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Product listing: AMPK Subunit Antibody Sampler Kit, UniProt ID O43741 #9839 to ACSL1 (D2H5) Rabbit mAb, UniProt ID P33121 #9189

The AMPK Subunit Antibody Sampler Kit provides an economical means to investigate the role played by all AMPK subunits in cellular energy homeostasis. The kit contains enough primary and secondary antibodies to perform two Western blots with each antibody.

Background: AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle (1,2). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (1).

This peptide is used specifically to block AMPKβ 1/2 (57C12) Rabbit mAb #4150 reactivity.

Background: AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle (1,2). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (1).

The AS160 Signaling Antibody Sampler Kit provides an economical means of detecting select components involved in the AS160 signaling pathway. The kit contains enough primary antibodies to perform at least two western blot experiments per antibody.

Background: Insulin is a major hormone controlling critical energy functions, such as glucose and lipid metabolism. Insulin binds to and activates the insulin receptor (IR) tyrosine kinase, which phosphorylates and recruits adaptor proteins. The signaling pathway initiated by insulin and its receptor stimulates glucose uptake in muscle cells and adipocytes through translocation of the Glut4 glucose transporter from the cytoplasm to the plasma membrane (1). A 160 kDa substrate of the Akt Ser/Thr kinase (AS160, TBC1D4) is a Rab GTPase-activating protein that regulates insulin-stimulated Glut4 trafficking. AS160 is expressed in many tissues including brain, kidney, liver, and brown and white fat (2). Multiple Akt phosphorylation sites have been identified on AS160 in vivo, with five sites (Ser318, Ser570, Ser588, Thr642, and Thr751) showing increased phosphorylation following insulin treatment (2,3). Studies using recombinant AS160 demonstrate that insulin-stimulated phosphorylation of AS160 is a crucial step in Glut4 translocation (3) and is reduced in some patients with type 2 diabetes (4). The interaction of 14-3-3 regulatory proteins with AS160 phosphorylated at Thr642 is a necessary step for Glut4 translocation (5). Phosphorylation of AS160 by AMPK is involved in the regulation of contraction-stimulated Glut4 translocation (6).

The C/EBP Antibody Sampler Kit provides an economical means of evaluating the C/EBP family of transcription factors and several phosphorylation sites that are involved in its activation. The kit includes enough antibody to perform two western blot experiments with each primary antibody.
$118
10 western blots
200 µl
Nonphosphorylated AMPK Control Cell Extracts: Total cell extracts from C2C12 cells, prepared with CIP/λ phosphatase, serve as a negative control. Supplied in SDS Sample Buffer.Phosphorylated AMPK Control Cell Extracts: Total cell extracts from C2C12 cells, prepared by serum starvation, serve as a positive control. Supplied in SDS Sample Buffer.
APPLICATIONS

Application Methods: Western Blotting

Background: AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6,7). Phosphorylation at Ser108 of the β1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKγ subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle (1,2). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (1).

Molecular Weight:258.24 g/mol

Background: AICAR (5-Aminoimidazole-4-carboxyamide ribonucleoside) is an adenosine analog taken up by muscle and phosphorylated to form 5-aminoimidazole-4-carboxamide-1--D-ribofuranosyl-5'-monophosphate (ZMP), which stimulates AMPK activity and glucose transport in skeletal muscle (1). AICAR has been used in studies measuring glucose uptake, diabetes and insulin resistance, and energy regulation during exercise. AICAR acts by entering nucleoside pools and significantly increasing levels of adenosine during periods of ATP breakdown (2).

Molecular Weight: 792.3 g/mol(Average based on isomer content)

Background: During oxidative phosphorylation in mitochondria, the electron transport system pumps H+ from the matrix into the intermembrane compartment. This process generates a H+ gradient across the mitochondrial inner membrane. This H+ gradient is used to drive mitochondrial FoF1 ATPase to convert ADP to ATP. Oligomycin, an antibiotic from Streptomyces diastatochromogenes, blocks oxidative phosphorylation by binding to the Fo part of the ATPase to inhibit its activity (1-3).

This peptide is used specifically to block COX IV Antibody #4844 and COX IV (3E11) Rabbit mAb #4850 reactivity.

Background: Cytochrome c oxidase (COX) is a hetero-oligomeric enzyme consisting of 13 subunits localized to the inner mitochondrial membrane (1-3). It is the terminal enzyme complex in the respiratory chain, catalyzing the reduction of molecular oxygen to water coupled to the translocation of protons across the mitochondrial inner membrane to drive ATP synthesis. The 3 largest subunits forming the catalytic core are encoded by mitochondrial DNA, while the other smaller subunits, including COX IV, are nuclear-encoded. Research studies have shown that deficiency in COX activity correlates with a number of human diseases (4). The COX IV antibody can be used effectively as a mitochondrial loading control in cell-based research assays.

