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Product listing: Phospho-PKCδ (Ser359) (D2X1P) Rabbit mAb, UniProt ID Q05655 #14787 to PTP-PEST (D4W7W) Rabbit mAb, UniProt ID Q05209 #14735

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).

$489
96 assays
1 Kit
The PathScan® Total PD-L1 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of PD-L1 protein. A rabbit antibody toward intracellular PD-L1 has been coated onto the microwells. After incubation with cell lysates, PD-L1 protein is captured by the coated antibody. Following extensive washing, a mouse detection antibody toward extracellular PD-L1 is added to detect the captured PD-L1 protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for the developed color is proportional to the quantity of PD-L1 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Programmed cell death 1 ligand 1 (PD-L1, B7-H1, CD274) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses. The PD-L1 ligand binds the PD-1 transmembrane receptor and inhibits T cell activation. PD-L1 was discovered following a search for novel B7 protein homologs and was later shown to be expressed by antigen presenting cells, activated T cells, and tissues including placenta, heart, and lung (1-3). Similar in structure to related B7 family members, PD-L1 protein contains extracellular IgV and IgC domains and a short, cytoplasmic region. Research studies demonstrate that PD-L1 is expressed in several tumor types, including melanoma, ovary, colon, lung, breast, and renal cell carcinomas (4-6). Expression of PD-L1 in cancer is associated with tumor infiltrating lymphocytes, which mediate PD-L1 expression through the release of interferon gamma (7). Additional research links PD-L1 expression to cancers associated with viral infections (8,9).

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

Application Methods: Western Blotting

Background: Van Gogh-like proteins (VANGL1, VANGL2) are human orthologs of Drosophila Van Gogh (Vang/Stbm), a multi-pass transmembrane protein that is required to establish cell polarity in embryonic eyes, legs, and bristles (1,2). As in Drosophila, mammalian VANGL proteins are core components of the planar cell polarity (PCP) pathway that promotes asymmetric orientation of cells across a planar surface, and drives convergence-extension movements that are critical for tissue morphogenesis (3). Mutations in the human VANGL1 gene have been identified in patients diagnosed with neural tube defects (e.g., spina bifida), providing evidence that VANGL1 plays a role in human embryonic morphogenesis (4,5). These findings are supported by genetic studies in mice, where mutations in both Vangl1 and Vangl2 result in neural tube defects (6,7). A possible role for VANGL in tumor progression is suggested by an increased expression of VANGL1 mRNA in breast cancer patients with an elevated risk of relapse (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Cystathionine beta-synthase (CBS) is a key enzyme involved in sulfur amino acid metabolism because it catalyzes the formation of cystathionine from serine and homocysteine (1,2). The CBS protein contains a heme-binding domain that modulates enzyme activity by sensing redox changes or carbon monoxide binding (1). S-adenosylmethionine binds the carboxyl-terminal CBS domain to allosterically regulate CBS catalytic activity (3,4). In addition to catalyzing cystathionine formation, CBS also catalyzes the generation of hydrogen sulfide, a neuromodulator in the brain, through alternative reactions (5,6). Mutations in the corresponding CBS gene result in homocystinuria, an autosomal recessive disorder characterized by abnormal sulfur metabolism, mental retardation, eye anomalies, and vascular disease (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Fatty acid binding proteins (FABPs) are cytoplasmic lipid chaperones that bind fatty acids and lipids for transport to various cellular components (1,2). Research studies demonstrate differential FABP expression in several types of tumors and their normal-cell counterparts (3). Fatty acid binding protein 3 (FABP3) is predominantly expressed in heart, skeletal muscle, brain, and mammary gland (4). FABP3 may play a role in supplying energy to the heart and other tissues (5). The release of FABP3 from the heart upon infarction is used as a serum marker for myocardial stress and cardiotoxicity (6). Additional studies suggest that FABP3 is a potential tumor suppressor in breast cancer (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Transcription factor E3 (TFE3) is a member of a family of basic helix-loop-helix leucine zipper transcription factors that includes MITF, TFEB, TFE3, and TFEC. Members of this family form heterodimers with each other, bind the same DNA sequences, and undergo the same types of post-translational modifications, including sumoylation (1). Research studies indicate that TFE3 and other family members play roles in development, organelle biogenesis, nutrient sensing, autophagy, and energy metabolism (2,3). Additional studies report that TFE3 controls the gate for pluripotent cells to exit the state of pluripotency prior to differentiation (4). Translocations involving the TFE3 gene region have been identified in a number of tumors, including sporadic renal cell tumors. Several specific translocations that result in kidney cancer and involve the TFE3 gene have been described and characterized in detail (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Synoviolin-1 (SYVN1/HRD1) is a RING-type E3 ubiquitin-protein ligase and major component of the endoplasmic reticulum (ER) quality control system that is involved in the ubiquitin-dependent degradation of misfolded proteins (1). SYVN1 is a multispanning ER membrane protein whose expression is upregulated at the protein level under conditions that promote ER stress (1-4). Research studies have shown that SYVN1 is an anti-apoptotic factor that is implicated in the pathogenesis of arthropathy by promoting synovial hyperplasia (5). Furthermore, gene-targeting studies have demonstrated that SYVN1 expression is indispensable for embryogenesis (6).

