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Merck
CN

AV45673

抗 ARG1 (AB2) 兔抗

IgG fraction of antiserum

别名:

Anti-Arginase, liver

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关于此项目

NACRES:
NA.41
UNSPSC Code:
12352203
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产品名称

抗 ARG1 (AB2) 兔抗, IgG fraction of antiserum

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

35 kDa

species reactivity

dog, human

concentration

0.5 mg - 1 mg/mL

technique(s)

immunohistochemistry: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

Gene Information

human ... ARG1(383)

Application

Anti-ARG1 (AB2) antibody is used to tag arginase 1 proteins for detection and quantitation by Western blotting and in cells and tissues by immunohistochemical (IHC) techniques. It is used as a probe to study the role of arginase-1 in the management of nitrogen balance within mammalian cells.

Biochem/physiol Actions

Anti-ARG1 (AB2) antibody reacts with bovine, human, rabbit, pig, canine, mouse, and rat arginase-1 enzymes.
Arginase catalyzes the hydrolysis of arginine to ornithine and urea. The type I isoform of ARG1, is a cytosolic enzyme and expressed predominantly in the liver as a component of the urea cycle. Inherited deficiency of this enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia.Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exist (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type I isoform encoded by this gene, is a cytosolic enzyme and expressed predominantly in the liver as a component of the urea cycle. Inherited deficiency of this enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia.Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exist (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type I isoform encoded by this gene, is a cytosolic enzyme and expressed predominantly in the liver as a component of the urea cycle. Inherited deficiency of this enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

Arginase 1 (Arginase, liver) is a liver enzyme that completes the urea cycle in mammals by producing urea, which can be excreted, and L-ornithine through the hydrolysis of L-arginine. Defects in arginase 1 activity lead to a metabolic condition of hyperargininemia.

Immunogen

Synthetic peptide directed towards the C terminal region of human ARG1

Other Notes

Synthetic peptide located within the following region: LDIMEVNPSLGKTPEEVTRTVNTAVAITLACFGLAREGNHKPIDYLNPPK

Physical form

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

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存储类别

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Ewa Zajac et al.
Blood, 122(25), 4054-4067 (2013-11-01)
A proangiogenic function of tissue-infiltrating monocytes/macrophages has long been attributed to their matrix metalloproteinase-9 zymogen (proMMP-9). Herein, we evaluated the capacity of human monocytes, mature M0 macrophages, and M1- and M2-polarized macrophages to induce proMMP-9-mediated angiogenesis. Only M2 macrophages induced
Naohiko Nakamura et al.
BMC cancer, 19(1), 621-621 (2019-06-27)
Noninvasive biomarkers are urgently needed for optimal management of nonalcoholic fatty liver disease (NAFLD) for the prevention of disease progression into nonalcoholic steatohepatitis (NASH) and hepatocellular carcinoma (HCC). In order to identify the biomarkers, we generated the swine hepatocellular carcinoma
Milorad Dragić et al.
ASN neuro, 13, 17590914211044882-17590914211044882 (2021-09-28)
The present study examined the involvement of purinergic signaling components in the rat model of hippocampal degeneration induced by trimethyltin (TMT) intoxication (8 mg/kg, single intraperitoneal injection), which results in behavioral and neurological dysfunction similar to neurodegenerative disorders. We investigated spatial
Katarina Milosevic et al.
International journal of molecular sciences, 23(7) (2022-04-13)
Neuroinflammation and microglial activation, common components of most neurodegenerative diseases, can be imitated in vitro by challenging microglia cells with Lps. We here aimed to evaluate the effects of agmatine pretreatment on Lps-induced oxidative stress in a mouse microglial BV-2
Marija Jakovljevic et al.
Frontiers in neuroscience, 13, 410-410 (2019-05-21)
Purinergic signaling is critically involved in neuroinflammation associated with multiple sclerosis (MS) and its major inflammatory animal model, experimental autoimmune encephalomyelitis (EAE). Herein, we explored the expression of ectonucleoside triphosphate diphosphohydrolase1 (NTPDase1/CD39) in the spinal cord, at the onset (Eo)

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