Anti-SLFN12 antibody (51-101 aa) (STJ193855)

SPECIFICATIONS
ClonalityPolyclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
ImmunogenSynthesized peptide derived from the human SLN12 at the amino acid range 51-101
STJ193855
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General Information

Short DescriptionRabbit polyclonal anti-Ribonuclease SLFN12 (51-101 aa) for use in WB in Human, Rat and Mouse samples. Datasheet included with dilution recommendations, and related reagents.
ApplicationsWB
HostRabbit
ReactivityHuman/Rat/Mouse
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ClonalityPolyclonal
IsotypeIgG
ConjugationUnconjugated
Concentration1 mg/mL
PurificationThe antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Dilution RangeWB 1:500-2000
FormulationLiquid in PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide.
Storage InstructionStore at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.

Target Information

Gene SymbolSLFN12
Gene ID55106
Uniprot IDSLN12_HUMAN
ImmunogenSynthesized peptide derived from the human SLN12 at the amino acid range 51-101
Immunogen Region51-101 aa
SpecificityThis antibody detects endogenous levels of SLN12 at Human

Additional Info

Function Ribonuclease which is part of an E2/17beta-estradiol-induced pro-apoptotic signaling pathway. E2 stabilizes the PDE3A/SLFN12 complex in the cytosol, promoting the dephosphorylation of SLFN12 and activating its pro-apoptotic ribosomal RNA/rRNA ribonuclease activity. This apoptotic pathway might be relevant in tissues with high concentration of E2 and be for instance involved in placenta remodeling. May play a role in cell differentiation.
Protein Name Ribonuclease Slfn12
Schlafen Family Member 12
Database Links
Cellular Localisation Nucleus
Cytoplasm
Cytosol
Alternative Antibody Names Anti-Ribonuclease Slfn12 antibody
Anti-Schlafen Family Member 12 antibody
Anti-SLFN12 antibody

Information sourced from Uniprot.org

Citations

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