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Product listing: MEK1/2 Antibody, UniProt ID P36507 #9122 to Acetyl-Histone H2B (Lys12) (D7H4) Rabbit mAb (ChIP Formulated), UniProt ID P33778 #9072

$260
100 µl
$630
300 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat, S. cerevisiae

Application Methods: Immunoprecipitation, Western Blotting

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Maspin (SERPINB5) was discovered as a mammary tumor suppressor that is expressed in normal mammary epithelium but lost in most breast cancer cell lines (1). While maspin is related to the serpin family of serine protease inhibitors, it may not function as a protease inhibitor (2). It plays an essential role in embryonic development through critical roles in cell adhesion (3). While the precise mechanism of maspin signaling is unclear (4), the tumor suppressing activity of maspin has been attributed to its ability to inhibit cell invasion/metastasis (5,6) and angiogenesis (7), while promoting apoptosis (8). Nuclear translocation of active IKKα has been shown to repress maspin transcription and promote prostate cancer metastasis (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Microtubule associated proteins regulate the stability of microtubules and control processes such as cell polarity/differentiation, neurite outgrowth, cell division and organelle trafficking (1). The MARK (MAP/microtubule affinity-regulating kinases) family (MARK1-4) of serine/threonine kinases was identified based on their ability to phosphorylate microtubule-associated proteins (MAPs) including tau, MAP2 and MAP4 (2-6). MARK proteins phosphorylate MAPs within their microtubule binding domains, causing dissociation of MAPs from microtubules and increased microtubule dynamics (2-4). In the case of tau, phosphorylation has been hypothesized to contribute to the formation of neurofibrillary tangles observed in Alzheimer's disease. Overexpression of MARK leads to hyperphosphorylation of MAPs, morphological changes and cell death (4). The tumor suppressor kinase LKB1 phosphorylates MARK and the closely related AMP-kinases within their T-loops, leading to increased activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Maspin (SERPINB5) was discovered as a mammary tumor suppressor that is expressed in normal mammary epithelium but lost in most breast cancer cell lines (1). While maspin is related to the serpin family of serine protease inhibitors, it may not function as a protease inhibitor (2). It plays an essential role in embryonic development through critical roles in cell adhesion (3). While the precise mechanism of maspin signaling is unclear (4), the tumor suppressing activity of maspin has been attributed to its ability to inhibit cell invasion/metastasis (5,6) and angiogenesis (7), while promoting apoptosis (8). Nuclear translocation of active IKKα has been shown to repress maspin transcription and promote prostate cancer metastasis (9).

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

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

Background: The entry of eukaryotic cells into mitosis is regulated by cdc2 kinase activation, a process controlled at several steps including cyclin binding and phosphorylation of cdc2 at Thr161 (1). However, the critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of cdc2 at Thr14 and Tyr15 (2). Phosphorylation at Thr14 and Tyr15, resulting in inhibition of cdc2, can be carried out by Wee1 and Myt1 protein kinases (3,4). The cdc25 phosphatase may be responsible for removal of phosphates at Thr14 and Tyr15 and subsequent activation of cdc2 (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Blimp-1 (B lymphocyte-induced maturation protein) is a nuclear zinc-finger containing transcriptional repressor that is considered a master regulator of terminal B-cell development (1). The human homolog, PRDI-BF1, was identified by its ability to bind to the PRDI element on the IFN-β promoter and can inhibit virus-mediated IFN-β production (2). Expression of Blimp-1 is sufficient to drive terminal differentiation of BCL1 lymphoma cells into antibody secreting plasma cells, increasing the expression of the cell surface marker Syndecan-1 (1). In the B-cell lineage, Blimp-1 is specifically expressed in antibody-secreting cells including activated B and plasma cells. In addition, Blimp-1 has been found during macrophage differentiation (3) and in a subset of T-cells (4,5) suggesting it may play a wider role in homeostasis and differentiation (6). Mechanistically, Blimp-1 is thought to act by recruiting chromatin-modifying enzymes including histone deacetylases (7) and methyltransferases (8,9). Target genes of Blimp-1 transcriptional repression with potential roles in differentiation include c-Myc (10), CIITA (11), Pax5 (12), Spi-B, and Id3 (13).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The entry of eukaryotic cells into mitosis is regulated by cdc2 kinase activation, a process controlled at several steps including cyclin binding and phosphorylation of cdc2 at Thr161 (1). However, the critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of cdc2 at Thr14 and Tyr15 (2). Phosphorylation at Thr14 and Tyr15, resulting in inhibition of cdc2, can be carried out by Wee1 and Myt1 protein kinases (3,4). The cdc25 phosphatase may be responsible for removal of phosphates at Thr14 and Tyr15 and subsequent activation of cdc2 (1,5).

