Sterol Regulatory Element Binding Transcription Factor 2 (SREBF2) (Center) antibody

Antigen: Sterol Regulatory Element Binding Transcription Factor 2 (SREBF2)

Synonyms: SREBP2, bHLHd2, SREBP-2, AI608257, SREBP2gc, MGC124823, Srebf2_retired, SREBF2, srebp2, zgc:158371

Binding Site: Center

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC), ELISA

Certificates: ISO 9001:2008

Catalog no.: ABIN654630

Additional Information

Alternative name: SREBF2

Gene ID: 6721

UniProt: NP_004590.2, Q12772

Immunogen: This SREBF2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 402-431 amino acids from the Central region of human SREBF2.

Isotype: Ig

Description: Other names: Sterol regulatory element-binding protein 2,SREBF2,BHLHD2, SREBP2

Characteristics: Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)

Specificity: This SREBF2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 402-431 amino acids from the Central region of human SREBF2.

Molecular Weight: 123688 DA

Comments:

Background: SREBPs, including SREBP-1a, SREBP-1c, and SREBP-2, constitute a family of basic helix-loop-helix (bHLH) transcription factors that play a critical role in lipid homeostasis by regulating genes involved in cholesterol and fatty acid metabolism. Each SREBP consists of three domains, including an amino-terminal transcription factor domain of ~480 amino acids, a middle hydrophobic region of ~80 amino acids containing two hydrophobic transmembrane segments, and a carboxy-terminal regulatory domain of ~590 amino acids. SREBP-2 regulates cholesterol synthesis by activating the transcription of genes for HMG-CoA reductase and other enzymes of the cholesterol synthetic pathway. SREBP-2 is ubiquitously detected in various tissues. Under basal conditions SREBP is bound to ER membranes as a glycosylated precursor protein. Upon cholesterol depletion, the protein is cleaved to its active forms (about 50-68 kDa) and translocated into the nucleus to stimulate transcription of genes involved in the uptake and synthesis of cholesterol. LS-B1609 polyclonal antibody detects both precursor and active forms of the protein in tissues and cells such as liver, brown fat, testis, Hep-G2 cells, and human fibroblast. The apparent molecular weight on SDS-PAGE may be higher than the calculated molecular weight (about 126 kDa) due to glycosylation of the protein.

Application Details

Application Notes: The suggested dilution is: ELISA ~~ 1:1,000 Western blotting~~ 1:100~500 Immunohistochemistry ~~ 1:50~100

Concentration: 0.25 mg/ml

Purification: Purified

Buffer: Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.

Storage: Maintain refrigerated at 2-8 deg C for up to 6 months. For long term storage store at -20 deg C in small aliquots to prevent freeze-thaw cycles

Research Area: Translation Factors, Phospho-specific antibodies, Cell Structure, Protein Modifications, Transcription Factors, Signaling, Metabolism

Restrictions: For Research Use only

Images

Confocal immunofluorescent analysis of SREBF2 Antibody (Center) (ABIN654630) with HepG2 cell followed by Alexa Fluor 488-conjugated goat anti-rabbit lgG (green). DAPI was used to stain the cell nuclear (blue).

Publications

Product: Najafi-Shoushtari, Kristo, Li et al.: "MicroRNA-33 and the SREBP host genes cooperate to control cholesterol homeostasis." in: Science (New York, N.Y.), Vol. 328, Issue 5985, pp. 1566-9, 2010 (PubMed).

Marquart, Allen, Ory et al.: "miR-33 links SREBP-2 induction to repression of sterol transporters." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 107, Issue 27, pp. 12228-32, 2010 (PubMed).

Gerin, Clerbaux, Haumont et al.: "Expression of miR-33 from an SREBP2 intron inhibits cholesterol export and fatty acid oxidation." in: The Journal of biological chemistry, Vol. 285, Issue 44, pp. 33652-61, 2010 (PubMed).