Product Description
SPTLC2 Antibody | 26-333 | ProSci
Host: Rabbit
Reactivity: Human, Mouse, Rat
Homology: N/A
Immunogen: Antibody produced in rabbits immunized with a synthetic peptide corresponding a region of human SPTLC2.
Research Area: Other
Tested Application: E, WB
Application: SPTLC2 antibody can be used for detection of SPTLC2 by ELISA at 1:312500. SPTLC2 antibody can be used for detection of SPTLC2 by western blot at 1 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50, 000 - 100, 000.
Specificiy: N/A
Positive Control 1: Cat. No. 1211 - HepG2 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: 63 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 SPTLC2 antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles.
Alternate Name: SPTLC2, KIAA0526, LCB2, SPT2, HSN1C, LCB2A, NSAN1C, hLCB2a
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: SPTLC2 is a long chain base subunit of serine palmitoyltransferase. Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It catalyzes the pyridoxal-5-prime-phosphate-dependent condensation of L-serine and palmitoyl-CoA to 3-oxosphinganine. Mutations in this gene were identified in patients with hereditary sensory neuropathy type I.This gene encodes a long chain base subunit of serine palmitoyltransferase. Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It catalyzes the pyridoxal-5-prime-phosphate-dependent condensation of L-serine and palmitoyl-CoA to 3-oxosphinganine. Mutations in this gene were identified in patients with hereditary sensory neuropathy type I. Alternatively spliced variants encoding different isoforms have been identified.