Human Matrix Metalloproteinase 2, Active Protein, Cat#RPU60100
SDS-PAGE
MMP2 is a zinc-dependent enzymes capable of cleaving components of the extracellular matrix, which belongs to the matrix metalloproteinase (MMP) family .It is a gelatinase A, 72 kDa type IV collagenase which can hydrolyze gelatin under certain conditions. Gelatin zymography is mainly used for the detection of the gelatinases, MMP-2 and MMP-9 and It is extremely sensitive because levels of 10 pg of MMP-2 can already be detected .Briefly，various concentrations of MMP2 (50ng, 25ng, 13ng, 6.5ng, 3.3ng, 1.7ng) were denatured by SDS loading buffer, electrophoresed through sodium dodecylsulphate–polyacrylamide gel (SDS–PAGE; 10% gels) containing gelatin (1 mg/ml) with nonreducing conditions. After renaturation, incubation and CCB-stained, active MMP2 would hydrolyze gelatin nearby, which was indicated by the white binds on the gel. In this experiment we use trypsin as positive control. The result was shown.
The activity of recombinant human MMP2 is also measured by its ability to cleave a fluorogenic peptide substrate MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. The rhMMP2 is diluted to 100 ug/ml in assay buffer, then activated by p-aminophenylmercuric acetate (APMA) in a final concentration of 1 mM incubated at 37 °C for 1 hours. The activated rhMMP2 is diluted to 2.5 ug/mL in assay buffer. Loading into a black well plate 50 uL of 2.5 ug/mL rhMMP2 and start the reaction by adding 50 uL of 20 uM substrate, with a substrate blank containing 50 uL assay buffer, 50 uL substrate, and no rhMMP2. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant human MMP2 is > 170 pmol/min/ug.
Roll over image to zoom in Click on image to zoom
Human Matrix Metalloproteinase 2, Active Protein, Cat#RPU60100 SDS-PAGE MMP2 is a zinc-dependent enzymes capable of cleaving components of the extracellular matrix, which belongs to the matrix metalloproteinase (MMP) family .It is a gelatinase A, 72 kDa type IV collagenase which can hydrolyze gelatin under certain conditions. Gelatin zymography is mainly used for the detection of the gelatinases, MMP-2 and MMP-9 and It is extremely sensitive because levels of 10 pg of MMP-2 can already be detected .Briefly，various concentrations of MMP2 (50ng, 25ng, 13ng, 6.5ng, 3.3ng, 1.7ng) were denatured by SDS loading buffer, electrophoresed through sodium dodecylsulphate–polyacrylamide gel (SDS–PAGE; 10% gels) containing gelatin (1 mg/ml) with nonreducing conditions. After renaturation, incubation and CCB-stained, active MMP2 would hydrolyze gelatin nearby, which was indicated by the white binds on the gel. In this experiment we use trypsin as positive control. The result was shown. The activity of recombinant human MMP2 is also measured by its ability to cleave a fluorogenic peptide substrate MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. The rhMMP2 is diluted to 100 ug/ml in assay buffer, then activated by p-aminophenylmercuric acetate (APMA) in a final concentration of 1 mM incubated at 37 °C for 1 hours. The activated rhMMP2 is diluted to 2.5 ug/mL in assay buffer. Loading into a black well plate 50 uL of 2.5 ug/mL rhMMP2 and start the reaction by adding 50 uL of 20 uM substrate, with a substrate blank containing 50 uL assay buffer, 50 uL substrate, and no rhMMP2. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant human MMP2 is > 170 pmol/min/ug.

Human Matrix Metalloproteinase 2, Active Protein

BiomatikSKU: RPU60100-50ug
Size: 50ug
Request Information
!

