Recombinant Human Protein-Arginine Deiminase Type-2 (PADI2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-09540P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) PADI2.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) PADI2.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) PADI2.
Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) PADI2.

Recombinant Human Protein-Arginine Deiminase Type-2 (PADI2) Protein (His)

Beta LifeScience SKU/CAT #: BLC-09540P
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Product Overview

Description Recombinant Human Protein-Arginine Deiminase Type-2 (PADI2) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q9Y2J8
Target Symbol PADI2
Synonyms KIAA0994; OTTHUMP00000044625; PAD 2; PAD H19 ; PAD-H19; PAD2; PADI 2; Padi2; PADI2 protein; PADI2_HUMAN; PDI 2; PDI2; Peptidlyarginine deiminase type II; Peptidyl arginine deiminase II; Peptidyl arginine deiminase type II; Peptidylarginine deiminase II; Protein arginine deiminase; Protein arginine deiminase type 2; Protein arginine deiminase type II; Protein-arginine deiminase type II; Protein-arginine deiminase type-2
Species Homo sapiens (Human)
Expression System Yeast
Tag N-6His
Target Protein Sequence MLRERTVRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAEEVATNGKQRWLLSPSTTLRVTMSQASTEASSDKVTVNYYDEEGSIPIDQAGLFLTAIEISLDVDADRDGVVEKNNPKKASWTWGPEGQGAILLVNCDRETPWLPKEDCRDEKVYSKEDLKDMSQMILRTKGPDRLPAGYEIVLYISMSDSDKVGVFYVENPFFGQRYIHILGRRKLYHVVKYTGGSAELLFFVEGLCFPDEGFSGLVSIHVSLLEYMAQDIPLTPIFTDTVIFRIAPWIMTPNILPPVSVFVCCMKDNYLFLKEVKNLVEKTNCELKVCFQYLNRGDRWIQDEIEFGYIEAPHKGFPVVLDSPRDGNLKDFPVKELLGPDFGYVTREPLFESVTSLDSFGNLEVSPPVTVNGKTYPLGRILIGSSFPLSGGRRMTKVVRDFLKAQQVQAPVELYSDWLTVGHVDEFMSFVPIPGTKKFLLLMASTSACYKLFREKQKDGHGEAIMFKGLGGMSSKRITINKILSNESLVQENLYFQRCLDWNRDILKKELGLTEQDIIDLPALFKMDEDHRARAFFPNMVNMIVLDKDLGIPKPFGPQVEEECCLEMHVRGLLEPLGLECTFIDDISAYHKFLGEVHCGTNVRRKPFTFKWWHMVP
Expression Range 1-665aa
Protein Length Full Length
Mol. Weight 77.6kDa
Research Area Epigenetics And Nuclear Signaling
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 Catalyzes the deimination of arginine residues of proteins.
Subcellular Location Cytoplasm.
Protein Families Protein arginine deiminase family
Database References
Tissue Specificity Detected in keratinocytes in epidermis (at protein level).

