bs-70643R

DATASHEET

Host: Rabbit

Target Protein: RCAN1/Dscr1 (central region)

Specificity: The antibody detects several isoforms of RCAN1 on SDS-PAGE immunoblots of mouse C2C12, rat PC12, and human Jurkat cells. The predominate isoform detected is the 38 kDa RCAN1L, but the antibody may also detect RCAN2 and RCAN3. This sequence is highly conserved in rat and mouse RCAN1, and this sequence is found in all four isoforms of RCAN1. In addition, this sequence has significant homology to RCAN2 and RCAN3.

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: P53805

Source: RCAN1 synthetic peptide (coupled to carrier protein) corresponds to amino acids from the central region of human RCAN1S (isoform 2).

Purification: Antigen Affinity purification

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

Background:

An important element of calcium signaling pathways involves calmodulin activation of calcineurin (phosphatase PP2B), leading to dephosphorylation of transcription factors such as NFAT and MEF2. A wide variety of proteins other than calmodulin have also been implicated in regulating calcineurin activity. Regulators of Calcineurin (RCANs) include RCAN1, RCAN2, and RCAN3. RCAN1 has previously been referred to as Down's syndrome candidate region-1 (Dscr1), MCIP, calcipressin, and Adapt78. This RCAN is expressed as several different variants with RCAN1L (38 kDa) and RCAN1S (31 kDa) being most prevalent. RCAN1 is increased in Down's syndrome tissues and in a mouse model of Down's syndrome. Increased expression of RCAN1 leads to significant suppression of tumor growth in mice as result of deficits in calcineurin-induced tumor angiogenesis. RCAN1 can recruit TAB1, TAK1, and calcineurin into a macromolecular signaling complex, and TAK1 can phosphorylate Ser-94 and Ser-136 in RCAN1S. This phosphorylation converts RCAN1 from an inhibitor to a facilitator of calcineurin-NFAT signaling.