Recombinant Human PAD1 Protein

Beta LifeScience SKU/CAT #: BL-1408SG

Recombinant Human PAD1 Protein

Beta LifeScience SKU/CAT #: BL-1408SG
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.

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Product Overview

Tag GST
Host Species Human
Accession NM_013358
Synonym HPAD10; PADI1; PDI; PDI1
Background PAD1 is a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. PAD1 is a component of the 26S proteasome, a multiprotein complex that degrades proteins targeted for destruction by the ubiquitin pathway. The overexpression of PAD1 induced a distinctive pattern of multidrug resistance in mammalian cells and moderate resistance to ultraviolet light (1). PAD1 is also responsible for substrate deubiquitination during proteasomal degradation (2).
Description Recombinant full-length human PAD1 was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source Sf9 insect cells
AA Sequence Full Length
Molecular Weight ~95 kDa
Purity For specific purity information on a given lot, see related COA.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability The recombinant protein is stable for up to 12 months at -70°C
Usage For Research Use Only
Storage Recombinant Human PAD1 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Catalyzes the deimination of arginine residues of proteins.
Subcellular Location Cytoplasm.
Protein Families Protein arginine deiminase family
Database References
Tissue Specificity Detected in epidermal keratinocytes (at protein level). Epidermis, prostate, testis, placenta, spleen and thymus.

Gene Functions References

  1. Authors showed that PAD1 interacts with and citrullinates MEK1 thereby disrupting MEK1-catalyzed ERK1/2 phosphorylation, thus leading to the MMP2 overexpression. PMID: 28844713
  2. Identify acefylline as an activator of peptidylarginine deiminase 1 and 3 in the epidermis, resulting in filaggrin deimination. PMID: 26616205
  3. NF-kappaB-mediated signaling pathway is involved in PADI1 regulation in human epidermal keratinocytes PMID: 20596086
  4. cloning, gene organization, and expression analysis PMID: 12416996
  5. peptidylarginine deiminase types 1 and 3 loci map to chromosomal band 1p36.13 PMID: 15150696
  6. PAD1 and 3 are able to modify filaggrin PMID: 15675958
  7. PAD1 is co-located with filaggrin within the filamentous matrix of the deeper corneocytes where the protein is deiminated. PMID: 16091842
  8. MZF1 and Sp1/Sp3 binding to the promoter region drive the PADI1 expression in keratinocytes PMID: 17851584
  9. The expressoin of COL1A1-PADI1 genes were particularly effective in distinguishing OCSS from normal tissue. PMID: 18669583
  10. peptidylarginine deiminase citrullinates the chemokine CXCL8, and thus may dampen neutrophil extravasation during acute or chronic inflammation PMID: 18710930

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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