Product: N-Acetyl-Calicheamicin
ADAMTS4 Antibody Summary
| Immunogen |
Synthetic 15 amino acid peptide from Disintegrin-like domain of human ADAMTS4.
|
| Specificity |
Human ADAMTS4. BLAST analysis of the peptide immunogen showed no homology with other human proteins.
|
| Predicted Species |
Rat (93%), Porcine (93%), Opossum (93%). Backed by our 100% Guarantee.
|
| Clonality |
Polyclonal
|
| Host |
Rabbit
|
| Gene |
ADAMTS4
|
| Purity |
Immunogen affinity purified
|
| Innovators Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase.
Learn about the Innovators Reward
|
Applications/Dilutions
| Dilutions |
|
Reactivity Notes
Orangutan, Gibbon, Marmoset. Predicted cross-reactivity based on sequence identity: Elephant (100%), Panda (100%).
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
|
| Buffer |
PBS
|
| Preservative |
0.1% Sodium Azide
|
| Concentration |
1.0 mg/ml
|
| Purity |
Immunogen affinity purified
|
Alternate Names for ADAMTS4 Antibody
- a disintegrin-like and metalloprotease (reprolysin type) with thrombospondintype 1 motif, 4
- ADAM metallopeptidase with thrombospondin type 1 motif, 4
- ADAM-TS 4
- ADAMTS2
- ADAMTS-2
- ADAMTS4
- ADAM-TS4
- ADAMTS-4
- ADMP-1
- ADMP-1EC 3.4.24.82
- Aggrecanase 1
- aggrecanase-1
- EC 3.4.24
- KIAA0688A disintegrin and metalloproteinase with thrombospondin motifs 4
Background
ADAMTS4, also known as aggrecanase-1, is a Metallopeptidase M12B type protease that is responsible for degradation of the articular cartilage protein aggrecan and the brain extracellular matrix proteoglycan brevican. The ADAMTS4 protein contains a signal sequence, a propeptide domain, a catalytic domain, a disintegrin-like motif, and a C-terminal domain with a thrombospondin (TSP) type 1 motif. ADAMTS4 has been implicated in inflammatory joint diseases, and it also may be a factor in the progression of glioma and Alzheimers disease. ADAMTS4 expression has been documented in normal human brain, cartilage, heart, lung, placenta, muscle, and synovium. ESTs have been isolated from human tissue libraries, including normal brain, lung, pancreas, and skeletal muscle and cancerous breast.