Antibody data
- Antibody Data
- Antigen structure
- References [4]
- Comments [0]
- Validations [0]
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- Product number
- AF930 - Provider product page
- Provider
- R&D Systems
- Product name
- Human TACE/ADAM17 Ectodomain Antibody
- Antibody type
- Polyclonal
- Description
- Immunogen affinity purified. Detects human TACE/ADAM17 Ectodomain in direct ELISAs and Western blots. In direct ELISAs, less than 5% cross-reactivity with recombinant human (rh) BACE, rhADAM8, rhADAM10, and recombinant mouse ADAM10 is observed.
- Reactivity
- Human
- Host
- Chicken/Avian
- Conjugate
- Unconjugated
- Antigen sequence
P78536
- Isotype
- IgY
- Vial size
- 100 ug
- Concentration
- LYOPH
- Storage
- Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Submitted references The shedding activity of ADAM17 is sequestered in lipid rafts.
FHL2 interacts with both ADAM-17 and the cytoskeleton and regulates ADAM-17 localization and activity.
ADAMs, a disintegrin and metalloproteinases, mediate shedding of oxytocinase.
ADAMs, a disintegrin and metalloproteinases, mediate shedding of oxytocinase.
Tellier E, Canault M, Rebsomen L, Bonardo B, Juhan-Vague I, Nalbone G, Peiretti F
Experimental cell research 2006 Dec 10;312(20):3969-80
Experimental cell research 2006 Dec 10;312(20):3969-80
FHL2 interacts with both ADAM-17 and the cytoskeleton and regulates ADAM-17 localization and activity.
Canault M, Tellier E, Bonardo B, Mas E, Aumailley M, Juhan-Vague I, Nalbone G, Peiretti F
Journal of cellular physiology 2006 Aug;208(2):363-72
Journal of cellular physiology 2006 Aug;208(2):363-72
ADAMs, a disintegrin and metalloproteinases, mediate shedding of oxytocinase.
Ito N, Nomura S, Iwase A, Ito T, Kikkawa F, Tsujimoto M, Ishiura S, Mizutani S
Biochemical and biophysical research communications 2004 Feb 20;314(4):1008-13
Biochemical and biophysical research communications 2004 Feb 20;314(4):1008-13
ADAMs, a disintegrin and metalloproteinases, mediate shedding of oxytocinase.
Ito N, Nomura S, Iwase A, Ito T, Kikkawa F, Tsujimoto M, Ishiura S, Mizutani S
Biochemical and biophysical research communications 2004 Feb 20;314(4):1008-13
Biochemical and biophysical research communications 2004 Feb 20;314(4):1008-13
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