Recombinant Human PAD2 Protein

Name: Recombinant Human PAD2 Protein
Brand: Beta LifeScience
SKU: BL-1410SG
Availability: InStock

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_007365
Synonym	PADI2; PDI2; PAD-H19
Background	PAD2 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. PAD2 has peptidylarginine deiminase activity against synthetic substrates (1). PAD2 is mainly expressed in the central nervous system, skeletal muscle, spinal cord, cerebrum, cerebellum, and submaxillary gland (2). PAD2 play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis.
Description	Recombinant full-length human PAD2 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	102 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 PAD2 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	HGNC: 18341 OMIM: 607935 KEGG: hsa:11240 STRING: 9606.ENSP00000364635 UniGene: Hs.33455
Tissue Specificity	Detected in keratinocytes in epidermis (at protein level).

Gene Functions References

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
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
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
Peptidyl arginine deiminase 2 (PADI2) is required for activation of androgen receptor (AR) signaling under androgen-deprived condition. PMID: 28819028
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
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
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
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
this study shows that a miR-4728 downregulates PADI2, a novel rheumatoid arthritis risk gene PMID: 26927695
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
Protein arginine deiminase 2 binds six calcium ions in an ordered fashion. PMID: 25621824
PAD2 activity was significantly higher in cell-free synovial fluid of rheumatoid arthritis patients compared to osteoarthritis patients. PMID: 26245941
PAD2 activity was detected in synovial fluid samples from patients with rheumatoid arthritis. PMID: 25475141
Report increased levels of extracellular PAD2 in the lungs of smokers. PMID: 25897949
PADI2 and vimentin participate in the apoptotic mechanisms of activated T lymphocytes. PMID: 24850148
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
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
Data suggest peptidylarginine deiminase 2 (PAD2) as a possible biomarker in various inflammatory diseases. PMID: 24384061
PAD2 and PAD4 have distinct substrate specificities. PMID: 24594197
These findings suggest that PAD2 and citrullinated proteins may play a key role in the brain pathology of prion diseases. [review] PMID: 23022892
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
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
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
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
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
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
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
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
PADI2 does not contribute to genetic susceptibility to schizophrenia. PMID: 19478818
PAD2 is expressed in human monocytic leukaemia THP-1 cells during differentiation into macrophages PMID: 19564157
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
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
hPADI2 and hPADI4 have different roles under physiological and pathological conditions PMID: 15629448
The amount of peptidyl arginine deiminase type II enzyme and citrullinated myelin basic protein was increased in multiple sclerosis PMID: 17469138
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
These data provide new structure-function dimensions for chemokines in leukocyte mobilization, disclosing an anti-inflammatory role for PAD. PMID: 18645041
The citrullinating enzyme PAD-4 was detected in synovial fluid from patients with rheumatoid arthritis and spondylarthritides. PMID: 18668562
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.

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