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Product listing: Btk (D3H5) Rabbit mAb (Biotinylated), UniProt ID Q06187 #12624 to Rabbit (DA1E) mAb IgG XP® Isotype Control (Biotinylated) #4096

$305
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 Btk (D3H5) Rabbit mAb #8547.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Bruton's tyrosine kinase (Btk) is a member of the Btk/Tec family of cytoplasmic tyrosine kinases. Like other Btk family members, it contains a pleckstrin homology (PH) domain and Src homology SH3 and SH2 domains. Btk plays an important role in B cell development (1,2). Activation of B cells by various ligands is accompanied by Btk membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate (3-5). The membrane-localized Btk is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinases, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation (6,7). The activation of Btk is negatively regulated by PKCβ through phosphorylation of Btk at Ser180, which results in reduced membrane recruitment, transphosphorylation, and subsequent activation (8). The PKC inhibitory signal is likely to be a key determinant of the B cell receptor signaling threshold to maintain optimal Btk activity (8).

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

Application Methods: Western Blotting

Background: Mitotic control is important for normal growth, development, and maintenance of all eukaryotic cells. Research studies have demonstrated that inappropriate control of mitosis can lead to genomic instability and cancer (reviewed in 1,2). A regulator of mitosis, Greatwall kinase (Gwl), was first identified in Drosophila melanogaster (3). Subsequent studies showed that, based on sequence homology and function, microtubule-associated serine/threonine kinase-like (MASTL) is the human ortholog of Gwl (4). Regulation of MASTL/Gwl activation has been shown to be critical for the correct timing of mitosis. Research studies have shown that Gwl is activated by hyperphosphorylation (5). The phosphorylation of human Gwl at Thr194 and Thr207 by active cyclin B1-cdc2 leads to possible autophosphorylation at Ser875 (Ser883 in Xenopus), which stabilizes the kinase. Activated Gwl phosphorylates α-Endosulfine (ENSA) and cAMP-regulated phosphoprotein 19 (ARPP19) at Ser67 and Ser62, respectively. Phosphorylated ENSA and ARPP19 inhibit the activity of the B55 subunit-associated form of protein phosphatase 2A (PP2A-B55), allowing for complete phosphorylation of mitotic substrates by cyclin B1-cdc2 and mitotic entry. When Gwl is inactivated, PP2A-B55 reactivates, which leads to dephosphorylation of cyclin B1-cdc2 and mitotic exit (5,6, reviewed in 7).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated PDGF Receptor α (D13C6) XP® Rabbit mAb #5241.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Platelet derived growth factor (PDGF) family proteins exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor α (PDGFRα) and PDGF receptor β (PDGFRβ). PDGFRα and PDGFRβ share 75% to 85% sequence homology between their two intracellular kinase domains, while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRα homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRβ homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor α/β binds PDGF B, C, and D homodimers, as well as the PDGF AB heterodimer (2). PDGFRα and PDGFRβ can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules, such as GRB2, Src, GAP, PI3 kinase, PLCγ, and NCK. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRβ is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRβ (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRβ (7). Tyr740 is also required for PDGFRβ-mediated PI3 kinase activation (8).

PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.

Background: c-Jun is a member of the Jun family containing c-Jun, JunB, and JunD, and is a component of the transcription factor activator protein-1 (AP-1). AP-1 is composed of dimers of Fos, Jun, and ATF family members and binds to and activates transcription at TRE/AP-1 elements (reviewed in 1). Extracellular signals including growth factors, chemokines, and stress activate AP-1-dependent transcription. The transcriptional activity of c-Jun is regulated by phosphorylation at Ser63 and Ser73 through SAPK/JNK (reviewed in 2). Knock-out studies in mice have shown that c-Jun is essential for embryogenesis (3), and subsequent studies have demonstrated roles for c-Jun in various tissues and developmental processes including axon regeneration (4), liver regeneration (5), and T cell development (6). AP-1 regulated genes exert diverse biological functions including cell proliferation, differentiation, and apoptosis, as well as transformation, invasion and metastasis, depending on cell type and context (7-9). Other target genes regulate survival, as well as hypoxia and angiogenesis (8,10). Research studies have implicated c-Jun as a promising therapeutic target for cancer, vascular remodeling, acute inflammation, and rheumatoid arthritis (11,12).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Toll-like Receptor 9 (D9M9H) XP® Rabbit mAb #13674.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Members of the Toll-like receptor (TLR) family, named for the closely related Toll receptor in Drosophila, play a pivotal role in innate immune responses (1-4). TLRs recognize conserved motifs found in various pathogens and mediate defense responses (5-7). Triggering of the TLR pathway leads to the activation of NF-κB and subsequent regulation of immune and inflammatory genes (4). The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the Toll/Interleukin-1 receptor (TIR) domain (1). Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adaptor-like/TIR-associated protein (MAL/TIRAP), Toll-receptor-associated activator of interferon (TRIF), and Toll-receptor-associated molecule (TRAM) (8-10). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK (8,11-14). Activation of IKK leads to the degradation of IκB, which normally maintains NF-κB in an inactive state by sequestering it in the cytoplasm.

