Anti-Camp Antibody Picoband® fluoro488 Vervoeging

This gene encodes a member of an antimicrobial peptide family, characterized by a highly conserved N-terminal signal peptide containing a cathelin domain and a structurally variable cationic antimicrobial peptide, which is produced by extracellular proteolysis from the C-terminus. The protein plays an important role in innate immunity defense against viruses. In addition to its antibacterial, antifungal, and antiviral activities, the encoded protein functions in cell chemotaxis, immune mediator induction, and inflammatory response regulation.

Tetraspanin-12; Tspan-12; Tetraspan NET-2; Transmembrane 4 superfamily member 12; TSPAN12; NET2; TM4SF12; UNQ774/PRO1568

Camp

316010

G3V8S9

Mouse, Rat

No cross-reactivity with other proteins.

A synthetic peptide corresponding to a sequence at the C-terminus of rat Camp, which shares 83.3% amino acid (aa) sequence identity with mouse Camp.

Expressed in testis, in Sertoli cells, ejaculated spermatozoa and in seminal fluid (at protein level) .

Flow Cytometry

Alzheimer's Disease, Cell Biology, Metalloprotease, Neurodegenerative Disease, Neurology Process, Neuroscience, Proteolysis/Ubiquitin, Proteolytic Enzymes, Sensory System, Visual System

Immunogen affinity purified.

Liquid

Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activate the norrin (NDP) -dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1) (By similarity) . Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP) . Activates MMP14/MT1-MMP-dependent cleavage activity.

1. Agerberth, B., Gunne, H., Odeberg, J., Kogner, P., Boman, H. G., Gudmundsson, G. H. FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. Proc. Nat. Acad. Sci. 92: 195-199, 1995. 2. Chromek, M., Slamova, Z., Bergman, P., Kovacs, L., Podracka, L., Ehren, I., Hokfelt, T., Gudmundsson, G. H., Gallo, R. L., Agerberth, B., Brauner, A. The antimicrobial peptide cathelicidin protects the urinary tract against invasive bacterial infection. Nature Med. 12: 636-641, 2006. 3. Frohm, M., Agerberth, B., Ahangari, G., Stahle-Backdahl, M., Liden, S., Wigzell, H., Gudmundsson, G. H. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272: 15258-15263, 1997.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

39411 MW

6

Tetraspanin 12

Cell membrane; Multi-pass membrane protein.

Zinc finger protein Helios

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.