Human ADAM12 Biotinylated Antibody

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BAF4416
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Human ADAM12 Biotinylated Antibody Summary

Species Reactivity
Human
Specificity
Detects human ADAM12 in Western blots. In Western blots, approximately 10% cross-reactivity with recombinant human (rh) ADAM8 is observed and less than 1% cross-reactivity with rhADAM19 and rhADAM33 is observed.
Source
Polyclonal Sheep IgG
Purification
Antigen Affinity-purified
Immunogen
Chinese hamster ovary cell line CHO-derived recombinant human ADAM12
Arg29-Ser513
Accession # AAC08702
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Label
Biotin

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Human ADAM12 (Catalog # 4416-AD)

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Background: ADAM12

ADAM12, also known as meltrin-alpha, is a member of the ADAM family with metalloprotease activity (1). It consists of a propeptide, metalloproteinase, disintegrin, cysteine-rich, and EGF-like domains, a transmembrane segment, and a cytoplasmic tail with SH3 binding motifs. Human ADAM12 exists in two alternatively spliced forms: the prototype transmembrane form and a shorter secreted form lacking the transmembrane domain and the cytoplasmic tail. The secreted form has a 34 amino acid substitution in place of the transmembrane and cytoplasmic regions. In mouse, only the transmembrane form has been observed. The propeptide, which is cleaved in the Golgi by furin-like proprotein convertases, is retained in a noncovalent complex after ADAM12 secretion (2). Thus, the pro domain may function as an inhibitor of the proteolytic activity or play another unknown function. The known physiological substrates of ADAM12 are HBEGF in the heart (3) and IGFBP-3 and -5 in placental serum (4). Its proteolytic activity is inhibited by the tissue inhibitor of metalloproteinase-3 (rhTIMP-3, R&D Systems, Catalog # 973‑TM) and alpha ‑2‑macroglobulin. It also mediates cell-cell adhesion by interacting with integrins and syndecans as well as with additional unidentified molecules (4). ADAM12 may be a promising marker in prenatal diagnostics and breast cancer (5, 6). The recombinant ADAM12 contains the pro, metalloproteinase, and disintegrin domains. In addition to TIMP-3, the activity can also be inhibited by 5 mM 1,10-phenanthroline.

References
  1. Wewer, U.M. (2004) in Handbook of Proteolytic Enzymes, Barrett, A. J. et al. eds. pp 724.
  2. Wewer, U.M. et al. (2006) J. Biol. Chem. 281:9481.
  3. Asakura, M. et al. (2002) Nat. Med. 8:35.
  4. Loechel, F. et al. (2000) Biochem. Biophys. Res. Comm. 278:511.
  5. Laigaard, J. et al. (2006) Prenat Diagn. 26:973.
  6. Roopali, R. et al. (2004) J. Biol. Chem. 279:51323.
Long Name
A Disintegrin and Metalloprotease-like Domain 12
Entrez Gene IDs
8038 (Human)
Alternate Names
a disintegrin and metalloproteinase domain 12 (meltrin alpha); ADAM 12; ADAM metallopeptidase domain 12; ADAM12; disintegrin and metalloproteinase domain-containing protein 12; EC 3.4.24; EC 3.4.24.58; MCMP; MCMPMltna; Meltrin alpha; meltrin-alpha; MLTNA; MLTNEC 3.4.24.-

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