$122
20 µl
$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat, S. cerevisiae, Xenopus

Application Methods: Immunoprecipitation, Western Blotting

Background: The entry of eukaryotic cells into mitosis is regulated by cdc2 kinase activation, a process controlled at several steps including cyclin binding and phosphorylation of cdc2 at Thr161 (1). However, the critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of cdc2 at Thr14 and Tyr15 (2). Phosphorylation at Thr14 and Tyr15, resulting in inhibition of cdc2, can be carried out by Wee1 and Myt1 protein kinases (3,4). The cdc25 phosphatase may be responsible for removal of phosphates at Thr14 and Tyr15 and subsequent activation of cdc2 (1,5).

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

Application Methods: Western Blotting

Background: Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs, such as cell proliferation, differentiation, motility, and death. The p44/42 MAPK (Erk1/2) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines (1-3), and research investigators consider it an important target in the diagnosis and treatment of cancer (4). Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK or MAP3K), a MAP kinase kinase (MAPKK or MAP2K), and a MAP kinase (MAPK). Multiple p44/42 MAP3Ks have been identified, including members of the Raf family, as well as Mos and Tpl2/COT. MEK1 and MEK2 are the primary MAPKKs in this pathway (5,6). MEK1 and MEK2 activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187, respectively. Several downstream targets of p44/42 have been identified, including p90RSK (7) and the transcription factor Elk-1 (8,9). p44/42 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases, known as DUSPs or MKPs (10), along with MEK inhibitors, such as U0126 and PD98059.

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Mink, Monkey, Mouse, Pig, Rat, Zebrafish

Application Methods: Western Blotting

Background: Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs, such as cell proliferation, differentiation, motility, and death. The p44/42 MAPK (Erk1/2) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines (1-3), and research investigators consider it an important target in the diagnosis and treatment of cancer (4). Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK or MAP3K), a MAP kinase kinase (MAPKK or MAP2K), and a MAP kinase (MAPK). Multiple p44/42 MAP3Ks have been identified, including members of the Raf family, as well as Mos and Tpl2/COT. MEK1 and MEK2 are the primary MAPKKs in this pathway (5,6). MEK1 and MEK2 activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187, respectively. Several downstream targets of p44/42 have been identified, including p90RSK (7) and the transcription factor Elk-1 (8,9). p44/42 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases, known as DUSPs or MKPs (10), along with MEK inhibitors, such as U0126 and PD98059.

$303
200 µl
$717
600 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Mink, Monkey, Mouse, Pig, Rat, Zebrafish

Application Methods: Flow Cytometry, Western Blotting

Background: Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs, such as cell proliferation, differentiation, motility, and death. The p44/42 MAPK (Erk1/2) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines (1-3), and research investigators consider it an important target in the diagnosis and treatment of cancer (4). Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK or MAP3K), a MAP kinase kinase (MAPKK or MAP2K), and a MAP kinase (MAPK). Multiple p44/42 MAP3Ks have been identified, including members of the Raf family, as well as Mos and Tpl2/COT. MEK1 and MEK2 are the primary MAPKKs in this pathway (5,6). MEK1 and MEK2 activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187, respectively. Several downstream targets of p44/42 have been identified, including p90RSK (7) and the transcription factor Elk-1 (8,9). p44/42 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases, known as DUSPs or MKPs (10), along with MEK inhibitors, such as U0126 and PD98059.

The Phospho-Bad Antibody Sampler Kit provides an economical means to investigate the role of Bad protein in apoptosis. The kit contains primary and secondary antibodies to perform two Western blots with each antibody.