$489
96 assays
1 Kit
The PathScan® Phospho-LAT (Tyr191) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-LAT (Tyr191). A LAT mouse antibody has been coated onto the microwells. After incubation with cell lysates, LAT protein (phosphorylated and non-phosphorylated) is captured by the coated antibody. Following extensive washing, a phospho-LAT (Tyr191) rabbit detection antibody is added to detect the captured phospho-LAT (Tyr191). HRP-linked anti-rabbit antibody is then used to recognize the bound detection antibody. The HRP substrate TMB is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of phospho-LAT (Tyr191).Antibodies in kit are custom formulations specific to kit
REACTIVITY
Human

Background: LAT, a transmembrane adaptor protein expressed in T, NK and mast cells, is an important mediator for T cell receptor (TCR) signaling (1). Upon TCR engagement, activated Zap-70 phosphorylates LAT at multiple conserved tyrosine residues within SH2 binding motifs, exposing these motifs as the docking sites for downstream signaling targets (2,3). The phosphorylation of LAT at Tyr171 and Tyr191 enables the binding of Grb2, Gads/SLP-76, PLCγ1 and PI3 kinase through their SH2 domain and translocates them to the membrane. This process eventually leads to activation of the corresponding signaling pathways (1-4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: S-adenosylhomocysteine hydrolase-like protein 1 (AHCYL1) is a member of S-adenosylhomocysteine hydrolase family, which participates in the metabolism of S-adenosyl-L-homocysteine (1). Two Drosophila homologs of S-adenosylhomocysteine hydrolase-like proteins, dAhcyL1 and dAhcyL2, were identified as novel components of methionine metabolism (2). dAhcyL1 and dAhcyL2 function as dominant-negative regulators of S-adenosylhomocysteine hydrolase (2). Global down-regulation of both dAhcyL1 and dAhcyL2 extended life span (2). In addition, brain-specific down regulation of dAhcyL1 extended life span (2). AHCYL1 is also known as inositol 1,4,5-trisphosphate receptor (IP3R) binding protein released with IP3 (IRBIT) (1, 3). This protein binds to the endoplasmic reticulum calcium release channel IP3R and represses its acitivity (1, 3). As a multifunctional regulator, AHCYL1/IRBIT can also form a complex with and suppress the activity of ribonucleotide reductase, thereby influencing the balance of deoxynucleotide triphosphates essential for DNA replication and genomic integrity (4).

$122
20 µl
$307
200 µl
APPLICATIONS
REACTIVITY
Monkey, Mouse

Application Methods: Western Blotting

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

Application Methods: Immunoprecipitation, Western Blotting

Background: BAFF, a member of the TNF superfamily of proteins, is a homotrimeric transmembrane protein, which is cleaved to produce a soluble cytokine (1). BAFF may also further oligomerize into 60-mer structures (1). BAFF is expressed by monocytes, neutrophils, macrophages, dendritic cells, activated T cells, and epithelial cells (1,2). BAFF plays a key role in B cell development, survival, and activation (1,3,4). BAFF binds to three distinct receptors, BAFF-R, TACI, and BCMA (1). These receptors are differentially expressed during B cell development and among B cell subsets (1,2,4). While BAFF-R and BCMA bind to the homotrimeric form of BAFF, TACI only binds to membrane bound or higher order BAFF structures (1). The BAFF/ BAFF-R interaction activates both canonical and non-canonical NF-κB pathways, PI3K/Akt, and mTOR (2,4). Activation of the noncanonical NF-κB pathway via BAFF-R is negatively regulated by TRAF3 (5). Research studies have shown that elevated levels of BAFF may exacerbate many autoimmune disorders, making it a potential therapeutic target (2).

$303
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human

Application Methods: Western Blotting

Background: Endothelial nitric-oxide synthase (eNOS) is an important enzyme in the cardiovascular system. It catalyzes the production of nitric oxide (NO), a key regulator of blood pressure, vascular remodeling, and angiogenesis (1,2). The activity of eNOS is regulated by phosphorylation at multiple sites. The two most thoroughly studied sites are the activation site Ser1177 and the inhibitory site Thr495 (3). Several protein kinases including Akt/PKB, PKA, and AMPK activate eNOS by phosphorylating Ser1177 in response to various stimuli (4,5). In contrast, bradykinin and H2O2 activate eNOS activity by promoting both Ser1177 phosphorylation and Thr495 dephosphorylation (6,7).

