Anti-Triadin/TRDN Antibody Picoband® fluoro488 Vervoeging

This gene encodes an integral membrane protein found in skeletal and cardiac muscle. The encoded protein plays a role in skeletal muscle excitation-contraction coupling as part of the calcium release complex and is required for normal skeletal muscle strength. This protein inly links triads and microtubules in skeletal muscle. Mutations in this gene are associated with cardiac arrythmia syndrome and some variants in this gene may be associated with sudden cardiac death.

Disintegrin and metalloproteinase domain-containing protein 28; ADAM 28;3.4.24.-; Epididymal metalloproteinase-like, disintegrin-like, and cysteine-rich protein II; eMDC II; Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L; MDC-L; ADAM28; ADAM23, MDCL

TRDN

10345

Q13061

Human

No cross-reactivity with other proteins.

E.coli-derived human Triadin/TRDN recombinant protein (Position: M67-Q729) .

Expressed predominantly in secondary lymphoid tissues, such as lymph node, spleen, small intestine, stomach, colon, appendix and trachea. The lymphocyte population is responsible for expression of this protein in these tissues. Isoform 2 is expressed preferentially in spleen.

Flow Cytometry

Signal Transduction

Immunogen affinity purified.

Liquid

May play a role in the adhesive and proteolytic events that occur during lymphocyte emigration or may function in ectodomain shedding of lymphocyte surface target proteins, such as FASL and CD40L. May be involved in sperm maturation.

1. Altmann, H. M., Tester, D. J., Will, M. L., Middha, S., Evans, J. M., Eckloff, B. W., Ackerman, M. J. Homozygous/compound heterozygous triadin mutations associated with autosomal-recessive long-QT syndrome and pediatric sudden cardiac arrest: elucidation of the triadin knockout syndrome. Circulation 131: 2051-2060, 2015. 2. Chopra, N., Yang, T., Asghari, P., Moore, E. D., Huke, S., Akin, B., Cattolica, R. A., Perez, C. F., Hlaing, T., Knollmann-Ritschel, B. E. C., Jones, L. R., Pessah, I. N., Allen, P. D., Franzini-Armstrong, C., Knollmann, B. C. Ablation of triadin causes loss of cardiac Ca2+ release units, impaired excitation-contraction coupling, and cardiac arrhythmias. Proc. Nat. Acad. Sci. 106: 7636-7641, 2009. 3. Hong, C.-S., Ji, J.-H., Kim, J. P., Jung, D. H., Kim, D. H. Molecular cloning and characterization of mouse cardiac triadin isoforms. Gene 278: 193-199, 2001.

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

87148 MW

6

ADAM metallopeptidase domain 28

Isoform 1: Cell membrane; Single-pass type I membrane protein.

ADAM metallopeptidase domain 28

Rabbit IgG

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