KB-RAS (AA 179-192) antibody

Catalog No. ABIN118014

Product Details

Target: KB-RAS

Binding Specificity: AA 179-192

Reactivity: Human, Mouse

Host: Rabbit

Clonality: Polyclonal

Conjugate: Un-conjugated

Application: Enzyme Immunoassay (EIA)

Sequence: L-P-G-R-K-N-K-G-N-S-N-S-E-N Remarks: A single amino acid changes of S190P exists in mouse.

Purification: Immunoaffinity chromatography.

Immunogen: This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to aa 179-192 of human KB-RAS.

Application Details

Application Notes: This affinity purified antibody has been tested for use in ELISA against the immunizingpeptide. The antibody is likely suitable for Western blotting and other immunoassays. Specific conditions must be optimized by the investigator. This product has been assayedby ELISA against 0.1 μg of the immunizing peptide. A 1: 10,000 to 1: 50,000 dilution of theantibody is recommended for this assay.

Restrictions: For Research Use only

Handling

Concentration: 1.0 mg/mL (by UV absorbance at 280 nm)

Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 0.01 % (w/v) Sodium Azide as preservative.

Preservative: Sodium azide

Precaution of Use: This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Handling Advice: Avoid repeated freezing and thawing. This product is photosensitive and should be protected from light

Storage: 4 °C/-20 °C

Storage Comment: Store undiluted at 2-8 °C for one month or (in aliquots) at -20 °C for longer.

Target Details

Target: KB-RAS

Background: NFκB was originally identified as a factor that binds to the immunoglobulin kappa light chain enhancer in B cells. It was subsequently found in non-B cells in an inactive cytoplasmic form consisting of NFκB bound to IκB. Upon stimulation, IκB is phosphorylated and degraded, and then NF-κB translocates into the nucleus to activate the transcription of target genes. Two IκB proteins, IκBα and IκBβ, exhibit divergent biochemical and genetic characteristics, exemplified by their different degradation kinetics. These differences indicate their distinctive physiological functions. Mutated forms of the small G-protein Ras are found in about 30 % of all human cancers, including 95 % of pancreatic and 50 % of colon cancers. KB-RAS is the most commonly mutated form of Ras. KB-RAS was found to interact with the PEST domains of both IκB proteins in vitro. NFκB was originally identified as a heterodimeric DNA binding protein complex consisting of p65 (RelA) and p50 (NFKB1) subunits. Other identified subunits include p52 (NFKB2), c-Rel, and RelB. The p65, cRel, and RelB subunits are responsible for transactivation. The p50 and p52 subunits possess DNA binding activity but limited ability to transactivate. p52 has been reported to form transcriptionally active heterodimers with the NFκB subunit p65, similar to p50/p65 heterodimers. The heterodimers of p52/p65 and p50/p65 are regulated by physical inactivation in the cytoplasm by IκB-α. IκB-α binds to the p65 subunit, preventing nuclear localization and DNA binding. Low levels of p52 and p50 homodimers can also exist in cells.Synonyms: KB RAS