Recombinant Human 60S Acidic Ribosomal Protein P2 (RPLP2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-09186P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) RPLP2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) RPLP2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) RPLP2.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) RPLP2.

Recombinant Human 60S Acidic Ribosomal Protein P2 (RPLP2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-09186P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human 60S Acidic Ribosomal Protein P2 (RPLP2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P05387
Target Symbol RPLP2
Synonyms 2700049I22Rik; 60S acidic ribosomal protein P2; Acidic ribosomal phosphoprotein P2; D11S2243E; LP2; MGC71408; OTTMUSP00000029428; OTTMUSP00000029429; OTTMUSP00000029430; P2; Renal carcinoma antigen NY-REN-44; Ribosomal protein P2; Ribosomal protein, large, P2; RLA2_HUMAN; rplP2; RPP2
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His
Target Protein Sequence MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD
Expression Range 1-115aa
Protein Length Full Length
Mol. Weight 15.7 kDa
Research Area Cancer
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Plays an important role in the elongation step of protein synthesis.
Protein Families Eukaryotic ribosomal protein P1/P2 family
Database References

Gene Functions References

  1. Collectively, the present results suggest that PhoRpp21 binds the loop between P11 and P12 helices through overall positively charged clusters on the surface of the complex and serves as a scaffold for PhoRpp29 to optimize structural conformation of its N-terminal helix (alpha2) in PhoRpp21, as well as C-terminal residues in PhoRpp29, for RNase P activity. PMID: 27810361
  2. Results show that the conserved C-terminal segment of P2 from three different eukaryotic species- Human, Plasmodium falciparum and Toxoplasma gondii is intrinsically disordered. PMID: 25412900
  3. relevance of the observed cross-reactive IgE autoantibodies against P2 proteins in systemic lupus eryth remains to be elucidated PMID: 21410706
  4. the eukaryotic stalk protein P2 forms a symmetric homodimer in solution, and is structurally distinct from the bacterial counterpart L12 homodimer. PMID: 20385603
  5. Ribosomal protein P2 has been identified as a novel substrate of GRK2 in HEK-293 cells where P2 phosphorylation is increased following agonist stimulation of the beta 2-adrenergic receptor under conditions of tyrosine kinase PKC and PKA inhibition. PMID: 12379128
  6. Antisense-mediated depletion may disrupt the proteome of cancer cells. PMID: 14981896
  7. Distinct roles for CD39 and P2-purinergic signaling in both tissue remodeling and fibrogenesis with respect to human pancreatic diseases. PMID: 16920697

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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