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Primary Antibodies > Enzyme Antibodies

Selenophosphate Synthetase 2 Antibody

Rabbit Polyclonal

Code

200-401-999

Size

100 µg

Price

$294.00

Availability

Ships next business day.

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Western blot using Rockland's Protein A purified anti-SPS2 antibody shows detection of SPS2 in NIH3T3 cells over-expressing this protein. No signal is seen in control lysates or in lysates from cells over-expressing the protein after pre-treatment with SPS2 siRNA. Endogenous SPS2 can be detected in mouse kidney, liver and testes tissue lysates. Partial cross-reactivity is seen against recombinant SPS1. The primary antibody was used at a 1:1000 dilution. Personal Communication, D. Hatfield, NCI, Bethesda, MD.

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Synonyms: Selenide, water dikinase 2 antibody, Selenium donor protein 2 antibody, SEPHS2 antibody, SPS2 antibody

Datasheet
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Selenophosphate Synthetase 2 Antibody Properties

Description

Anti-Selenophosphate Synthetase 2 (SPS2) (RABBIT) Antibody - 200-401-999

Host

Rabbit

Target Species

Mouse

Known Cross Reactivity

mouse

Clonality

Polyclonal

Application

ELISA : 1:5,000 - 1:20,000
Western Blot : 1:500 - 1:2,000
ImmunoPrecipitation: 1:100
Other Dilution: User Optimized

Physical State

Liquid (sterile filtered)

Shipping condition

Dry Ice

Format

IgG

Label

Unconjugated

Concentration

2.3 mg/mL by UV absorbance at 280 nm

Buffer

0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

Preservative

0.01% (w/v) Sodium Azide

Stabilizer

None

GeneName

SPS2

Selenophosphate Synthetase 2 Antibody Description

Background

This antibody is designed, produced, and validated as part of a collaboration between Rockland and the National Cancer Institute (NCI) and is suitable for Cancer, Immunology and Nuclear Signaling research. Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of selenocysteine-tRNA, the precursor of selenocysteine in selenoenzymes. A second selenophosphate synthetase (SPS2) was identified in mammals. SPS2 is itself a selenoprotein in mammals.

Immunogen

This Protein A purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a full-length recombinant protein corresponding to mouse SPS2.

Immunogen Type

Recombinant Protein

Storage Condition

Store vial at -20° C prior to opening. Aliquot contents and freeze at -20° C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use.

Application Note

This Protein A purified antibody has been tested for use in ELISA and western blotting. Specific conditions for reactivity should be optimized by the end user. Expect a band approximately 48 kDa in size corresponding to SPS2 by western blotting in the appropriate cell lysate or extract.

Purity/Specifity

This product was purified by Protein A chromatography from monospecific antiserum. This antibody reacts with mouse SPS2 and shows partial cross-reactivity with SPS1. A BLAST analysis was used to suggest cross-reactivity with SPS2 from human sources based on an 84% homology with the immunizing sequence. Cross-reactivity with SPS2 from other sources has not been determined.

Disclaimer Note-General

This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 326, Gilbertsville, Pennsylvania, USA.

General Reference

Guimaraes MJ, Peterson D, Vicari A, Cocks BG, Copeland NG, Gilbert DJ, Jenkins NA, Ferrick DA, Kastelein RA, Bazan JF, Zlotnik A (1996) Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism? Proc. Natl. Acad. Sci. USA 93(26):15086-15091. Low SC, Harney JW, Berry MJ (1995) Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis. J. Biol. Chem. 270(37):21659-21664. Tamura T, Yamamoto S, Takahata M, Sakaguchi H, Tanaka H, Stadtman TC, Inagaki K (2004) Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation. Proc. Natl. Acad. Sci. USA 101(46):16162-16167. Kim TS, Yu MH, Chung YW, Kim J, Choi EJ, Ahn K, Kim IY (1999) Fetal mouse selenophosphate synthetase 2 (SPS2): biological activities of mutant forms in Escherichia coli. Mol. Cells 9(4):422-428. Rother M, Resch A, Wilting R, Bock A (2001) Selenoprotein synthesis in archaea. Biofactors 14(1-4):75-83. Review. Persson BC, Bock A, Jackle H, Vorbruggen G (1997) SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity. J. Mol. Biol. 274(2):174-180. Leinfelder W, Forchhammer K, Veprek B, Zehelein E, Bock A (1990) In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product. Proc. Natl. Acad. Sci. USA 87(2):543-547.

Specific Reference

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