$232
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PD-L1 (E1L3N®) XP® Rabbit mAb #13684.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Programmed cell death 1 ligand 1 (PD-L1, B7-H1, CD274) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses. The PD-L1 ligand binds the PD-1 transmembrane receptor and inhibits T cell activation. PD-L1 was discovered following a search for novel B7 protein homologs and was later shown to be expressed by antigen presenting cells, activated T cells, and tissues including placenta, heart, and lung (1-3). Similar in structure to related B7 family members, PD-L1 protein contains extracellular IgV and IgC domains and a short, cytoplasmic region. Research studies demonstrate that PD-L1 is expressed in several tumor types, including melanoma, ovary, colon, lung, breast, and renal cell carcinomas (4-6). Expression of PD-L1 in cancer is associated with tumor infiltrating lymphocytes, which mediate PD-L1 expression through the release of interferon gamma (7). Additional research links PD-L1 expression to cancers associated with viral infections (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CEACAM1 (also known as C-CAM and CD66a) is a member of CEA-related cell-adhesion molecule (CEACAM) subfamily of the carcinoembryonic antigen (CEA) family (1). CEACAM1 is expressed by certain epithelial, endothelial, lymphoid, and myeloid cells. Human CEACAM1 has many different splice variants; the abundance of CEACAM1 and the relative ratio of the different isoforms varies markedly among cell types and may be regulated in a context-dependent fashion. The isoforms with long (L) and short (S) cytoplasmic tails have different signaling properties. Notably, L isoforms contain a functional ITIM (immunoreceptor tyrosine-based inhibitory motif) and several serine and threonine residues that could serve as potential phosphorylation targets. The extracellular domain of CEACAM1 is heavily glycosylated, making its apparent molecular weight during electrophoresis much larger than its predicted size (57.6 kDa) (2). CEACAM1 mediates intercellular adhesion through homo- and heterophilic interaction with other members of the CEACAM family. Studies indicate that CEACAM1 plays important roles in angiogenesis, neovascularization, insulin signaling, T cell signaling, and tumorigenesis (3-8). In addition, CEACAM1 can function as a receptor for several microbial pathogens (9,10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: SH2 domain-containing leukocyte protein of 76 kDa (SLP-76) is a hematopoietic adaptor protein that is important in multiple biochemical signaling pathways and necessary for T cell development and activation (1). ZAP-70 phosphorylates SLP-76 and LAT as a result of TCR ligation. SLP-76 has amino-terminal tyrosine residues followed by a proline rich domain and a carboxy-terminal SH2 domain. Phosphorylation of Tyr113 and Tyr128 result in recruitment of the GEF Vav and the adapter protein Nck (2). TCR ligation also leads to phosphorylation of Tyr145, which mediates an association between SLP-76 and Itk, which is accomplished in part via the proline rich domain of SLP-76 and the SH3 domain of ITK (3). Furthermore, the proline rich domain of SLP-76 binds to the SH3 domains of Grb2-like adapter Gads (3,4). In resting cells, SLP-76 is predominantly in the cytosol. Upon TCR ligation, SLP-76 translocates to the plasma membrane and promotes the assembly of a multi-protein signaling complex that includes Vav, Nck, Itk and PLCγ1 (1). The expression of SLP-76 is tightly regulated; the protein is detected at very early stages of thymocyte development, increases as thymocyte maturation progresses, and is reduced as cells mature to CD4+ CD8+ double-positive thymocytes (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: IFIT1 (interferon-induced protein with tetratricopeptide repeats 1) belongs to the IFIT family of