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RPL22 polyclonal Antibody | BS65203

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BW-BS65203
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NULL366.00 - NULL549.00

Description

RPL22 polyclonal Antibody | BS65203 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human,Mouse,Rat

Application: IHC-p,IF (paraffin section),ELISA

Application Range: Immunohistochemistry: 1/100 - 1/300. ELISA: 1/10000. Not yet tested in other applications.

Background: ribosomal protein L22 (RPL22) Homo sapiens Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a cytoplasmic ribosomal protein that is a component of the 60S subunit. The protein belongs to the L22E family of ribosomal proteins. Its initiating methionine residue is post-translationally removed. The protein can bind specifically to Epstein-Barr virus-encoded RNAs (EBERs) 1 and 2. The mouse protein has been shown to be capable of binding to heparin. Transcript variants utilizing alternative polyA signals exist. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. It was previously thought that this gene mapped to 3q26 and that it was fused to the acute myeloid leukemia 1 (AML1

Storage & Stability: -20°C/1 year

Specificity: Ribosomal Protein L22 Polyclonal Antibody detects endogenous levels of Ribosomal Protein L22 protein.

Molecular Weight: /

Note: For research use only, not for use in diagnostic procedure.

Alternative Names: RPL22; 60S ribosomal protein L22; EBER-associated protein; EAP; Epstein-Barr virus small RNA-associated protein; Heparin-binding protein HBp15

Immunogen: The antiserum was produced against synthesized peptide derived from human RPL22. AA range:51-100

Conjugate: Unconjugated

Modification: Unmodification

Purification & Purity: The Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Pathway:

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