Product Description

MRPL14 Polyclonal Antibody

Product: Liquid in 0.42% Potassium phosphate, 0.87% Sodium chloride, pH 7.3, 30% glycerol, and 0.01% sodium azide.

Catalogue Numbers: BS67025-50, BS67025-100

Sizes: 50µl, 100µl

Swiss-Prot: Q6P1L8

Host: Rabbit

Reactivity: Human, Mouse, Rat

Applications: WB, IHC

Background: Forms part of 2 intersubunit bridges in the assembled ribosome. Upon binding to MALSU1 intersubunit bridge formation is blocked, preventing ribosome formation and repressing translation (Probable).

Product: Liquid in 0.42% Potassium phosphate, 0.87% Sodium chloride, pH 7.3, 30% glycerol, and 0.01% sodium azide.

Purification and Purity: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

Specificity: Recognizes endogenous levels of MRPL14 protein.

Note: For research use only, not for use in diagnostic procedure.

Extra Notes: Western blot analysis of MRPL14 expression in A549 (A), H446 (B), mouse kidney (C), mouse lung (D), rat kidney (E) whole cell lysates., Immunohistochemical analysis of MRPL14 staining in human breast cancer formalin fixed paraffin embedded tissue section. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0). The section was then incubated with the antibody at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.

Bioworld Molecular Weight: ~ 16 kDa

Storage and Stability: Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Alternative Name: MRPL32; RPML32; 39S ribosomal protein L14 mitochondrial; L14mt; MRP-L14; 39S ribosomal protein L32 mitochondrial; L32mt; MRP-L32

Immunogen: KLH-conjugated synthetic peptide encompassing a sequence within the C-term region of human MRPL14. The exact sequence is proprietary.

Conjugate: Unconjugated

Modification: Unmodified