The Fatty Acid and Lipid Metabolism Antibody Sampler Kit provides an economical means to evaluate key proteins involved in fatty acid and lipid metabolism. This kit includes enough primary antibody to perform two western miniblot experiments with each primary antibody.
$524
100 assays (96 well format)
1 Kit
The Glucose-6-Phosphate Dehydrogenase (G6PD) Activity Assay Kit contains the necessary reagents for rapid, sensitive, and simple detection of G6PD activity in various samples. In the assay, glucose-6-phosphate (G6P), in the presence of NADP, is oxidized by G6PD to generate 6-phosphogluconolactone and NADPH. The generated NADPH is then amplified by the diaphorase-cycling system to produce highly fluorescent resorufin molecules (see Figure 1). The relative fluorescent units (RFU) can then be determined using a plate reader with excitation about 540 nm and emission about 590 nm. The magnitude of RFU is proportional to G6PD activity in the sample.
REACTIVITY
All Species Expected

Background: Glucose-6-phosphate dehydrogenase (G6PD) catalyses the first, and rate-limiting, step of the pentose phosphate pathway (1). The NADPH generated from this reaction is essential to protect cells from oxidative stress (1). Research studies have shown that p53 interacts with G6PD and inhibits its activity, therefore suppressing glucose consumption through the pentose phosphate pathway (2). In cancer cells with p53 mutations, the increased glucose consumption is directed towards increased biosynthesis, which is critical for cancer cell proliferation (2).

The Glycolysis Antibody Sampler Kit provides an economical means to investigate select enzymes involved in glycolysis. The kit contains enough primary antibody to perform two western blot experiments with each primary antibody.
The Glycolysis II Antibody Sampler Kit provides an economical means to investigate select enzymes involved in glycolysis. The kit contains enough primary antibody to perform two western blot experiments per primary antibody.
$320
100 µg
This peptide is used to block IGF-I Receptor β Antibody #3027 reactivity in dot blot protocols.
APPLICATIONS

Application Methods: Immunohistochemistry (Paraffin)

Background: Insulin-like growth factor 1 (IGF-1) is a small (7.65 kDa) growth factor that interacts with both the IGF-1 receptor and the insulin receptor to control cell growth and apoptosis. Release of this endocrine hormone from the liver is stimulated by growth hormone produced in the anterior pituitary (1). Circulating IGF-1 is typically bound to one of six known IGF binding proteins (IGF-BP) (2). At target cells, the IGF-1 ligand binds IGF receptors (or insulin receptors) leading to receptor autophosphorylation and activation (3). Activated receptors mediate downstream signaling pathways (including Akt and MAPK) that regulate cell proliferation, apoptosis, development and longevity. Altered expression or mutation of IGF-1 is associated with several human disorders, including type I diabetes and various forms of cancer (4). Recombinant human IGF-1 has been used in clinical trials as a potential therapeutic agent in the treatment of human diseases (5).

Each control slide contains formalin fixed, paraffin-embedded cell pellets, LNCaP (LKB1 positive) and A549 (LKB1 negative), that serve as a control for LKB1 immunostaining.

Background: LKB1 (STK11) is a serine/threonine kinase and tumor suppressor that helps control cell structure, apoptosis and energy homeostasis through regulation of numerous downstream kinases (1,2). A cytosolic protein complex comprised of LKB1, putative kinase STRAD, and the MO25 scaffold protein, activates both AMP-activated protein kinase (AMPK) and several AMPK-related kinases (3). AMPK plays a predominant role as the master regulator of cellular energy homeostasis, controlling downstream effectors that regulate cell growth and apoptosis in response to cellular ATP concentrations (4). LKB1 appears to be phosphorylated in cells at several sites, including human LKB1 at Ser31/325/428 and Thr189/336/363 (5).Mutation in the corresponding LKB1 gene causes Peutz-Jeghers syndrome (PJS), an autosomal dominant disorder characterized by benign GI tract polyps and dark skin lesions of the mouth, hands, and feet (6). A variety of other LKB1 gene mutations have been associated with the formation of sporadic cancers in several tissues (7).

The Insulin Receptor Substrate Antibody Sampler Kit provides an economical means to investigate IRS-1 and IRS-2 signaling and phosphorylation within the cell. The kit contains enough antibody to perform two western blots with each primary antibody.

