Recombinant Human MMP2

• Cat.No.: MMP2-408H

Specification

• Cat. No.: MMP2-408H
• Description: Matrix metallopeptidase 2, also known as MMP2, is an enzyme 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. Most MMP"s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP-2 degrades type IV collagen, the major structural component of basement membranes and plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. MMP2 has been found to be associated with tumor invasion in various cancers.
• Source: Mammalian cells
• Sequence: The DNA sequence encoding the Pro human MMP-2 enzyme was expressed in NSO cells.
• Purity: >90% by SDS Page and analyzed by silver stain.
• Endotoxin: <1.0 EU/µg as determined by the LAL method.
• Biological Activity: The biological activity of Human MMP-2 was determined by its ability to cleave a fluorogenic peptide substrate, (7-methoxycoumarin-4-yl) Acetyl-Pro-Leu-Gly-Leu- (3-[2, 4-dinitrophenyl-L-2, 3-diaminopropionyl)-Ala-Arg-NH2. The specific activity, measured under the described conditions, is >1,000 pmoles/min/μg.
• Storage: This lyophilized protein is stable for six to twelve months when stored desiccated at -20℃ to -70℃. After aseptic reconstitution, this protein may be stored at 2℃ to 8℃ for one month or at -20℃ to -70℃ in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
• Tag: Non

Gene Information

• Gene Name: MMP2 matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase) [ Homo sapiens ]
• Synonyms: MMP2; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); CLG4; MONA; CLG4A; TBE-1; MMP-II; EC 3.4.24.24; MMP-2 ; 72 kDa gelatinase; Gelatinase A; Matrix metalloproteinase-2; collagenase type IV-A; matrix metalloproteinase 2; matrix metalloproteinase 2 (gelatinase A, 72kD gelatinase; 72kDa type IV collagenase); matrix metalloproteinase-II; neutrophil gelatinase
• Gene ID: 4313
• mRNA Refseq: NM_001127891
• Protein Refseq: NP_001121363
• MIM: 120360
• UniProt ID: P08253
• Chromosome Location: 16q13-q21
• Pathway: Bladder cancer; GnRH signaling pathway; Leukocyte transendothelial migration; Pathways in cancer; Diabetes pathways
• Function: calcium ion binding; metalloendopeptidase activity; peptidase activity; protein binding; zinc ion binding

Reviews

06/19/2021

The solubility and ion exchange ability are very good, which is convenient for subsequent experimental treatment and purification.

05/13/2021

Kinetic parameters such as enzymatic reaction rate and binding affinity were tested in the early stage, and it was found that the protein performed well.

03/16/2021

MMP2 products undergo strict quality control to ensure the consistency and stability of each batch.

Q&As

How to regulate the activity of MMP2 in tumor therapy?

The activity of MMP2 is regulated by inhibitors and antibodies against it to inhibit tumor metastasis and invasion.

How is MMP2 related to metastases that promote disease progression?

MMP2 interacts with some transfer factors, such as VEGF and EGF, to promote tumor metastasis and invasion.

What are the application prospects of MMP2 inhibitors?

Inhibitors of MMP2 can be used as potential drug targets for the treatment of tumors, cardiovascular diseases and other related diseases.

Does MMP2 interact with the tumor microenvironment?

MMP2 interacts with tumor cells, immune cells, blood vessels, etc. in the tumor microenvironment to affect tumor progression and treatment effect.

What is the role of MMP2 in embryonic development?

It is involved in important processes such as morphogenesis, organ development and intraembryonic lymphatic vessel formation during embryonic development.

What are the effects of MMP2 mutations in human disease?

Mutations in MMP2 may affect its protein structure and function, leading to the occurrence and progression of related diseases.