This item is non-returnable unless there is a quality issue. See Returns Policy
Product Details

Technical Docs

Images

Description

Technical Documents

PDF icon Safety Data Sheet

Images

SDS-PAGE
MMP2 is a zinc-dependent enzymes capable of cleaving components of the extracellular matrix, which belongs to the matrix metalloproteinase (MMP) family .It is a gelatinase A, 72 kDa type IV collagenase which can hydrolyze gelatin under certain conditions. Gelatin zymography is mainly used for the detection of the gelatinases, MMP-2 and MMP-9 and It is extremely sensitive because levels of 10 pg of MMP-2 can already be detected .Briefly，various concentrations of MMP2 (50ng, 25ng, 13ng, 6.5ng, 3.3ng, 1.7ng) were denatured by SDS loading buffer, electrophoresed through sodium dodecylsulphate–polyacrylamide gel (SDS–PAGE; 10% gels) containing gelatin (1 mg/ml) with nonreducing conditions. After renaturation, incubation and CCB-stained, active MMP2 would hydrolyze gelatin nearby, which was indicated by the white binds on the gel. In this experiment we use trypsin as positive control. The result was shown.
The activity of recombinant human MMP2 is also measured by its ability to cleave a fluorogenic peptide substrate MCA-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 in the assay buffer 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5. The rhMMP2 is diluted to 100 ug/ml in assay buffer, then activated by p-aminophenylmercuric acetate (APMA) in a final concentration of 1 mM incubated at 37 °C for 1 hours. The activated rhMMP2 is diluted to 2.5 ug/mL in assay buffer. Loading into a black well plate 50 uL of 2.5 ug/mL rhMMP2 and start the reaction by adding 50 uL of 20 uM substrate, with a substrate blank containing 50 uL assay buffer, 50 uL substrate, and no rhMMP2. Then read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes. The specific activity of recombinant human MMP2 is > 170 pmol/min/ug.

Let customers speak for us

from 218 reviews

We were very pleased with Biomatik’s performance on a custom recombinant protein project earlier this summer. Communication throughout the project was excellent, technical questions were addressed promptly, and the supporting analytical and QC data were clear and comprehensive. The recombinant protein was produced to the requested specifications and delivered on schedule. Based on this experience, we have chosen Biomatik for an additional custom protein production project and would be pleased to work with them again.

Thomas Hatch

We have been ordering several proteins for our research. Biomatik always delivered very good products, and the service was very reliable. Their customer service has always been very responsive and professional. We are very satisfied with this company.

Davide Z

A reliable antibody and peptide synthesis company. We’ve been using Biomtik for polyconal antibodies in our research. Turnaround times are consistent, and communication is always clear and professional.

Hsing Yi Cho

We’ve been using Biomtik for peptide synthesis in our research, and they have proven to be extremely reliable. Turnaround times are consistent, product quality is excellent, and communication is always clear and professional. Highly recommend their services to any lab looking for dependable peptide synthesis.

Tarring Lu

Biomatik provided excellent support to our Biometrology team at NPL, with timely and reliable protein production services. The quality of the material delivered was to the expected standards, and the communication throughout the project was smooth and efficient.

Andrei Baluna

We got help from Biomatik for our studies, and the experience was excellent. The customer support team was responsive and knowledgeable, providing detailed documentation and timely updates throughout the process. We appreciate the reliable quality and professional service, and we look forward to working with Biomatik again for further.

Keyao Yu

I work on molecular farming, producing recombinant protein in plant suspention cells. I'm completely satisfied after almost 5 years ordering antibidies at Biomatik. Perfect reproducibility batch after batch and I hope to continiue like this!

Eduardo Peña

We have ordered peptides from Biomatik several times. Their quality is excellent and they work with you every step of the way to ensure a quality product.

A G

Estoy muy satisfecha con los servicios de síntesis de péptidos de Biomatik. Para mí como investigadora, Biomatik cumplió todas mis expectativas técnicas para realizar mi trabajo experimental. Toda su atención es buena!

Cristina Cevallos

We have purchased peptides from Biomatik for a few years now. Their ordering process was smooth, customer service was responsive and helpful, and the peptides arrived on time and of great quality.

Jeella Acedo

Great service. I'm a returning customer. The product quality and timeline are both outstanding.

Yue Home Liu

We have used Biomatik to generate two different antibodies and in both cases they worked extremely well in all the assays we tested, including ELISA, WB, and IFA. I would recommend this company.

Sarah Wootton

The peptide product is of exceptional quality and is highly recommended for its efficacy.

Haoyang Xin

I have been using Biomatik's modified peptides for a while and they deliver high quality peptides and a very good technical support

Roi Asor

I have bought peptides from Biomatic several times and the quality is the best!!!

Kyung Won Park

Recently viewed