Rabbit Anti-MMP12 Recombinant Antibody (RM381) (CBMAB-BR356LY)

Name: Rabbit Anti-MMP12 Recombinant Antibody (RM381)
SKU: CBMAB-BR356LY
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

Host Animal

Rabbit

Clone

RM381

Application

IHC: 1:300-1:500 dilution, WB: 0.1-0.5 μg/ml

Immunogen

A peptide corresponding to C-terminus of human Matrix metalloproteinase-12 (MMP-12)

Specificity

Human

Antibody Isotype

IgG

Clonality

Monoclonal

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format

Liquid

Buffer

50% glycerol, 1% BSA

Preservative

0.09% sodium azide

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

More Infomation

Target

Full Name

Matrix Metallopeptidase 12

Introduction

This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). Proteins in this family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. The encoded preproprotein is proteolytically processed to generate the mature protease. This protease degrades soluble and insoluble elastin. This gene may play a role in aneurysm formation and mutations in this gene are associated with lung function and chronic obstructive pulmonary disease (COPD). This gene is part of a cluster of MMP genes on chromosome 11. [provided by RefSeq, Jan 2016]

Entrez Gene ID

4321

UniProt ID

P39900

Alternative Names

Macrophage metalloelastase;MME;3.4.24.65;Macrophage elastase;ME;hME;Matrix metalloproteinase-12;MMP-12;MMP12;HME;

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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