Recombinant Human MMP2 Protein

Name: Recombinant Human MMP2 Protein
Brand: Beta LifeScience
SKU: BLPSN-3385
Availability: InStock

Collections: Enzymes, Protease, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	NP_004521.1
Synonym	CLG4, CLG4A, MMP-2, MMP-II, MONA, TBE-1
Background	Matrix Metalloproteinase-2 (MMP-2) is an enzyme that degrades components of the extracellular matrix and thus plays a pivotal role in cell migration during physiological and pathological processes. MMP-2 expression is dependent on extracellular matrix metalloproteinase inducer (EMMPRIN), Her2/neu, growth factors, cytokines, and hormones. Pro-MMP-2 activation needs MT1-MMP and TIMP-2 contribution. MMP-2 is changed in distribution and increased in amount in the ventral cochlear nucleus after unilateral cochlear ablation. A low level of MMP-2 is linked to favorable prognosis in patients with a hormone receptor-negative tumor, usually associated with high risk. As a zymogen requiring proteolytic activation for catalytic activity, MMP-2 has been implicated broadly in the invasion and metastasis of many cancer model systems, including human breast cancer (HBC). Blocking MMP-2 secretion and activation during breast carcinoma development may decrease metastasis. The detection of active MMP-2 alone or the rate of pro-MMP-2 and active MMP-2 is considered a very sensitive indicator of cancer metastasis. Modulation of MMP-2 expression and activation through specific inhibitors and activators may thus provide a new mechanism for breast cancer treatment.
Description	A DNA sequence encoding the native human MMP2 (NP_004521.1) (Met 1-Cys 660) was expressed and purified.
Source	HEK293
Predicted N Terminal	Ala 30
AA Sequence	Met 1-Cys 660
Molecular Weight	The recombinant human MMP2 consists of 631 a.a. and migrates as an 72 kDa band as predicted in SDS-PAGE under reducing conditions.
Purity	>(74.7+17.3)% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	1. Measured by its ability to cleave the fluorogenic peptide substrate Mca-PLGL-Dpa-AR-NH2 (AnaSpec, Catalog # 27076). The specific activity is > 1,000 pmoles/min/µg.2. Measured by its binding ability in a functional ELISA.3. Immobilized human MMP2 at 10 ug/mL (100 ul/well) can bind- human TIMP2/Fc. The EC50 of human TIMP2/Fc is 0.02 ug/mL.(Activation description: The proenzyme needs to be activated by APMA for an activated form)
Formulation	Lyophilized from sterile 0.05 % Brij-35, 150 mM NaCl, 5 mM CaCl2, 50 mM Tris, pH 7.5..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein 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.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.