Recombinant Human N (DDAH1) Protein (His&Myc)

Name: Recombinant Human N (DDAH1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-05171P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human N (DDAH1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O94760
Target Symbol	DDAH1
Synonyms	DDAH; DDAH I; DDAH-1; DDAH1; DDAH1_HUMAN; DDAHI; Dimethylargininase 1; Dimethylargininase-1; Dimethylarginine dimethylaminohydrolase 1; N(G); N(G)-dimethylarginine dimethylaminohydrolase 1; NG NG dimethylarginine dimethylaminohydrolase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	AGLGHPAAFGRATHAVVRALPESLGQHALRSAKGEEVDVARAERQHQLYVGVLGSKLGLQVVELPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADGLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDIAANCIYLNIPNKGHVLLHRTPEEYPESAKVYEKLKDHMLIPVSMSELEKVDGLLTCCSVLINKKVDS
Expression Range	2-285aa
Protein Length	Full Length of Mature Protein
Mol. Weight	38.4 kDa
Research Area	Cardiovascular
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.
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	Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
Protein Families	DDAH family
Database References	HGNC: 2715 OMIM: 604743 KEGG: hsa:23576 STRING: 9606.ENSP00000284031 UniGene: Hs.713411
Tissue Specificity	Detected in brain, liver, kidney and pancreas, and at low levels in skeletal muscle.