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

The IRS-1 Inhibition Antibody Sampler Kit provides an economical means to evaluate insulin signaling negative feedback loops via phosphorylation of various IRS-1 serine residues. The kit includes enough antibody to perform two western blot experiments with each primary antibody.
The Lipolysis Activation Antibody Sampler Kit provides an economical means to evaluate the activation status of multiple members of the lipolysis pathway, including phosphorylated HSL and perilipin. The kit includes enough antibody to perform two western mini-blot experiments with each primary antibody.
The Mitochondrial Dynamics Antibody Sampler Kit provides an economical means to examine signaling involved in mitochondrial dynamics. The kit contains enough primary antibody to perform two western blot experiments.

Background: Import of proteins into the mitochondria is regulated by the translocase of the outer mitochondrial membrane (TOM) complex, which facilitates transport through the outer mitochondrial membrane, and a complementary translocase of the inner membrane (TIM) complex, responsible for protein transport to the mitochondrial matrix. The TOM complex consists of the receptors Tom20, Tom22, and Tom70, and the channel-forming protein Tom40 (1). Tom20 is localized in the outer mitochondrial membrane and initially recognizes precursors with a presequence to facilitate protein import across the outer mitochondrial membrane (2).Changes in mitochondrial dynamics regulated by environmental cues affect mitochondrial size and shape and have been shown to dramatically impact mitochondrial metabolism, apoptosis, and autophagy (3). These processes are largely controlled by mitochondrial dynamin-related GTPases, including mitofusin-1, mitofusin-2, OPA1, and DRP1. DRP1 regulates mitochondrial fission, while the mitofusins and OPA1 control fusion at the outer and inner mitochondrial membrane, respectively. These proteins are tightly regulated. OPA1 activity is regulated through alternative splicing and post-translational modifications, including complex proteolytic processing by multiple proteases (4-9). In addition, OPA1 expression can be induced under conditions of metabolic demand through a pathway involving Parkin induced NF-κB activation (10). DRP1 is regulated in part through multiple phosphorylation sites (11). Phosphorylation of DRP1 at Ser616 by MAPK or during mitosis by CDKs stimulates mitochondrial fission (12-14). Mitochondrial fission factor (MFF) is a tail-anchored protein that resides within the outer mitochondrial membrane and is part of the mitochondrial fission complex. MFF participates in mitochondrial fission by serving as one of multiple receptors for the GTPase dynamin-related protein 1 (Drp1) (15-18). AMPK directly phosphorylates MFF at two sites to allow for enhanced recruitment of Drp1 to the mitochondria (19). 

