Analytical Data
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Gene name
MMP2
- Application
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Alternative Names
MMP2;CLG4A;72 kDa type IV collagenase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08253
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Expression Region
110-660aa
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AA Sequence
YNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRF SRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDD DELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWC STTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEG RTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNK YESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAM GLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTP TLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLV ATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSL GLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADA WNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLG C
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Molecular Weight
63 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Matrix metalloproteinase 2 (MMP2), a member of the matrix metalloproteinase family, plays a crucial role in the degradation of extracellular matrix components, particularly collagen. This enzyme is implicated in various physiological and pathological processes, including tissue remodeling, wound healing, and tumor invasion. Dysregulation of MMP2 activity has been associated with several diseases, such as cancer metastasis, cardiovascular diseases, and inflammatory disorders. The study of recombinant MMP2 has gained significant attention in recent years, as it offers insights into the enzyme's structure-function relationship and its potential as a therapeutic target. Recombinant protein technology enables the production of MMP2 in sufficient quantities for biochemical assays and functional studies, allowing researchers to investigate its enzymatic activity, regulation, and interactions with inhibitors. Additionally, understanding the mechanisms by which MMP2 contributes to disease progression could lead to the development of innovative therapeutic strategies aimed at modulating its activity. This research not only enhances our knowledge of MMP2's biological significance but also paves the way for clinical applications in treating conditions related to extracellular matrix remodeling.











