Description
Product Usage Information
This product is the carrier free version of product #4151. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol. This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us . Optimal dilutions/concentrations should be determined by the end user. BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.
Formulation
Supplied in 1X PBS (10 mM Na 2 HPO 4 , 3 mM KCl, 2 mM KH 2 PO 4 , and 140 mM NaCl (pH 7.8)). BSA and Azide Free. For standard formulation of this product see product # 4151
Storage
Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.
Specificity / Sensitivity
ADAM9 (D64B5) Rabbit Monoclonal Antibody (BSA and Azide Free) detects endogenous levels of total ADAM9 protein.
Species Reactivity: Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val611 of human ADAM9 protein.
Background
The ADAM (A Disintegrin and A Metalloprotease) family of multidomain membrane proteins influences cell signaling and adhesion by shedding cell surface proteins such as cytokines and growth factors, by influencing cell adhesion to the extracellular matrix (ECM), and by directly remodeling the ECM. Conserved domains in ADAM family members include a prodomain, a zinc-dependent metalloprotease domain, a disintegrin domain, a cysteine-rich domain, an EGF-like sequence, and a short cytoplasmic tail (1,2). The prodomain is thought to aid in protein folding. Disintegrin and cysteine-rich domains mediate adhesion, at least in part, through binding to integrins. Phosphorylation of the cytoplasmic tail as well as its interaction with other signaling proteins may influence intra- and extracellular signaling (1). ADAM9 is widely distributed and has been shown to affect migration in skin keratinocytes (3,4). Research studies have shown that ADAM9 is overexpressed in prostate cancer (5), pancreatic cancer (6), gastric cancer (7), and has been linked to invasion and metastasis in small cell lung cancer (8). Research has also shown that an alternatively spliced short (50 kDa) form of ADAM9 containing protease activity is involved in tumor cell invasion (9).
Alternate Names
a disintegrin and metalloproteinase domain 9 (meltrin gamma); ADAM 9; ADAM metallopeptidase domain 9; ADAM metallopeptidase domain 9 (meltrin gamma); ADAM9; Cellular disintegrin-related protein; cone rod dystrophy 9; CORD9; Disintegrin and metalloproteinase domain-containing protein 9; KIAA0021; MCMP; MDC9; Meltrin-gamma; Metalloprotease/disintegrin/cysteine-rich protein 9; MLTNG; Myeloma cell metalloproteinase