Background: Bad is a proapoptotic member of the Bcl-2 family that promotes cell death by displacing Bax from binding to Bcl-2 and Bcl-xL (1,2). Survival factors, such as IL-3, inhibit the apoptotic activity of Bad by activating intracellular signaling pathways that result in the phosphorylation of Bad at Ser112 and Ser136 (2). Phosphorylation at these sites promotes binding of Bad to 14-3-3 proteins to prevent an association between Bad with Bcl-2 and Bcl-xL (2). Akt phosphorylates Bad at Ser136 to promote cell survival (3,4). Bad is phosphorylated at Ser112 both in vivo and in vitro by p90RSK (5,6) and mitochondria-anchored PKA (7). Phosphorylation at Ser155 in the BH3 domain by PKA plays a critical role in blocking the dimerization of Bad and Bcl-xL (8-10).

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

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

Background: CREB is a bZIP transcription factor that activates target genes through cAMP response elements. CREB is able to mediate signals from numerous physiological stimuli, resulting in regulation of a broad array of cellular responses. While CREB is expressed in numerous tissues, it plays a large regulatory role in the nervous system. CREB is believed to play a key role in promoting neuronal survival, precursor proliferation, neurite outgrowth, and neuronal differentiation in certain neuronal populations (1-3). Additionally, CREB signaling is involved in learning and memory in several organisms (4-6). CREB is able to selectively activate numerous downstream genes through interactions with different dimerization partners. CREB is activated by phosphorylation at Ser133 by various signaling pathways including Erk, Ca2+, and stress signaling. Some of the kinases involved in phosphorylating CREB at Ser133 are p90RSK, MSK, CaMKIV, and MAPKAPK-2 (7-9).

$260
200 µl
$630
600 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Mink, Monkey, Mouse, Pig, Rat, S. cerevisiae, Zebrafish

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs, such as cell proliferation, differentiation, motility, and death. The p44/42 MAPK (Erk1/2) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines (1-3), and research investigators consider it an important target in the diagnosis and treatment of cancer (4). Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK or MAP3K), a MAP kinase kinase (MAPKK or MAP2K), and a MAP kinase (MAPK). Multiple p44/42 MAP3Ks have been identified, including members of the Raf family, as well as Mos and Tpl2/COT. MEK1 and MEK2 are the primary MAPKKs in this pathway (5,6). MEK1 and MEK2 activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187, respectively. Several downstream targets of p44/42 have been identified, including p90RSK (7) and the transcription factor Elk-1 (8,9). p44/42 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases, known as DUSPs or MKPs (10), along with MEK inhibitors, such as U0126 and PD98059.

$303
200 µl
$717
600 µl
APPLICATIONS
REACTIVITY
Bovine, C. elegans, D. melanogaster, Hamster, Human, Mink, Monkey, Mouse, Pig, Rat, Zebrafish

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

Background: Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs, such as cell proliferation, differentiation, motility, and death. The p44/42 MAPK (Erk1/2) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines (1-3), and research investigators consider it an important target in the diagnosis and treatment of cancer (4). Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK or MAP3K), a MAP kinase kinase (MAPKK or MAP2K), and a MAP kinase (MAPK). Multiple p44/42 MAP3Ks have been identified, including members of the Raf family, as well as Mos and Tpl2/COT. MEK1 and MEK2 are the primary MAPKKs in this pathway (5,6). MEK1 and MEK2 activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187, respectively. Several downstream targets of p44/42 have been identified, including p90RSK (7) and the transcription factor Elk-1 (8,9). p44/42 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases, known as DUSPs or MKPs (10), along with MEK inhibitors, such as U0126 and PD98059.

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated antibody (α-Tubulin (11H10) Rabbit mAb #2125).
APPLICATIONS
REACTIVITY
Bovine, D. melanogaster, Human, Monkey, Mouse, Pig, Rat, Zebrafish

Application Methods: Western Blotting

Background: The cytoskeleton consists of three types of cytosolic fibers: microtubules, microfilaments (actin filaments), and intermediate filaments. Globular tubulin subunits comprise the microtubule building block, with α/β-tubulin heterodimers forming the tubulin subunit common to all eukaryotic cells. γ-tubulin is required to nucleate polymerization of tubulin subunits to form microtubule polymers. Many cell movements are mediated by microtubule action, including the beating of cilia and flagella, cytoplasmic transport of membrane vesicles, chromosome alignment during meiosis/mitosis, and nerve-cell axon migration. These movements result from competitive microtubule polymerization and depolymerization or through the actions of microtubule motor proteins (1).

