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Key Documents

G8795

Sigma-Aldrich

Monoclonal Anti-GAPDH antibody produced in mouse

clone GAPDH-71.1, purified from hybridoma cell culture

Synonyme(s) :

Anti-G3PD, Anti-G3PDH, Anti-Glyceraldehyde-3-phosphate dehydrogenase

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified from hybridoma cell culture
purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

GAPDH-71.1, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~37 kDa

Espèces réactives

bovine, turkey, canine, chicken, monkey, mink, mouse, human, rabbit, rat, hamster

Ne doit pas réagir avec

prokaryotes

Conditionnement

antibody small pack of 25 μL

Concentration

~1 mg/mL

Technique(s)

immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 0.025-0.05 μg/mL using A431 total cell extract

Isotype

IgM

Numéro d'accès UniProt

Application(s)

research pathology

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... GAPDH(2597)
mouse ... Gapdh(14433)
rat ... Gapdh(24383)

Description générale

Monoclonal Anti-GAPDH (mouse IgM isotype) is derived from the hybridoma GAPDH-71.1 produced by the fusion of mouse myeloma cells (NS1 cells) and splenocytes from BALB/c mice immunized with rabbit GAPDH (glyceraldehyde-3-phosphate dehydrogenase). The gene glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is mapped to human chromosome 12p13. The protein localizes in the cytoplasm but can be translocated to the nucleus depending on cellular conditions.

Spécificité

Monoclonal Anti-GAPDH recognizes human, monkey, bovine, canine, rat, mouse, hamster, mink, rabbit, chicken, and turkey GAPDH. It does not cross-react with non-vertebrate and prokaryotic species.

Immunogène

Rabbit GAPDH.

Application

Monoclonal Anti-GAPDH antibody produced in mouse is suitable for western blotting using:
  • protein extracted from heart tissue of mice at a working dilution of 1:25,000
  • myelin and axogliasomal fractions from human CNS
  • nuclear and cytoplasmic fractions from TBP-13Q and TBP-105Q PC12 cells following recovery from heat shock
  • protein from bovine immortalized luteal endothelial cells
  • renal tubular epithelial cell extract
  • proteins from mouse embryonic fibroblasts
  • protein extract from ventricular myocardium tissues
  • A431 total cell extract at a working concentration of 0.025-0.05μg/mL
It is also suitable for immunostaining using leiomyomas and leiomyosarcomas. The antibody can also be used for immunocytochemistry, indirect ELISA and microarray.

Actions biochimiques/physiologiques

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a tetramer containing identical chains. It catalyzes the reversible oxidative phosphorylation of glyceraldehyde-phosphate, which is a critical energy-yielding step in carbohydrate metabolism. It binds to several proteins including actin, tubulin, amyloid precursor, polyglutamine peptides, DRPLA (dentatorubral-pallidoluysian atrophy), and huntingtin. Protein kinase Cι/λbinds and phosphorylates GAPDH. Phosphorylated GAPDH associates with cytoskeletal elements and controls microtubule dynamics in the early secretory pathway. Poly(ADP-ribose) polymerase-1 (PARP1) interacts with GAPDH and thereby mediates brain damage in the presence of oxidative/nitrosative stress. GAPDH forms a part of OCA-S, the multicomponent OCT1 (octamer-motif-binding factor) coactivator complex, which is involved in the S phase-dependent histone H2B transcription. This association is responsible for linking H2B transcriptional machinery to cell cycle regulation and to the cellular metabolic state. GAPDH is also a component of the functional GAIT (interferon-γ-activated inhibitor of translation) mRNP (messenger ribonucleoprotein). GAPDH expression is dysregulated during melanoma progression.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Stockage et stabilité

For continuous use, store at 2-8 °C for up to one month.
For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frostfree” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Frontiers in neurology and neuroscience research null
Gloria Ravegnini et al.
Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc, 26(5), 743-749 (2012-12-12)
Leiomyoma and leiomyosarcoma share morphological features and smooth muscle differentiation, and both arise most frequently within the uterine corpus of middle-aged women. However, they are considered biologically unrelated tumors due to their disparate clinical, cytogenetic, and molecular features. MED12, the
Frontiers in neurology and neuroscience research null
Xiaofeng Zuo et al.
The Journal of biological chemistry, 286(25), 22469-22477 (2011-05-06)
Primary cilia are found on many epithelial cell types, including renal tubular epithelial cells, where they participate in flow sensing. Disruption of cilia function has been linked to the pathogenesis of polycystic kidney disease. We demonstrated previously that the exocyst
Hang Zhao et al.
Free radical biology & medicine, 49(4), 641-648 (2010-06-01)
Methionine residues in protein can be oxidized by reactive oxygen species to generate methionine sulfoxide. Aerobic organisms have methionine sulfoxide reductases capable of reducing methionine sulfoxide back to methionine. Methionine sulfoxide reductase A acts on the S-epimer of methionine sulfoxide

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