The Mitochondrial Marker Antibody Sampler Kit provides an economical means to evaluate relevant mitochondial proteins. This kit contains enough primary antibody to perform two western blots per primary.
$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated 4F2hc/CD98 (D3F9D) XP® Rabbit mAb #47213.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: 4F2hc is a transmembrane protein that belongs to the solute carrier family. 4F2hc forms heterodimeric complexes with various amino acid transporters such as LAT1 and LAT2 and regulates uptake of amino acids (1-5). 4F2hc is one of the earliest expressed antigens on the surface of activated human lymphocytes (6), hence it is also named CD98. 4F2hc is expressed in all cell types with the exception of platelets, and is expressed at highest levels in the tubules of the kidney and the gastrointestinal tract (7,8). It is localized at the plasma membrane when associated with LAT1 or LAT2 (9) and at the apical membrane of placenta (10). Research studies have shown that 4F2hc is highly expressed in various tumors including glioma (11), ovarian cancer (12), and astrocytomas (13), and it has been implicated in tumor progression and correlated with poor outcome in patients with pulmonary neuroendocrine tumors (14). 4F2hc is also involved in integrin trafficking through association with β1 and β4 integrins, and regulates keratinocyte adhesion and differentiation (15).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: 4F2hc is a transmembrane protein that belongs to the solute carrier family. 4F2hc forms heterodimeric complexes with various amino acid transporters such as LAT1 and LAT2 and regulates uptake of amino acids (1-5). 4F2hc is one of the earliest expressed antigens on the surface of activated human lymphocytes (6), hence it is also named CD98. 4F2hc is expressed in all cell types with the exception of platelets, and is expressed at highest levels in the tubules of the kidney and the gastrointestinal tract (7,8). It is localized at the plasma membrane when associated with LAT1 or LAT2 (9) and at the apical membrane of placenta (10). Research studies have shown that 4F2hc is highly expressed in various tumors including glioma (11), ovarian cancer (12), and astrocytomas (13), and it has been implicated in tumor progression and correlated with poor outcome in patients with pulmonary neuroendocrine tumors (14). 4F2hc is also involved in integrin trafficking through association with β1 and β4 integrins, and regulates keratinocyte adhesion and differentiation (15).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: 4F2hc is a transmembrane protein that belongs to the solute carrier family. 4F2hc forms heterodimeric complexes with various amino acid transporters such as LAT1 and LAT2 and regulates uptake of amino acids (1-5). 4F2hc is one of the earliest expressed antigens on the surface of activated human lymphocytes (6), hence it is also named CD98. 4F2hc is expressed in all cell types with the exception of platelets, and is expressed at highest levels in the tubules of the kidney and the gastrointestinal tract (7,8). It is localized at the plasma membrane when associated with LAT1 or LAT2 (9) and at the apical membrane of placenta (10). Research studies have shown that 4F2hc is highly expressed in various tumors including glioma (11), ovarian cancer (12), and astrocytomas (13), and it has been implicated in tumor progression and correlated with poor outcome in patients with pulmonary neuroendocrine tumors (14). 4F2hc is also involved in integrin trafficking through association with β1 and β4 integrins, and regulates keratinocyte adhesion and differentiation (15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: 4F2hc is a transmembrane protein that belongs to the solute carrier family. 4F2hc forms heterodimeric complexes with various amino acid transporters such as LAT1 and LAT2 and regulates uptake of amino acids (1-5). 4F2hc is one of the earliest expressed antigens on the surface of activated human lymphocytes (6), hence it is also named CD98. 4F2hc is expressed in all cell types with the exception of platelets, and is expressed at highest levels in the tubules of the kidney and the gastrointestinal tract (7,8). It is localized at the plasma membrane when associated with LAT1 or LAT2 (9) and at the apical membrane of placenta (10). Research studies have shown that 4F2hc is highly expressed in various tumors including glioma (11), ovarian cancer (12), and astrocytomas (13), and it has been implicated in tumor progression and correlated with poor outcome in patients with pulmonary neuroendocrine tumors (14). 4F2hc is also involved in integrin trafficking through association with β1 and β4 integrins, and regulates keratinocyte adhesion and differentiation (15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Acetyl-CoA acetyltransferase 2 (ACAT2), also known as cytosolic acetoacetyl-CoA thiolase, plays a role in regulating lipid metabolism (1). It catalyzes the synthesis of acetoacetyl-CoA from two acetyl-CoA molecules, which is later converted into steroids (2).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytoplasmic acetyl-CoA synthetase (AceCS1) catalyzes the conversion of acetate and CoA to acetyl-CoA (1, 2). Acetyl-CoA synthesized by AceCS1 is used for fatty acid and lipid biosynthesis (1, 2). Studies suggest that this enzyme is regulated by sterol regulatory element-binding proteins (2). It was also shown that this enzyme is acetylated by protein acetyltransferases in cells (3, 4). SIRT1 deacetylates this enzyme at Lys661 resulting in its activation and the increase of fatty acid synthesis (3, 4).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the biosynthesis and oxidation of fatty acids (1). In rodents, the 265 kDa ACC1 (ACCα) form is primarily expressed in lipogenic tissues, while 280 kDa ACC2 (ACCβ) is the main isoform in oxidative tissues (1,2). However, in humans, ACC2 is the predominant isoform in both lipogenic and oxidative tissues (1,2). Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (3). ACC is a potential target of anti-obesity drugs (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the biosynthesis and oxidation of fatty acids (1). In rodents, the 265 kDa ACC1 (ACCα) form is primarily expressed in lipogenic tissues, while 280 kDa ACC2 (ACCβ) is the main isoform in oxidative tissues (1,2). However, in humans, ACC2 is the predominant isoform in both lipogenic and oxidative tissues (1,2). Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (3). ACC is a potential target of anti-obesity drugs (4,5).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Aconitase 2 (ACO2) catalyzes the conversion of citrate to isocitrate via cis-aconitate in the second step of the tricarboxylic acid (TCA) cycle (1,2). ACO2 is also an important regulator of iron homeostasis within cells (1-4). In addition, research studies have shown that this enzyme is deficient in the mitochondrial disease Friedreich's Ataxia (4,5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Mammalian long-chain acyl-CoA synthetase (ACSL) catalyzes the ligation of the fatty acid to CoA to form fatty acyl-CoA in a two-step reaction (1). Five isoforms of ACSL have been identified (1). These isoforms have different substrate preferences and subcellular localizations (1). Overexpression of ACSL1 results in changes to fatty acid metabolism in rat primary hepatocytes (2).