence

Amino Acid: 21-465

Species

Mouse

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

Purity

>85% 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 8

Function

Can degrade fibrillar type I, II, and III collagens.

Biological Process

Collagen catabolic process Source: GO_Central
Endodermal cell differentiation Source: UniProtKB
Extracellular matrix disassembly Source: Reactome
Extracellular matrix organization Source: GO_Central
Negative regulation of gene expression Source: ARUK-UCL
Negative regulation of interleukin-10 production Source: ARUK-UCL
Positive regulation of DNA binding Source: ARUK-UCL
Positive regulation of gene expression Source: ARUK-UCL
Positive regulation of interleukin-6 production Source: ARUK-UCL
Positive regulation of JNK cascade Source: ARUK-UCL
Positive regulation of MAPK cascade Source: ARUK-UCL
Positive regulation of microglial cell activation Source: ARUK-UCL
Positive regulation of neuroinflammatory response Source: ARUK-UCL
Positive regulation of NIK/NF-kappaB signaling Source: ARUK-UCL
Positive regulation of nitric oxide biosynthetic process Source: ARUK-UCL
Positive regulation of reactive oxygen species biosynthetic process Source: ARUK-UCL
Positive regulation of tumor necrosis factor production Source: ARUK-UCL
Proteolysis Source: UniProtKB
Regulation of microglial cell activation Source: ARUK-UCL
Regulation of neuroinflammatory response Source: ARUK-UCL

Cellular Location

Extracellular region or secreted
extracellular matrix
Other locations
Cytoplasmic granule
Note: Stored in intracellular granules.

Baidya, S. K., Banerjee, S., Guti, S., Jha, T., & Adhikari, N. (2024). Matrix metalloproteinase-8 (MMP-8) and its inhibitors: A minireview. European Journal of Medicinal Chemistry Reports, 100130.

Atanasova, T., Stankova, T., Bivolarska, A., & Vlaykova, T. (2023). Matrix Metalloproteinases in Oral Health—Special Attention on MMP-8. Biomedicines, 11(6), 1514.

Luchian, I., Goriuc, A., Sandu, D., & Covasa, M. (2022). The role of matrix metalloproteinases (MMP-8, MMP-9, MMP-13) in periodontal and peri-implant pathological processes. International Journal of Molecular Sciences, 23(3), 1806.

Umeizudike, K., Räisänen, I., Gupta, S., Nwhator, S., Grigoriadis, A., Sakellari, D., & Sorsa, T. (2022). Active matrix metalloproteinase‐8: A potential biomarker of oral systemic link. Clinical and Experimental Dental Research, 8(1), 359-365.

Goncharova, E. A., Kudryashova, T. V., Maroli, G., & Pullamsetti, S. S. (2021). Matrix Metalloproteinase-8 in Pulmonary Hypertension: The Sheep in the Wolf’s Skin?. American Journal of Respiratory and Critical Care Medicine, 204(12), 1361-1363.

Dieffenbach, P. B., Mallarino Haeger, C., Rehman, R., Corcoran, A. M., Coronata, A. M. F., Vellarikkal, S. K., ... & Fredenburgh, L. E. (2021). A novel protective role for matrix metalloproteinase-8 in the pulmonary vasculature. American Journal of Respiratory and Critical Care Medicine, 204(12), 1433-1451.

Forsblom, E., Tervahartiala, T., Ruotsalainen, E., Järvinen, A., & Sorsa, T. (2021). Matrix metalloproteinase MMP-8, TIMP-1 and MMP-8/TIMP-1 ratio in plasma in methicillin-sensitive Staphylococcus aureus bacteremia. Plos one, 16(5), e0252046.

Orozco-Páez, J., Rodríguez-Cavallo, E., Díaz-Caballero, A., & Méndez-Cuadro, D. (2021). Quantification of matrix metalloproteinases MMP-8 and MMP-9 in gingival overgrowth. The Saudi Dental Journal, 33(5), 260-267.

Wu, W., Peng, S., Shi, Y., Li, L., Song, Z., & Lin, S. (2021). NPY promotes macrophage migration by upregulating matrix metalloproteinase‐8 expression. Journal of Cellular Physiology, 236(3), 1903-1912.

Juurikka, K., S. Butler, G., Salo, T., Nyberg, P., & Åström, P. (2019). The role of MMP8 in cancer: a systematic review. International journal of molecular sciences, 20(18), 4506.

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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

Alternative Versions

Human Recombinant MMP8 protein (CAT#: V2LY-0526-LY5618)

Mouse Recombinant MMP8 protein, His Tag (CAT#: V2LY-0526-LY8679)

Human Recombinant MMP8 protein, His Tag (CAT#: V2LY-0526-LY5619)

Human Recombinant MMP8 protein, His Tag-1 (CAT#: V2LY-0526-LY5620)

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Mouse Recombinant MMP8 protein, His Tag (CAT#: V2LY-0526-LY8679)

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Human Recombinant MMP8 protein (CAT#: V2LY-0526-LY5618)

Isotype control

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

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