proteins, which consists of four members in humans (IFIT1, IFIT2, IFIT3, and IFIT5) and three members in mice (IFIT1, IFIT2, and IFIT3) (1). IFIT1 expression is induced by Type I Interferons resulting from viral infection (2). IFIT1 is an antiviral protein that directly binds viral RNA that has a 5’ triphosphate group (PPP-RNA) (2). In humans, the viral PPP-RNA bound IFIT1 forms a complex with IFIT2 and IFIT3 to sequester the viral PPP-RNA and prevent replication (2). IFIT1 has also been shown to inhibit translation by binding to the eukaryotic initiation factor-3 (eIF-3) (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Nucleotide excision repair (NER) is a process by which cells identify and repair DNA lesions resulting from chemical or radiation exposure (1). XPC forms a complex with HR23B (2) that acts as a damage sensor due to its high affinity for geometry distorting DNA lesions. This complex localizes to sites of DNA damage and recruits the remaining members of the preincision complex necessary for initiation of NER (3). XPC is one of eight NER proteins (XPA-G, XPV) where defects result in Xeroderma pigmentosum, a disease characterized by sunlight sensitivity, a predisposition to cancer of exposed tissue, and, in some instances, neurological defects (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Phorbol-12-myristate-13-acetate-induced protein 1 (PMAIP1, Noxa) is a small protein that plays a key role in mediating apoptotic signaling. Noxa is a pro-apoptotic Bcl-2 family protein that contains a single Bcl-2 homology (BH3) domain (1). Members of the “BH3-only” family (e.g. Noxa, Bad, Bim, Puma, Bid, Bik, and Hrk) are highly regulated proteins that induce apoptosis through BH3-dependent interaction with anti-apoptotic Bcl-2 family proteins (2). Noxa localizes to mitochondria and binds the anti-apoptotic proteins Mcl-1 and A1/Bfl-1, but does not bind to Bcl-2 or Bcl-xL (3). The Noxa protein competes with Mcl-1 for binding to mitochondrial Bak protein. Noxa was originally identified as a phorbol ester inducible protein that is highly expressed in adult T-cell leukemia cell lines (4). Several different stimuli, including DNA damage, hypoxia, interferon, viral infection, and double-stranded RNA, induce Noxa expression in cells. Higher levels of Noxa protein are typically found hematopoietic cells (3,5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Mcl-1 is an anti-apoptotic member of the Bcl-2 family originally isolated from the ML-1 human myeloid leukemia cell line during phorbol ester-induced differentiation along the monocyte/macrophage pathway (1). Similar to other Bcl-2 family members, Mcl-1 localizes to the mitochondria (2), interacts with and antagonizes pro-apoptotic Bcl-2 family members (3), and inhibits apoptosis induced by a number of cytotoxic stimuli (4). Mcl-1 differs from its other family members in its regulation at both the transcriptional and post-translational level. First, Mcl-1 has an extended amino-terminal PEST region, which is responsible for its relatively short half-life (1,2). Second, unlike other family members, Mcl-1 is rapidly transcribed via a PI3K/Akt dependent pathway, resulting in its increased expression during myeloid differentiation and cytokine stimulation (1,5-7). Mcl-1 is phosphorylated in response to treatment with phorbol ester, microtubule-damaging agents, oxidative stress, and cytokine withdrawal (8-11). Phosphorylation at Thr163, the conserved MAP kinase/ERK site located within the PEST region, slows Mcl-1 protein turnover (10) but may prime the GSK-3 mediated phosphorylation at Ser159 that leads to Mcl-1 destabilization (11). Mcl-1 deficiency in mice results in peri-implantation lethality (12). In addition, conditional disruption of the corresponding mcl-1 gene shows that Mcl-1 plays an important role in early lymphoid development and in the maintenance of mature lymphocytes (13).

