Purified anti-NCOA2/GRIP1

NCOA2/GRIP1 (nuclear receptor coactivator 2/glucocorticoid receptor-interacting protein 1 (GRIP1)) is a 159 kD member of the p160/steroid receptor coactivator family containing a nuclear localization sequence, bHLH, and PAS domain. Two isoforms of this protein have been reported. NCOA/GRIP1 is expressed in the cytoplasm and translocated into the nucleus upon phosphorylation. This protein is highly expressed in the placenta, skeletal muscle, uterus with lower expression in B cells, lymphocytes, and some tumors. NCOA/GRIP1 has histone acetyltransferase activity, and is a transcriptional coactivator for steroid and nuclear hormone receptor. This protein mediates ligand-independent nuclear translocation and activates the CAR receptor in response to phenobarbital. This protein is modified by phosphorylation. NCOA/GRIP1 forms a multisubunit coactivation complex with NCOA3, IKKA, IKKB, IKBKG and histone acetyltransferase protein CREB binding protein and has also been shown to interact with HIF1A, APEX, NR3C1, and CAR. The Poly6090 antibody recognizes the N-terminal region of human NCOA2/GRIP1 and has been shown to be useful for Western blotting.

Prices direct from BioLegend

Quick response times

Exclusive Biosave savings/discounts

SPECIFICATIONS

Catalog Number

609002

Size

200 microl

Applications

WB

Hosts

Rabbit

Reactivities

Hum

Clone

Poly6090

Antigen

Recombinant (partial) , N-terminal

Gene Id

23426

Isotype

Rabbit Polyclonal

Clonality

Polyclonal

Dilutions

Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 10 microl per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.

Storage Temp

-20 C

Concentration

Shipping Temp

Ambient RT

Storage Buffer

Upon receipt, store frozen at -20 C.

Alternative Names

Nuclear receptor coactivator 2, Glucocorticoid receptor-interacting protein 1 (GRIP1)

Regulatory Status

RUO