Gene Functions References

MiR-21-mediated DDAH1/ADMA/NO signal pathway. PMID: 29682517
DDAH-1 expression is associated with promotion of angiogenesis stimulating factor VEGF. PMID: 28741166
These findings suggest that DDAH1 functions as a tumor suppressor in gastric cancer (GC) and may be exploited as a diagnostic and prognostic biomarker for GC. PMID: 28580735
Data demonstrate that DDAH1 deficiency promotes the epithelial to mesenchymal transition in renal proximal tubular epithelial cells and causes fibrosis, and oxidative stress in aging and diabetic kidneys. The study provides the first direct evidence that the DDAH1 has a marked effect on kidney fibrosis and oxidative stress induced by aging or diabetes. PMID: 28594240
Results confirmed DDAH1 3'-UTR as a target for miR-21, and endogenous miR-21 showed increased inhibitory effect on DDAH1-V3 transcript. PMID: 27663503
Inflammatory factors expressed in response to myocardial ischemia contributed to up-regulation of DDAH1. PMID: 28145161
DDAH1 plays dual roles in a particular matter-induced cell death in alveolar epithelial cells. PMID: 26996393
rs3087894 in DDAH1 was significantly associated with hypertension and showed conflicting results in different ethnic groups. This is therefore a candidate for further studies with the aim of helping to ascertain the mechanisms of hypertension in different populations. PMID: 26786611
wild-type rs480414 was 92% sensitive and 53% specific for pulmonary hypertension in bronchopulmonary dysplasia PMID: 26663142
results suggest that miR-21 may regulate renal fibrosis by the Wnt pathway via directly targeting DDAH1 PMID: 26455824
The most significant associations were detected for PECAM1*V/V + DDAH1*C (OR = 4.17 CI 1.56-11.15 Pperm = 0.005) PMID: 26662939
FoxO1 regulates asymmetric dimethylarginine via downregulation of dimethylaminohydrolase 1 in HUVECs and subjects with carotid atherosclerosis. PMID: 26226438
Genebased analyses revealed associations of the DDAH1 gene with longitudinal Blood Pressure phenotypes, associations with essential hypertension, Blood Pressure salt sensitivity, preeclampsia, or preclinical stages of atherosclerosis. PMID: 25424718
DDAH1 deficiency attenuates endothelial cell cycle progression and angiogenesis. PMID: 24260221
the advanced glycation end products-receptor for advanced glycation end products-mediated reactive oxygen species generation could be involved in endothelial dysfunction in diabetic end-stage renal disease patients PMID: 23766377
DDAH1 genotypes were closely related to asymmetric dimethylarginine levels, but not to measures of endothelium-dependent vasodilation in an elderly population. PMID: 23892448
Only the DDAH1-V1 transcript is responsible for ADMA metabolism, and transcript specific primers are recommended to determine DDAH1 mRNA expression. PMID: 23864585
Elevated asymmetric dimethylaginine is not a part of the proatherogenic risk profile in the young adult offspring of patients with premature Coronary artery disease. PMID: 23022711
A significant decrease in asymmetric dimethylarginine levels was found in ex-extremely low birth weight young adults compared to term birth weight young adults. PMID: 21420186
Data suggest that estradiol alone has no effect on DDAH/asymmetric dimethylarginine/nitric oxide pathway in arterial endothelium, but rather counters oxidized LDL; estradiol restores DDAH activity and prevents loss of eNOS (nitric oxide synthase 3). PMID: 22982060
DDAH1 gene DNA methylation is impoetant in the pathogenesis of idiopathic pulmonary fibrosis. PMID: 22700861
Genetic polymorphisms in DDAH genes influence serum ADMA levels in individuals with T1 diabetes mellitus. PMID: 22521321
High DDAH1 is associated with pediatric diffuse intrinsic pontine glioma. PMID: 22492959
Non-diabetic hypertensive subjects with a hypertensive response to exercise compared to those with normal response were characterized by augmented asymmetric dimethylarginine and osteoprotegerin levels. PMID: 21975354
did not find evidence for association with pre-eclampsia PMID: 21174581
In acute congestive heart failure acute renal impairment function and the modulation of metabolism and extracellular transport by the DDAH-1/CAT-1 system determine high ADMA and SDMA levels after therapy for acute congestive heart failure. PMID: 21722652
Data show that DDAH inhibition reduces fibroblast-induced collagen deposition in an ADMA-independent manner and reduces abnormal epithelial proliferation in an ADMA-dependent manner. PMID: 21677199
HDL significantly increased the attenuated endothelial cell NO production induced by ox-LDL, which was attributed to its effect on DDAH/ADMA pathway PMID: 21264497
Indicate that DDAH1 is required for metabolizing asymmetrical dimethylarginine and N(omega)-monomethyl-L-arginine. PMID: 21493890
Results provide evidence that SNP rs1241321 in DDAH1 is associated with type 2 diabetes and its long-term outcome. PMID: 21303562
DDAH1 exerts a unique role in activating Akt that affects endothelial function independently of degrading endogenous nitirc oxide synthase inhibitors. PMID: 21212404
Recent studies in this review suggest that DDAH may regulate endothelial nitric oxide activity and endothelial function through both asymmetric dimethylarginine-dependent and -independent mechanisms. PMID: 19682581
Expression of hDDAH1 messenger RNA is found in all organs of DDAH1 transgenic mice investigated, whereas human DDAH1 is absent in wild-type littermates. PMID: 19666120
Circulating methylarginine levels and the decline in renal function in patients with chronic kidney disease are modulated by DDAH1 polymorphisms. PMID: 20010544
Results suggest that the DDAH1 loss-of-function polymorphism is associated with both increased risk of thrombosis stroke and coronary artery disease in the Chinese Han population. PMID: 20167924
Recombinant human DDAH1 overexpression protects transgenic mice from adverse structural and functional changes in cerebral arterioles in hyperhomocysteinemia but not from accelerated carotid artery thrombosis induced by the HM/LF diet. PMID: 20019334
hydrolyzes methylated inhibitors of nitric oxide synthase is present in circulating human red blood cells PMID: 11811522
The first evidence of the importance of DDAH1 polymorphisms in pre-eclampsia susceptibility was provided. PMID: 15501905
By increasing the synthesis of the proangiogenic factor nitric oxide, DDAH promotes postnatal angiogenesis and arteriogenesis. PMID: 15781754
DDAH-1 and DDAH-2 messenger RNA and protein were demonstrated in first trimester placental tissue, primary extravillous trophoblasts and extravillous trophoblast-derived cell lines. PMID: 16920729
it is concluded that L-arginine regulates asymmetric dimethylarginine (ADMA) metabolism dose-dependently by competing for DDAH thus maintaining the metabolic balance of L-arginine and ADMA, and endothelial NO homeostasis PMID: 17075694
DDAH-1 activity leads to accumulation of asymmetric dimethylarginine and reduction in nitric oxide signaling. PMID: 17273169
Demonstrate a critical role for DDAH-1 and endogenous methylarginines in the pathogenesis of endothelial dysfunction. PMID: 17881609
human dimethylarginine dimethylaminohydrolase-1 is inhibited by S-nitroso-L-homocysteine and hydrogen peroxide PMID: 17895252
maintenance of normoglycemia and not glycemia-independent actions of insulin maintained dimethylarginine tissue levels by preserving physiological DDAH activity. PMID: 18292189

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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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