OSBPL9 Antibody | 30-091

OSBPL9 Antibody | 30-091 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human, Dog

Homology: N/A

Immunogen: Antibody produced in rabbits immunized with a synthetic peptide corresponding a region of human OSBPL9.

Research Area: Neuroscience

Tested Application: E, WB, IHC

Application: OSBPL9 antibody can be used for detection of OSBPL9 by ELISA at 1:62500. OSBPL9 antibody can be used for detection of OSBPL9 by western blot at 0.25 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50, 000 - 100, 000.

Specificiy: N/A

Positive Control 1: Cat. No. 1205 - Jurkat Cell Lysate

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: 61 kDa, 83 kDa, 63 kDa, 64 kDa, 70 kDa, 82 kDa, 84 kDa

Validation: N/A

Isoform: N/A

Purification: Antibody is purified by peptide affinity chromatography method.

Clonality: Polyclonal

Clone: N/A

Isotype: N/A

Conjugate: Unconjugated

Physical State: Liquid

Buffer: Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Concentration: batch dependent

Storage Condition: For short periods of storage (days) store at 4˚C. For longer periods of storage, store OSBPL9 antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles.

Alternate Name: OSBPL9, FLJ12492, FLJ14629, FLJ14801, FLJ32055, FLJ34384, MGC15035, ORP9, ORP-9

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: OSBPL9 is a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain.This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain. Multiple transcript variants, most of which encode distinct isoforms, have been identified.