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Merck
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Key Documents

AV41699

Sigma-Aldrich

Anti-PKLR antibody produced in rabbit

IgG fraction of antiserum

Sinónimos:

Anti-PK1, Anti-PKL, Anti-Pyruvate kinase, liver and RBC, Anti-RPK

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

100

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

58 kDa

species reactivity

human, rat, pig, rabbit, bovine, dog, mouse

concentration

0.5 mg - 1 mg/mL

technique(s)

immunohistochemistry: suitable
western blot: suitable

NCBI accession no.

NP_000289

UniProt accession no.

P30613-2

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PKLR(5313)

Categorías relacionadas

General description

Pyruvate kinase (PKLR) is a liver/erythrocyte-specific enzyme that exists as a tetramer. It comprises structural and functional domains namely N. A and C domains. The C domain is erythrocyte-specific and the A domain is active site residues. The PKLR gene is mapped to human chromosome 1q22.

Immunogen

Synthetic peptide directed towards the N terminal region of human PKLR

Application

Anti-PKLR antibody produced in rabbit has been used in western blotting.

Biochem/physiol Actions

Pyruvate kinase (PKLR) is needed for energy generation in erythrocytes. Deficiency of PKLR in mice reduces the risk of blood-stage malarial parasite Plasmodium chabaudi induced infection.

Sequence

Synthetic peptide located within the following region: STSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVRE

Physical form

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

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.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Daiki Nakatsu et al.
Proceedings of the National Academy of Sciences of the United States of America, 112(10), E1067-E1076 (2015-02-26)
Increase in the concentration of plasma L-cysteine is closely associated with defective insulin secretion from pancreatic β-cells, which results in type 2 diabetes (T2D). In this study, we investigated the effects of prolonged L-cysteine treatment on glucose-stimulated insulin secretion (GSIS)
Rebekah van Bruggen et al.
PloS one, 10(12), e0144555-e0144555 (2015-12-15)
Pyruvate kinase (PKLR) is a critical erythrocyte enzyme that is required for glycolysis and production of ATP. We have shown that Pklr deficiency in mice reduces the severity (reduced parasitemia, increased survival) of blood stage malaria induced by infection with
Nicholas Wong et al.
International journal of cell biology, 2013, 242513-242513 (2013-03-12)
Aerobic glycolysis is the dominant metabolic pathway utilized by cancer cells, owing to its ability to divert glucose metabolites from ATP production towards the synthesis of cellular building blocks (nucleotides, amino acids, and lipids) to meet the demands of proliferation.
Erin J Stephenson et al.
Nature communications, 13(1), 6062-6062 (2022-10-14)
Almost all effective treatments for non-alcoholic fatty liver disease (NAFLD) involve reduction of adiposity, which suggests the metabolic axis between liver and adipose tissue is essential to NAFLD development. Since excessive dietary sugar intake may be an initiating factor for
Hua-Lin Zhou et al.
Nature, 565(7737), 96-100 (2018-11-30)
Endothelial nitric oxide synthase (eNOS) is protective against kidney injury, but the molecular mechanisms of this protection are poorly understood1,2. Nitric oxide-based cellular signalling is generally mediated by protein S-nitrosylation, the oxidative modification of Cys residues to form S-nitrosothiols (SNOs).

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