Analytical Data
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Gene name
MMP8
- Application
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Alternative Names
MMP8;CLG1;Neutrophil 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
P22894
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Expression Region
101-467aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSLTPGNPKWERTNLTYRIRNYTPQLSEA EVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPN GILAHAFQPGQGIGGDAHFDAEETWTNTSANYNLFLVAAHEFGHSLGLAH SSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYGLSSNPIQPTGPSTPK PCDPSLTFDAITTLRGEILFFKDRYFWRRHPQLQRVEMNFISLFWPSLPT GIQAAYEDFDRDLIFLFKGNQYWALSGYDILQGYPKDISNYGFPSSVQAI DAAVFYRSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGIESKVDAV FQQEHFFHVFSGPRYYAFDLIAQRVTRVARGNKWLNCRYG
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Molecular Weight
44 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 8 (MMP-8), also known as collagenase-2, is a crucial enzyme in the matrix metalloproteinase family, primarily involved in the degradation of collagen and other extracellular matrix components. This enzyme plays a significant role in various physiological processes, including tissue remodeling, wound healing, and inflammation. Its dysregulation is associated with a range of pathological conditions, including arthritis, cancer metastasis, and cardiovascular diseases. Research on MMP-8 has gained momentum due to its potential as a therapeutic target and biomarker for disease progression. The recombinant expression of MMP-8 allows for the production of this protein in a purified form, facilitating studies on its structure-function relationships, regulatory mechanisms, and inhibitors. Such studies are essential for understanding the detailed role of MMP-8 in health and disease and for developing novel therapeutic strategies that may involve MMP-8 modulation. Advances in recombinant DNA technology have enabled researchers to produce active MMP-8 with significant yields, further encouraging investigations into its biochemical properties and potential applications in clinical settings. As a result, MMP-8 continues to be a focus of research aimed at unraveling the complexities of extracellular matrix dynamics and developing targeted interventions for related diseases.