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

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

Background: Vesicle transport through interaction with t-SNAREs homolog 1 (Vti1) has two protein members, Vti1a and Vti1b. Human Vti1 was first identified as a homolog of the yeast v-SNARE Vti1p and was able to functionally rescue the phenotype of Vti1p-deficient yeast (1). The mammalian proteins Vti1a and Vti1b exhibit distinct but overlapping localization. Vti1a and Vti1b are both localized in the trans-Golgi network, with Vti1a also found in the Golgi apparatus and Vti1b in endosomes (2). Vti1 proteins have been implicated in a number of protein-protein interactions with partners such as VAMP4, syntaxin 6, syntaxin 8, syntaxin 16, and synaptobrevin (2-4).

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

Application Methods: Western Blotting

Background: La-related protein 1 (LARP1) is a ubiquitously expressed RNA binding protein that promotes both global and specific mRNA translation in cells (1). LARP1 belongs to the La-related protein family and contains two RNA binding domains, a La motif (LAM), and a neighboring RNA recognition motif-like (RRM-L) domain (1). Research studies indicate that LARP1 acts downstream of mTORC1 to facilitate cell proliferation and growth by promoting global mRNA translation and translation of mRNAs containing a 5'Terminal Oligo-Pyrimidine (5'TOP) motif, which code for translational machinery components (2,3). At the molecular level, LARP1 associates with 5'TOP mRNAs and multiple translation machinery components to positively regulate translation (2,4). Additional studies show that LARP1 expression is upregulated in hepatocellular carcinoma (HCC) patients and that high LARP1 expression in HCC negatively correlates with survival rate (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Protein arginine N-methyltransferase 7 (PRMT7) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). The three types of PRMTs share the ability to mono-methylate arginine residues, but vary in their ability to generate differential methylation states (1-3). Mono-methylated arginine residues are further methylated by type I PRMTs to generate an asymmetric di-methyl arginine or by type II PRMTs to form a symmetric-dimethyl arginine. Type III methyltransferases are only able to mono-methylate arginine residues (1-3). Research studies indicate that PRMT7 is a type III PRMT that displays substrate specificity for an arginine-X-arginine (RXR) motif surrounded by several basic residues (4,5). PRMT7 interacts with a wide array of protein substrates and likely plays a role in many biological processes including pluripotency, neuronal differentiation, genomic instability, snRNP biogenesis, and breast cancer metastasis (6-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The megakaryoblastic leukemia proteins 1 and 2 (MKL1, MKL2) are myocardin-related transcription factors (MRTF-A, MRTF-B) that serve as actin-regulated transcription coactivators for the serum response factor (SRF). Interaction between G-actin and MKL proteins retains the coactivator within the cytoplasm of resting cells. Activated Rho-A promotes F-actin assembly and a reduction of the G-actin pool in serum-stimulated cells. This results in the accumulation of MKL proteins in the nucleus, where the coactivator associates with the SRF to activate target gene transcription and mediate multiple cellular processes (1-4). A number of other signaling pathways, including the TGFβ, BMP, and PDGF pathways, also make use of MKL-mediated activation of target gene transcription (5-9). Chromosomal translocations involving the genes encoding MKL1 and MKL2 have been identified in several cases of acute megakaryoblastic leukemia and chondroid lipoma (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The voltage gated potassium channel Kv7.2 (KCNQ2) associates with its family member Kv7.3 (KCNQ3) to form an M-channel that is involved in synaptic input response and sub-threshold excitability of neurons (1). This heteromeric channel generates the M-current, a slowly activating and deactivating potassium conductance that determines the neuronal excitability (2,3). Expression of these two M-channel proteins is mainly seen within the central nervous system, with both Kv7.2 and Kv7.3 expressed post-synaptically in the human cortex and hippocampus (4). The calcium-binding protein calmodulin binds two separate sites in Kv7.2 to influence exit of the channel protein from the endoplasmic reticulum and translocation to the plasma membrane (5). Mutations in the corresponding KCNQ2 gene cause benign familial neonatal seizures-1 (BFNS1), an autosomal dominant form of epilepsy characterized by seizure clusters closely following birth (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The p53 tumor suppressor protein regulates the cellular response to multiple stresses, including DNA damage and oxidative stress. Activation of p53 can lead to cell cycle arrest and DNA repair, or apoptosis (1). Activated p53 transcription factor regulates the expression of multiple genes that regulate cell metabolism and the cell cycle. One p53-inducible gene is C12orf5, which encodes for a fructose-2,6-bisphosphatase known as TIGAR. TP53-inducible glycolysis and apoptosis regulator (TIGAR) protects cells from oxidative stress as it negatively regulates glycolysis and reduces the production of reactive oxygen species (ROS) in cells (2,3). Research studies demonstrate that knockdown of TIGAR expression induces autophagy and apoptosis (4,5), and its expression protects cells from ROS-related cell death (6,7). Additional studies show that TIGAR promotes cell cycle arrest and supports dephosphorylation of the retinoblastoma (Rb) protein (8).