$282
1000 assays (96 well format)
1 Kit
The XTT Cell Viability Assay Kit is a colorimetric assay that detects the cellular metabolic activities. During the assay, the yellow tetrazolium salt XTT is reduced to a highly colored formazan dye by dehydrogenase enzymes in metabolically active cells. This conversion only occurs in viable cells and thus, the amount of the formazan produced is proportional to viable cells in the sample. The formazan dye formed in the assay is soluble in aqueous solution and can be quantified by measuring the absorbance at wavelength 450 nm using a spectrophotometer. An electron coupling reagent, such as PMS (N-Methylphenazonium methyl sulfate), can significantly improve the efficiency of XTT reduction in cells.
The StemLight™ Surface Marker Kit contains a panel of antibodies for the detection of antigens that are specifically expressed on the surface of human pluripotent cells. The kit can be used to track the pluripotent potential of human embryonic stem (ES) or induced pluripotent (iPS) cells. The loss of these markers indicates a loss of pluripotency or differentiation of the culture. The kit components are pre-optimized for parallel use in immunofluorescent analysis.

Background: Pluripotency is the ability of a cell to differentiate into cell types of the three germ layers, the endoderm, ectoderm, and mesoderm. It is a property shared by embryonic stem cells, embryonic carcinoma, and induced pluripotent cells.SSEA4, TRA-1-81, and TRA-1-60 antibodies recognize antigens expressed on the cell surface of all pluripotent cells. SSEA4 recognizes a glycolipid carbohydrate epitope (1). TRA-1-60(S) and TRA-1-81 antibodies recognize different proteoglycan epitopes on variants of the same protein, podocalyxin (2). These epitopes are neuraminidase sensitive and resistant, respectively. Reactivity of SSEA4, TRA-1-81 and TRA-1-60 antibodies with their respective cell surface markers are lost upon differentiation of pluripotent cells, corresponding with a loss of pluripotent potential (3).

StemLight™ Pluripotency Transcription Factor Antibody Kit contains a panel of antibodies for the detection of Oct-4, Nanog, and Sox2, key components of the core pluripotency transcription network in embryonic stem (ES) and induced pluripotent stem (iPS) cells. The kit can be used to track the pluripotent potential of human ES or iPS cells. The loss of these markers indicates a loss of pluripotency or differentiation of the culture. The kit components are pre-optimized for parallel use in immunofluorescent analysis at a standard dilution, but components are also validated for use in other applications - please refer to individual datasheet information for application specific recommendations. Enough reagents are provided for 160 immunofluorescent assays based on a working volume of 100 μl.

Background: Pluripotency is the ability of a cell to differentiate into cell types of the three germ layers, the endoderm, ectoderm and mesoderm. It is a property shared by embryonic stem cells, embryonic carcinoma, and induced pluripotent cells.Oct-4, Sox2, and Nanog are key transcriptional regulators that are highly expressed in pluripotent cells (1). Together they form a transcriptional network that maintains cells in a pluripotent state (2,3). Over-expression of Oct-4 and Sox2, along with KLF4 and c-Myc can induce pluripotency in both mouse and human somatic cells, highlighting their roles as key regulators of the transcriptional network necessary for renewal and pluripotency (4-5). It has also been demonstrated that overexpression of Oct-4, Sox2, Nanog, and Lin28 can induce pluripotency in human somatic cells (6). Upon differentiation of pluripotent cultures, expression of Oct-4, Nanog, and Sox2 is downregulated.

The StemLight™ iPS cell Reprogramming Antibody Kit contains a panel of antibodies for the detection of various proteins, combinations of which have been used to reprogram somatic cells to Induced Pluripotent Stem (iPS) cells. The kit can be used to track efficiency of expression of the reprogramming factors following transfection, viral transduction and other means of protein delivery. The kit components are pre-optimized for parallel use in immunofluorescent analysis at a standard dilution, but components are also validated for use in other applications --please refer to individual data sheet information for application specific recommendations. Enough reagents are provided for 160 immunofluorescent assays based on a working volume of 100 μl.