Gene Functions References

  1. the mRNA expression of PADI2, PADI4 and Sp1 is upregulated in rheumatoid arthritis bone marrow CD34+ cells independently of the systemic inflammation or treatment regimen. PMID: 29148420
  2. These data suggest that overexpression of the human PAD2 transgene in the epidermis of transgenic mice increases the malignant conversion rate of benign tumors by promoting an inflammatory microenvironment. PMID: 28766045
  3. Brain gene expression of PADI2, ZNF385A, PSD2, and A2ML1 and DNA methylation dysregulations are implicated in the alteration of brain tissue properties associated with late-life cognitive decline above and beyond the influence of common neuropathologic conditions. PMID: 29084334
  4. Peptidyl arginine deiminase 2 (PADI2) is required for activation of androgen receptor (AR) signaling under androgen-deprived condition. PMID: 28819028
  5. Data suggest that protein-arginine deiminase 2 (PADI2) suppresses the proliferation of colonic epithelial cells through catalysis of protein citrullination, and that downregulation of PADI2 expression might therefore contribute to colon carcinogenesis. PMID: 28403548
  6. Downregulation of PADI2 is an early event in the pathogenesis of colorectal cancer associated with poor prognosis and points toward a possible role of citrullination in modulating tumor cells and their microenvironment. PMID: 27280713
  7. Multiple proteins citrullinated by hypoxia-induced PADs were identified. In addition, the extracellular domain of vascular endothelial growth factor receptor 2 was citrullinated by human PAD2 in vitro. CONCLUSION: Our data may contribute to understanding of pathophysiology of malignant gliomas from the aspects of protein citrullination. PMID: 27818200
  8. Deimination of myelin basic protein (MBP) by peptidylarginine deiminase (PAD) prevents its binding to the proteasome and decelerates its degradation by the proteasome in mammalian cells. Potential anticancer drug tetrazole analogue of chloramidine 2, at concentrations greater than 1 microM inhibits the enzymatic activity of PAD in vitro. PMID: 27599511
  9. this study shows that a miR-4728 downregulates PADI2, a novel rheumatoid arthritis risk gene PMID: 26927695
  10. We identified the presence of PADI3 mRNA expression in synovial tissue and PADI2 and PADI4 mRNA expressions in fibroblast-like synoviocytes from patients with rheumatoid arthritis. PMID: 26255191
  11. Protein arginine deiminase 2 binds six calcium ions in an ordered fashion. PMID: 25621824
  12. PAD2 activity was significantly higher in cell-free synovial fluid of rheumatoid arthritis patients compared to osteoarthritis patients. PMID: 26245941
  13. PAD2 activity was detected in synovial fluid samples from patients with rheumatoid arthritis. PMID: 25475141
  14. Report increased levels of extracellular PAD2 in the lungs of smokers. PMID: 25897949
  15. PADI2 and vimentin participate in the apoptotic mechanisms of activated T lymphocytes. PMID: 24850148
  16. these studies provide the first genetic evidence that PAD2 functions as an oncogene and suggest that PAD2 may promote tumor progression by enhancing inflammation within the tumor microenvironment. PMID: 25213324
  17. PAD2 appears to use a substrate-assisted mechanism of catalysis in which the positively charged substrate guanidinium depresses the pKa of the nucleophilic cysteine PMID: 24989433
  18. Data suggest peptidylarginine deiminase 2 (PAD2) as a possible biomarker in various inflammatory diseases. PMID: 24384061
  19. PAD2 and PAD4 have distinct substrate specificities. PMID: 24594197
  20. These findings suggest that PAD2 and citrullinated proteins may play a key role in the brain pathology of prion diseases. [review] PMID: 23022892
  21. Our observations show increased levels of protein deimination but not PAD2 in age related macular degeneration retinas and retinal pigment epithelium suggesting reduced rate of turnover of deiminated proteins. PMID: 23562679
  22. PAD2 binds directly to the promoters of the PTN and MAGEA12 genes and that the likely mechanism by which PAD2 regulates expression of these genes is via citrullination of arginine residues 2-8-17 on histone H3 tails. PMID: 22911765
  23. Contact between stimulated T cells and monocyte-macrophages or cytokine-activated monocyte-macrophages constitutes a highly likely source of PAD2 and PAD4, which are observed in inflamed synovial tissues. PMID: 22614825
  24. Normal human and canine mammary epithelium showed strong cytoplasmic and nuclear expression of PAD2, but there was reduced PAD2 expression in mammary carcinomas from both species. PMID: 22520816
  25. 17beta-estradiol stimulation induces the recruitment of PAD2 to target promoters by ERalpha, whereby PAD2 then citrullinates H3R26, which leads to local chromatin decondensation and transcriptional activation. PMID: 22853951
  26. Defective regulation of PAD2 in the periphery blood, without the immunological shelter of the blood-brain barrier, may contribute to the development of the autoimmune responses in MS. PMID: 21878453
  27. This is the first report demonstrating that like in primary open angle glaucoma, normal tension glaucoma also possesses elevated levels of both PAD2 and protein-bound citrulline. PMID: 20806090
  28. PAD2 activation and aberrant citrullinated proteins could play a role in pathogenesis and have value as a marker for the postmortem classification of neurodegenerative diseases. PMID: 20013286
  29. PADI2 does not contribute to genetic susceptibility to schizophrenia. PMID: 19478818
  30. PAD2 is expressed in human monocytic leukaemia THP-1 cells during differentiation into macrophages PMID: 19564157
  31. molecular cloning and gene organization; expressed by all the living epidermal layers, suggesting that PAD type II is functionally important during terminal differentiation of epidermal keratinocytes PMID: 12392711
  32. first report to demonstrate a measurable response in the amounts of peptidylarginine deiminase type II mRNA, protein and activity in human astrocytes by prolonged hypoxic exposure PMID: 15555572
  33. hPADI2 and hPADI4 have different roles under physiological and pathological conditions PMID: 15629448
  34. The amount of peptidyl arginine deiminase type II enzyme and citrullinated myelin basic protein was increased in multiple sclerosis PMID: 17469138
  35. PAD-2 & PAD-4 are only isotypes expressed in synovial tissue in rheumatoid arthritis & other arthritides; inflammatory cells are major source, but PAD-4 also comes from hyperplastic synoviocytes; both isotypes probably involved in citrullination of fibrin PMID: 17968929
  36. These data provide new structure-function dimensions for chemokines in leukocyte mobilization, disclosing an anti-inflammatory role for PAD. PMID: 18645041
  37. The citrullinating enzyme PAD-4 was detected in synovial fluid from patients with rheumatoid arthritis and spondylarthritides. PMID: 18668562
  38. Results describe the in vitro kinetic properties of the human peptidylarginine deiminase isoform 2 (hPAD2), and explore the putative inhibitory action of the methyl ester side chain of paclitaxel. PMID: 18923545

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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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