• Western blot analysis of extracts of various cell lines, using RPP30 antibody (STJ114434) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-rabbit IgG (H+L) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Enhanced Kit. Exposure time: 90s.

Anti-RPP30 antibody (1-268) (STJ114434)

SKU:
STJ114434

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Host: Rabbit
Applications: WB
Reactivity: Mouse/Rat
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-RPP30 (1-268) is suitable for use in Western Blot research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: PBS with 0.02% Sodium Azide, 50% Glycerol, pH7.3.
Purification: Affinity purification
Dilution Range: WB 1:500-1:2000
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: RPP30
Gene ID: 10556
Uniprot ID: RPP30_HUMAN
Immunogen Region: 1-268
Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 1-268 of human RPP30 (NP_006404.1).
Immunogen Sequence: MAVFADLDLRAGSDLKALRG LVETAAHLGYSVVAINHIVD FKEKKQEIEKPVAVSELFTT LPIVQGKSRPIKILTRLTII VSDPSHCNVLRATSSRARLY DVVAVFPKTEKLFHIACTHL DVDLVCITVTEKLPFYFKRP PINVAIDRGLAFELVYSPAI KDSTMRRYTISSALNLMQIC KGKNVIISSAAERPLEIRGP YDVANLGLLFGLSESDAKAA VSTNCRAALLHGETRKTAF
Function Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences.
Protein Name Ribonuclease P Protein Subunit P30
Rnasep Protein P30
Rnase P Subunit 2
Database Links Reactome: R-HSA-6784531
Reactome: R-HSA-6791226
Cellular Localisation Nucleus
Nucleolus
Alternative Antibody Names Anti-Ribonuclease P Protein Subunit P30 antibody
Anti-Rnasep Protein P30 antibody
Anti-Rnase P Subunit 2 antibody
Anti-RPP30 antibody
Anti-RNASEP2 antibody

Information sourced from Uniprot.org

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