Background: Pluripotency is the ability of a cell to differentiate into cell types of the three germ layers, the endoderm, ectoderm and mesoderm. It is a property shared by embryonic stem cells, embryonic carcinoma and induced pluripotent cells.Oct-4, Sox2 and Nanog are key transcriptional regulators that are highly expressed in pluripotent cells (1). Together they form a transcriptional network that maintains cells in a pluripotent state (2,3). Over-expression of Oct-4 and Sox2 along with Klf4 and c- Myc can induce pluripotency in both mouse and human somatic cells, highlighting their roles as key regulators of the transcrip- tional network necessary for renewal and pluripotency (4-5). It has also been demonstrated that overexpression of Oct-4, Sox2, Nanog and Lin28 can induce pluripotency in human somatic cells (6). Upon differentiation of pluripotent cultures, expression of Oct-4, Nanog and Sox2 is downregulated.SSEA4, TRA-1-81 and TRA-1-60 antibodies recognize antigens expressed on the cell surface of all pluripotent cells. SSEA4 recognizes a glycolipid carbohydrate epitope (7). TRA-1-60(S) and TRA-1-81 antibodies recognize different proteoglycan epitopes on variants of the same protein, podocalyxin (8). These epitopes are neuraminadase sensitive and resistant, respectively. Reactivity of SSEA4, TRA-1-81 and TRA-1-60 antibodies with their respective cell surface markers are lost upon differentiation of pluripotent cells, corresponding with a loss of pluripotent potential (9).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Lysosome-associated membrane protein 1 and 2 (LAMP1 and LAMP2) are two abundant lysosomal membrane proteins (1,2). Both are transmembrane proteins and are heavily glycosylated at the amino-terminal luminal side of the lysosomal inner leaflet, which protects the proteins from proteolysis (3). The carboxy terminus of LAMP1 is exposed to the cytoplasm and contains a tyrosine sorting motif that targets LAMP to lysosomal membranes (4). LAMP1 and LAMP2 are 37% homologous in their protein sequences. Both LAMP1 and LAMP2 are involved in regulating lysosomal motility during lysosome-phagosome fusion and cholesterol trafficking (5,6).

$336
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1,2). The p300/CBP histone acetyltransferases acetylate multiple lysine residues in the amino terminal tail of histone H2B (Lys5, 12, 15, and 20) at gene promoters during transcriptional activation (1-3). Hyper-acetylation of the histone tails neutralizes the positive charge of these domains and is believed to weaken histone-DNA and nucleosome-nucleosome interactions, thereby destabilizing chromatin structure and increasing the access of DNA to various DNA-binding proteins (4,5). In addition, acetylation of specific lysine residues creates docking sites that facilitate recruitment of many transcription and chromatin regulatory proteins that contain a bromodomain, which binds to acetylated lysine residues (6). Histone H2B is mono-ubiquitinated at Lys120 during transcriptional activation by the RAD6 E2 protein in conjunction with the BRE1A/BRE1B E3 ligase (also known as RNF20/RNF40) (7). Mono-ubiquitinated histone H2B Lys120 is associated with the transcribed region of active genes and stimulates transcriptional elongation by facilitating FACT-dependent chromatin remodeling (7-9). In addition, it is essential for subsequent methylation of histone H3 Lys4 and Lys79, two additional histone modifications that regulate transcriptional initiation and elongation (10). In response to metabolic stress, AMPK is recruited to responsive genes and phosphorylates histone H2B at Lys36, both at promoters and in transcribed regions of genes, and may regulate transcriptional elongation (11). In response to multiple apoptotic stimuli, histone H2B is phosphorylated at Ser14 by the Mst1 kinase (12). Upon induction of apoptosis, Mst1 is cleaved and activated by caspase-3, leading to global phosphorylation of histone H2B during chromatin condensation. Interestingly, histone H2B is rapidly phosphorylated at irradiation-induced DNA damage foci in mouse embryonic fibroblasts (13). In this case, phosphorylation at Ser14 is rapid, depends on prior phosphorylation of H2AX Ser139, and occurs in the absence of apoptosis, suggesting that Ser14 phosphorylation may have distinct roles in DNA-damage repair and apoptosis.

