Specifications
- Pack type:Vial
- Conjugation:Unconjugated
- Protein/Peptide Type:Recombinant
- Source:E. coli
- Species:Mouse
- Size:50 µg
- Tag sequence:MGHHHHHHSGSEF
- Storage Conditions:−20 °C
- Endotoxin Content:<1.0 EU per 1 µg (determined by the LAL method)
- Gene ID:17387
- Reconstitution Instructions:Reconstitute in 10 mM PBS (pH 7.4) to a concentration of 0.1 - 1.0 mg/ml. Do not vortex.
- Endotoxin-free:N
- Carrier-Free:Y
- Protease-free:N
- Animal-Free:Y
- Protein Synonyms:Matrix Metalloproteinase 14
- UniProtKB:P53690
- Protein/Peptide Name:MMP14 (prokaryotic)
- Purity:90 - 100%
- Molecular Weight:44 kDa
- Sequence:His121~Asn487
- Endotoxin Level:Low
- Concentration:0.2 mg/ml
- Formulation:Lyophilized from PBS, pH 7.4, containing 0.01% SKL, 5% Trehalose
- Nuclease-free:N
- Shipping Temperature:4 °C
- Tested Applications:Positive control, Immunogen, SDS-PAGE, Western blot.
- Cat. No.:MSPP-RPC056MU1
Specifications
About this item
This is a MMP14 recombinant protein (prokaryotic), Mouse is sequencing from His121~Asn487 with 90 to 100% purity. Lyophilized from PBS, pH 7.4, containing 0.01% SKL, 5% Trehalose with 0.2 mg/ml.
- High quality, purity, reproducibility and effectiveness
- Offers customized buffers and tag options
- 100% quality and service satisfaction guarantee
MMP14, also known as MT1-MMP, is a member of membrane type (MT) MMPs. It can degrade various components of the extracellular matrix such as type I collagen and activate pro-MMP-2 and process cell adhesion molecules such as CD44 and integrin alpha V. It is also essential for pericellular collagenolysis and modeling of skeletal and extra skeletal connective tissues during development. MMP14 plays a important role in many physiological and pathological processes such as angiogenesis and tumor invasion. This protein is mainly expressed in stromal cells of colon, breast, head and neck. There are four domains for native MMP14, a pro domain containing the furin cleavage site, a catalytic domain containing the zinc-binding site, a hemopexin-like domain and a transmembrane domain.