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MMP-8 / CLG1 Protein (Native) PDF Download

Catalog Size (Price) Quantity In Stock Operation Other Information
10254-HNAH
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Matrix Metalloproteinase-8 ( MMP-8 / CLG1 ) Protein

 

MMP8 / CLG1 Protein Price Inquiry ( Available Sizes )

MMP8 / CLG1 Protein Product Information

Synonym :

MMP8 ,  CLG1,   HNC,   MMP-8,   PMNL-CL

Protein Construction:

A DNA sequence encoding the pro form of human MMP8 ( NP_002415.1 ) ( Phe 21 - Gly 467 ) was expressed and purified, with an initial Met at the N-terminus

Source: Human
Expression Host: Human Cells

MMP8 / CLG1 Protein QC Testing

Purity: > 92 % as determined by SDS-PAGE SDS-PAGE:
MMP-8 protein

MMP-8 protein

Bio-activity:

Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 ( R&D Systems, Catalog # ES001 )
The specific activity is  >  250 pmoles / min / µg

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
Stability: Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal: Met
Molecular Mass:

The recombinant human MMP8 consisting of 448 amino acids and has a calculated molecular mass of 52 kDa. It migrates as an approximately 65 kDa band in SDS-PAGE under reducing conditions

Formulation: Lyophilized from sterile PBS , pH 7.4
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.

MMP8 / CLG1 Protein Usage Guide

Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

MMP8 / CLG1 Protein Related Products & Topics

Related Areas:

Enzyme>>Protease & Regulator>>Metalloprotease & Regulator>>Matrix Metalloproteinase>>MMP-8/MMP8

Cancer>>Angiogenesis>>Matrix Metalloproteinase>>MMP-8/MMP8

Proteins:

Molecule Species Description //For Detailed Info. and Price------CLICK! Cat. No
MMP-8/MMP8 Human MMP-8/MMP8 Protein, Recombinant 10254-H08H
MMP-8/MMP8 Human MMP-8/MMP8 Protein, Recombinant 10254-HNAH
MMP-8/MMP8 Mouse MMP-8/MMP8 Protein, Recombinant 50493-MNAH

Antibodies:

Molecule Application Description //For Detailed Info. and Price------CLICK! Cat. No
Human
MMP-8/MMP8
WB, ELISA MMP-8/MMP8 Antibody, Rabbit PAb 10254-RP01
Human
MMP-8/MMP8
WB, ELISA MMP-8/MMP8 Antibody, Rabbit PAb (Antigen Affinity Purified) 10254-RP02

MMP8 / CLG1 Protein Description

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. Neutrophil collagenase, also known as Matrix metalloproteinase-8, MMP-8, and CLG1, is a member of the peptidase M10A family. MMP-8 may affect the metastatic behaviour of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 in the tumour may have a protective effect against lymph node metastasis. MMP-8 may affect the metastatic behaviour of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 participates in wound repair by contributing to the resolution of inflammation and open the possibility to develop new strategies for treating wound healing defects.

References

  1. Belotti, D. et al., 2003, Cancer. Res. 63: 5224-9.
  2. Mira, E. et al., 2004, J. Cell. Sci. 117:1847-57.
  3. Ram, M. et al., 2006, J. Clin. Immunol. 26: 299-307.
  4. Gutiérrez-Fernández, A. et al., 2007, FASEB J. 21 (10): 2580-91.
  5. Decock, J. et al., 2008, BMC Cancer. 8 :77.
  6. Laxton,R.C. et al., 2009, Circ Res.105 (9): 921-9.