$208
10 x 50 ug
500 µg
MitoTracker® Red CMXRos is well retained after fixation allowing for further sample processing and immunostaining. Excitation: 579 nm, Emission: 599 nm, Molecular Weight: 531.52
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunofluorescence (Immunocytochemistry)

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein K (hnRNP K) belongs to a family of RNA binding multiprotein complexes (hnRNP proteins) that facilitate pre-mRNA processing and transport of mRNA from the nucleus to cytoplasm (1-3). hnRNP K contains three unique structural motifs termed KH domains that bind poly(C) DNA and RNA sequences (4,5). Intricate architecture enables hnRNP K to facilitate mRNA biosynthesis (6), transcriptional regulation (7), and signal transduction. Research studies have shown that cytoplasmic hnRNP K expression is increased in oral squamous cell carcinoma and pancreatic cancer, and may be a potential prognostic factor (8,9). hnRNP K coordinates with p53 to regulate its target gene transcription in response to DNA damage. Proteasome degradation of hnRNP K is mediated by E3 ligase MDM2 (10). The interaction between hnRNP K and c-Src leads to hnRNP K phosphorylation, which allows for hnRNP K activation of silenced mRNA translation (11).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated eIF2α (D7D3) XP® Rabbit mAb #5324.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Phosphorylation of the eukaryotic initiation factor 2 (eIF2) α subunit is a well-documented mechanism to downregulate protein synthesis under a variety of stress conditions. eIF2 binds GTP and Met-tRNAi and transfers Met-tRNA to the 40S subunit to form the 43S preinitiation complex (1,2). eIF2 promotes a new round of translation initiation by exchanging GDP for GTP, a reaction catalyzed by eIF2B (1,2). Kinases that are activated by viral infection (PKR), endoplasmic reticulum stress (PERK/PEK), amino acid deprivation (GCN2), or heme deficiency (HRI) can phosphorylate the α subunit of eIF2 (3,4). This phosphorylation stabilizes the eIF2-GDP-eIF2B complex and inhibits the turnover of eIF2B. Induction of PKR by IFN-γ and TNF-α induces potent phosphorylation of eIF2α at Ser51 (5,6).

$132
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Pacific Blue™ fluorescent dye and tested in-house for direct flow cytometry analysis in human cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

$208
10 x 50 ug
500 µg
MitoTracker® Green FM is recommended for live cell imaging only; fixation with aldehydes or alcohols will inhibit staining. Excitation: 490 nm, Emission: 516 nm, Molecular Weight: 671.88 g/mol
APPLICATIONS

Application Methods: Immunofluorescence (Immunocytochemistry)

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Immunoprecipitation

Background: The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1,2). The p300/CBP histone acetyltransferases acetylate multiple lysine residues in the amino terminal tail of histone H2B (Lys5, 12, 15, and 20) at gene promoters during transcriptional activation (1-3). Hyper-acetylation of the histone tails neutralizes the positive charge of these domains and is believed to weaken histone-DNA and nucleosome-nucleosome interactions, thereby destabilizing chromatin structure and increasing the access of DNA to various DNA-binding proteins (4,5). In addition, acetylation of specific lysine residues creates docking sites that facilitate recruitment of many transcription and chromatin regulatory proteins that contain a bromodomain, which binds to acetylated lysine residues (6). Histone H2B is mono-ubiquitinated at Lys120 during transcriptional activation by the RAD6 E2 protein in conjunction with the BRE1A/BRE1B E3 ligase (also known as RNF20/RNF40) (7). Mono-ubiquitinated histone H2B Lys120 is associated with the transcribed region of active genes and stimulates transcriptional elongation by facilitating FACT-dependent chromatin remodeling (7-9). In addition, it is essential for subsequent methylation of histone H3 Lys4 and Lys79, two additional histone modifications that regulate transcriptional initiation and elongation (10). In response to metabolic stress, AMPK is recruited to responsive genes and phosphorylates histone H2B at Lys36, both at promoters and in transcribed regions of genes, and may regulate transcriptional elongation (11). In response to multiple apoptotic stimuli, histone H2B is phosphorylated at Ser14 by the Mst1 kinase (12). Upon induction of apoptosis, Mst1 is cleaved and activated by caspase-3, leading to global phosphorylation of histone H2B during chromatin condensation. Interestingly, histone H2B is rapidly phosphorylated at irradiation-induced DNA damage foci in mouse embryonic fibroblasts (13). In this case, phosphorylation at Ser14 is rapid, depends on prior phosphorylation of H2AX Ser139, and occurs in the absence of apoptosis, suggesting that Ser14 phosphorylation may have distinct roles in DNA-damage repair and apoptosis.