$19
25 ml
$82
125 ml
SignalStain® EDTA Unmasking Solution (10X) is used for antigen unmasking of formalin fixed, paraffin-embedded tissue sections or cell pellets in immunohistochemical assays (IHC-P). Cell Signaling Technology recommends the optimal unmasking reagent for each IHC-P approved antibody. Please consult the primary antibody datasheet to determine if this solution is recommended for your specific product.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunohistochemistry (Paraffin)

$25
25 ml
$93
125 ml
SignalStain® Citrate Unmasking Solution (10X) is used for antigen unmasking of formalin fixed, paraffin-embedded tissue sections or cell pellets in immunohistochemical assays (IHC-P). Cell Signaling Technology recommends the optimal unmasking reagent for each IHC-P approved antibody. Please consult the primary antibody datasheet to determine if citrate is recommended for your specific product.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunohistochemistry (Paraffin)

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: SH2 domain-containing leukocyte protein of 76 kDa (SLP-76) is a hematopoietic adaptor protein that is important in multiple biochemical signaling pathways and necessary for T cell development and activation (1). ZAP-70 phosphorylates SLP-76 and LAT as a result of TCR ligation. SLP-76 has amino-terminal tyrosine residues followed by a proline rich domain and a carboxy-terminal SH2 domain. Phosphorylation of Tyr113 and Tyr128 result in recruitment of the GEF Vav and the adapter protein Nck (2). TCR ligation also leads to phosphorylation of Tyr145, which mediates an association between SLP-76 and Itk, which is accomplished in part via the proline rich domain of SLP-76 and the SH3 domain of ITK (3). Furthermore, the proline rich domain of SLP-76 binds to the SH3 domains of Grb2-like adapter Gads (3,4). In resting cells, SLP-76 is predominantly in the cytosol. Upon TCR ligation, SLP-76 translocates to the plasma membrane and promotes the assembly of a multi-protein signaling complex that includes Vav, Nck, Itk and PLCγ1 (1). The expression of SLP-76 is tightly regulated; the protein is detected at very early stages of thymocyte development, increases as thymocyte maturation progresses, and is reduced as cells mature to CD4+ CD8+ double-positive thymocytes (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Mitofusins are mitochondrial transmembrane GTPases that function to regulate mitochondrial fusion, a process that occurs in concert with mitochondrial division and is necessary for the maintenance of structural and genetic mitochondrial integrity (1,2). Two mitofusins have been described in mammals, mitofusin-1 and -2, which share 60% amino acid identity and appear to function coordinately to regulate mitochondrial fusion (3). Mitochondrial fusion is widely recognized as important for normal cell growth and development (4), and may have evolved as a mechanism to offset the deleterious effects of mtDNA mutations (3). Null mutations in either mitofusin are embryonic lethal in mice, whereas conditional knockout studies have shown that combined deletion of mitofusin-1 and mitofusin-2 in skeletal muscle results in severe mitochondrial dysfunction (3).

