| Host: |
HEK293 |
| Note: |
STRICTLY FOR FURTHER RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description: |
Recombinant-Mouse ADAM15-protein was developed from hek293. For use in research applications. |
| Conjugation: |
Unconjugated |
| Formulation: |
Lyophilised from 0.2 Mu m filtered PBS solution, pH7.2, 5% Trehalose. |
| Dilution Range: |
Spin the vial and reconstite in distilled water to a concentration not less than 0.1 mg/mL. This can then be diluted into other buffers. |
| Storage Instruction: |
Can be stored in working aliquots at 2°C-8°C C for one month, or at-20°C to-70°C for 1 year. Avoid repeated freeze/thaw cycles. NA |
| Endotoxin: |
Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg (1EU/µg). NA |
| Immunoreactivity: |
The activity was tested by the ability of immobilized recombinant mouse ADAM15 to bind Human PTK6. NA |
| Gene Symbol: |
Adam15 |
| Gene ID: |
11490 |
| Uniprot ID: |
ADA15_MOUSE |
| Immunogen Region: |
ASP208-THR697, ECD |
| Immunogen: |
Optimized DNA sequence encoding extracellular domain of mouse Disintegrin and metalloproteinase 15-ADAM15 (ASP208-THR697) including a C-terminal His tag was expressed in HEK293 cells. NA |
| Tissue Specificity | Expressed moderately in pericytes of retina. Expressed in testis and in spermatozoa from the caput, corpus, and cauda epididymis, as well as in non-capacitated and acrosome-reacted sperm (at protein level). Highly expressed in heart, brain, lung, and kidney. Expressed at lower levels in spleen, liver, testis and muscle. |
| Post Translational Modifications | The precursor is cleaved by a furin endopeptidase. An additional membrane proximal site of cleavage affects a small percentage of the proteins and results in disulfide-linked fragments. The prodomain is apparently cleaved in several positions that are N-terminal of the furin cleavage site. May be partially sialylated. Phosphorylation increases association with PTKs. |
| Function | Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. Interactions with egg membrane could be mediated via binding between the disintegrin-like domain to one or more integrin receptors on the egg. |
| Protein Name | Disintegrin And Metalloproteinase Domain-Containing Protein 15Adam 15Ad56Metalloprotease Rgd Disintegrin ProteinMetalloproteinase-Like - Disintegrin-Like - And Cysteine-Rich Protein 15Mdc-15Metargidin |
| Database Links | Reactome: R-MMU-1474228Reactome: -MMU-8941237 |
| Cellular Localisation | Endomembrane SystemSingle-Pass Type I Membrane ProteinCell JunctionAdherens JunctionCell ProjectionCiliumFlagellumCytoplasmic VesicleSecretory VesicleAcrosomeThe Majority Of The Protein Is Localized In A Perinuclear Compartment Which May Correspond To The Trans-Golgi Network Or The Late EndosomeThe Pro-Protein Is The Major Detectable Form On The Cell SurfaceWhereas The Majority Of The Protein In The Cell Is Processed |
| Alternative Protein Names | Disintegrin And Metalloproteinase Domain-Containing Protein 15 proteinAdam 15 proteinAd56 proteinMetalloprotease Rgd Disintegrin Protein proteinMetalloproteinase-Like - Disintegrin-Like - And Cysteine-Rich Protein 15 proteinMdc-15 proteinMetargidin proteinAdam15 proteinMdc15 protein |
Information sourced from Uniprot.org
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