Recombinant Human ORM2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3601

Recombinant Human ORM2 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3601
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Product Overview

Tag His
Host Species Human
Accession P19652
Synonym AGP-B, AGP-B', AGP2, ORM2
Background ORM2 belongs to the calycin superfamily, lipocalin family. Lipocalins share limited regions of sequence homology and a common tertiary structure architecture. They transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids. Lipocalins can be found in gram negative bacteria, vertebrate cells, and invertebrate cells, and in plants. They are associated with many biological processes. ORM2 functions as transport protein in the blood stream. It is expressed by the liver and secreted in plasma. It seems that ORM2 function in modulating the activity of the immune system during the acute-phase reaction. It binds various hydrophobic ligands in the interior of its beta-barrel domain. It also binds synthetic drugs and influences their distribution and availability.
Description A DNA sequence encoding the human ORM2 (P19652) (Met1-Ser201) was expressed with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Gln 19
AA Sequence Met1-Ser201
Molecular Weight The recombinant human ORM2 consists of 194 a.a. and predicts a molecular mass of 23.1 KDa. It migrates as an approximately 23 KDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Functions as transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction.
Subcellular Location Secreted.
Protein Families Calycin superfamily, Lipocalin family
Database References
Tissue Specificity Expressed by the liver and secreted in plasma.

Gene Functions References

  1. the glycosylation change of alpha-1-acid glycoprotein (AGP) in hepatocellular carcinoma (HCC), cirrhosis and controls PMID: 28621608
  2. Neural cell interactions are important for brain physiology and pathology. Particularly, the interaction between non-neuronal cells plays a central role in regulating brain inflammation, which is closely linked to many brain disorders. Here, we newly identified orosomucoid-2 (ORM2) as an endogenous protein that mediates such non-neuronal glial cell interactions PMID: 28193696
  3. Low ORM2 expression is associated with metastasis in hepatocellular carcinoma. PMID: 25965830
  4. Data suggest that human serum albumin (HSA) might serve as a carrier in delivering chitooligomers to target tissues than alpha-1-glycoprotein (AGP) which has pharmacological importance. PMID: 24359035
  5. Alteration in expression of ORM2 suggests that ORM2 could be used as a potential biomarker in the diagnosis of colorectal cancer. PMID: 22363757
  6. the sera of patients with acute inflammation demonstrated increased numbers of bi-antennary and alpha1,3-fucosylated N-glycan structures at each glycosylation site PMID: 15863355
  7. The binding of coumarin enantiomers to ORM2 is studied. PMID: 16290938
  8. Results describe the thermal unfolding and reversibility of temperature-induced changes in alpha(1)-acid glycoprotein. PMID: 16331959
  9. The results indicate that, in accordance with prior expectations, the ORM2 variant is responsible for the acute-phase property of alpha-1 acid glycoprotein. PMID: 19018521
  10. structure of the alpha1-acid glycoprotein (AGP), or orosomucoid (ORM), gene was investigated in a Ghanaian mother and her child, who shared an unusual variant, ORM1 S2(C), found by isoelectric focusing PMID: 11587070

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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