RNF23 Polyklonale Antilichaam

The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.

Ring finger protein 23; RNF23; Testis abundant finger protein; TFP; TFP RING FINGER PROTEIN 23; TRIM39; Tripartite mot containing 39; TRI39_HUMAN.

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Human, Mouse, Rat

101-200/518

RNF23

Unconjugated

KLH conjugated synthetic peptide derived from human RNF23

ELISA, IHC-P, IHC-F, IF

Purified by Protein A.

1µg/µl

ELISA (ELISA=1:5000-10000), IHC-P (IHC-P=1:100-500), IHC-F (IHC-F=1:100-500), IF (IF=1:50-200)

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Unmodified

Shipped at 4C. Store at -20C for one year. Avoid repeated freeze/thaw cycles.

56658