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RPLP1 polyclonal antibody

Product Specifications

Background

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 ribosomal phosphoprotein that is a component of the 60S subunit. The protein, which is a functional equivalent of the E. coli L7/L12 ribosomal protein, belongs to the L12P family of ribosomal proteins. It plays an important role in the elongation step of protein synthesis. Unlike most ribosomal proteins, which are basic, the encoded protein is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1 protein can interact with P0 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Two alternatively spliced transcript variants that encode different proteins have been observed. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

CAS Number

9007-83-4

Structure Composition

1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2

Product Name Alternative

RPLP1; LP1; P1; RPP1

Swiss Prot

P05386

Reactivity

Human, Mouse, Rat, Zebrafish

Immunogen

Recombinant fusion protein of human RPLP1 (NP_000994.1) .

Conjugation

Unconjugated

Applications

WB, IF/ICC

Dilution

WB,1:500 - 1:2000|IF/ICC,1:50 - 1:100

Purity

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Modification

Unmodification

Molecular Weight

17kDa

Storage Conditions

Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.

Notes

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

Specificity

Polyclonal Antibodies

Host or Source

Rabbit

Available Sizes

Frequently Asked Questions

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