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

Application Methods: Western Blotting

Background: The PAF (RNA polymerase II (RNAPII) associated factor) complex was initially identified in yeast and is comprised of subunits PAF1, Leo1, Ctr9, Cdc73, RTF1 and Ski8 (1,2). The PAF complex plays an important role in transcription initiation and elongation by RNAPII by regulating the establishment of proper histone modifications such as histone H2B ubiquitination and the recruitment of the histone chaperone FACT (facilitates chromatin transcription) (3-5). The PAF complex also plays a role in mRNA processing and maturation by interacting with and recruiting the cleavage and polyadenylation specificity factor and cleavage stimulation factor complexes via the Cdc73 subunit (6,7). In addition, the Ski8 subunit of the PAF complex is part of the hSKi complex that regulates RNA surveillance, suggesting an important function of the complex in coordinating events associated with proper RNA maturation during transcription (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation, but it has also been associated with a number of physiological processes including development, differentiation, neurodegenerative diseases, infection, and cancer (3). Autophagy marker Light Chain 3 (LC3) was originally identified as a subunit of microtubule-associated proteins 1A and 1B (termed MAP1LC3) (4) and subsequently found to contain similarity to the yeast protein Apg8/Aut7/Cvt5 critical for autophagy (5). Three human LC3 isoforms (LC3A, LC3B, and LC3C) undergo post-translational modifications during autophagy (6-9). Cleavage of LC3 at the carboxy terminus immediately following synthesis yields the cytosolic LC3-I form. During autophagy, LC3-I is converted to LC3-II through lipidation by a ubiquitin-like system involving Atg7 and Atg3 that allows for LC3 to become associated with autophagic vesicles (6-10). The presence of LC3 in autophagosomes and the conversion of LC3 to the lower migrating form, LC3-II, have been used as indicators of autophagy (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: PTP-PEST is a ubiquitously expressed cytosolic protein tyrosine phosphatase with multiple proline-rich regions that appear to be the docking sites for PTP-PEST binding partners or substrates (1). PTP-PEST regulates fibroblast adhesion, migration, and cytokinesis through its association with and dephosphorylation of p130 Cas, paxillin, PSTPIP1, WASP, and other adhesion molecules (1-5). By modulating phosphorylation states of Shc, Pyk2, Fak, and WASP, PTP-PEST negatively regulates lymphocyte activation (1,6). In mammary epithelial cells, EGF facilitates the dephosphorylation of Jak2 by PTP-PEST, thereby interfering with lactogenic hormone PRL signaling (7). PTP-PEST dephosphorylates c-Abl as well, which affects the phosphorylation states of PTP-PEST substrates such as paxillin, p130 Cas, Crk, and PSTPIP1 (8).PTP-PEST regulates adhesion and motility of cultured epithelial cells through modulation of Rho GTPase activity (9), and is required for integrin-mediated endothelial cell adhesion and migration (10).