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

Application Methods: Western Blotting

Background: BIRC6/BRUCE/APOLLON is a member of the inhibitor of apoptosis protein (IAP) family. BIRC6 is a huge 530 kDa membrane-associated protein with a single survivin-like baculoviral IAP repeat (BIR) domain at the amino terminus, and a ubiquitin-conjugating enzyme domain at the carboxy terminus (1-3). Several research studies support the notion that BIRC6 functions as a dual regulator of cell death and cell division (4-6), and BIRC6 is the only essential BIR-containing protein in mammalian cell growth and development (4,7). Research studies have documented the overexpression of BIRC6 in colon cancer stem cells and in other cancer cell lines (8,9). BIRC6 inhibits apoptosis by either 1) binding to and inhibiting caspases (10) or 2) ubiquitinating the IAP antagonist SMAC and the apoptosis initiator caspase 9, thereby targeting these proteins for proteasomal degradation (4,5). BIRC6 itself is regulated by ubiquitination and proteasomal degradation upon stimulation of apoptosis (7,11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: mRNA decapping is an important process in the mRNA turnover (1). DCP1A and DCP2 were identified as two human decapping enzymes and homologs of the better-characterized S. cerevisiae enzymes. Both putative decapping enzymes interact with the regulator of nonsense transcripts 1 (UPF1) and may be recruited by UPF1 or related proteins to mRNA sequences that contain premature termination codons (1). Additional research studies demonstrate that DCP1A, DCP1B (the homolog of DCP1A) and DCP2 colocalize with decapping activation factors RCK/p54 and Lsm proteins in cytoplasmic loci (2). DCP1A, DCP1B and DCP2 are components of cytoplasmic processing (P) bodies, with hyper-phosphorylation of DCP1A during mitosis suggesting a possible mechanism of P-body regulation during the cell cycle (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Legumain (LGMN) is an asparaginyl endopeptidase that mediates lysosomal processing of antigen for class II MHC presentation. Under normal conditions, LGMN is mostly found in lysosomes. However, its expression level, cellular compartmentalization, and function may change under certain conditions, including cancer (1, 2, 3). In colorectal cancer, LGMN is upregulated and is found extracellularly and in the nucleus in both primary tumors and colorectal cancer cell lines (4, 5). Legumain forms homodimers and may be activated by postranstranslational modifications, including autoproteolytic cleavage, as it moves from one cellular compartment to another (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: The yeast nucleotide excision repair (NER) radiation sensitive protein 23 (rad23) and its human homologs Rad23A (hHR23A) and Rad23B (hHR23B) are critical components of the cellular machinery that recognize DNA lesions and serve as receptors that target ubiquitinated substrates to the proteasome for degradation (1).

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

Application Methods: Western Blotting

Background: Glutamate oxaloacetate transaminase 1 (GOT1) catalyzes the interconversion of aspartate and oxaloacetate (1). The increased transamination primarily catalyzed by GOT1 leads to elevated levels of 2-hydroxyglutarate, which promotes methylation of the Foxp3 gene locus, inhibits Foxp3 expression and activates T helper 17 (TH17) cell differentiation (2). In addition, GOT1 is critical to the survival of cells with electron transport chain inhibition by generating aspartate, a metabolite determining the proliferation of these cells (3-4). Studies also show that GOT1 plays a key role in the noncanonical glutamine pathway that supports liver tumorigenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Methylation of DNA at cytosine residues in mammalian cells is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting and development (1,2). Three families of mammalian DNA methyltransferases have been identified: DNMT1, DNMT2 and DNMT3 (1,2). DNMT1 is constitutively expressed in proliferating cells and functions as a maintenance methyltransferase, transferring proper methylation patterns to newly synthesized DNA during replication. DNMT3A and DNMT3B are strongly expressed in embryonic stem cells with reduced expression in adult somatic tissues. DNMT3A and DNMT3B function as de novo methyltransferases that methylate previously unmethylated regions of DNA. DNMT2 is expressed at low levels in adult somatic tissues and its inactivation affects neither de novo nor maintenance DNA methylation. DNMT1, DNMT3A and DNMT3B together form a protein complex that interacts with histone deacetylases (HDAC1, HDAC2, Sin3A), transcriptional repressor proteins (RB, TAZ-1) and heterochromatin proteins (HP1, SUV39H1), to maintain proper levels of DNA methylation and facilitate gene silencing (3-8). Improper DNA methylation contributes to diseased states such as cancer (1,2). Hypermethylation of promoter CpG islands within tumor suppressor genes correlates with gene silencing and the development of cancer. In addition, hypomethylation of bulk genomic DNA correlates with and may contribute to the onset of cancer. DNMT1, DNMT3A and DNMT3B are over-expressed in many cancers, including acute and chronic myelogenous leukemias, in addition to colon, breast and stomach carcinomas (9-12).

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

Application Methods: Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The p21-activated kinase (PAK) family of serine/threonine kinases is engaged in multiple cellular processes, including cytoskeletal reorganization, MAPK signaling, apoptotic signaling, control of phagocyte NADPH oxidase, and growth factor-induced neurite outgrowth (1,2). Several mechanisms that induce PAK activity have been reported. Binding of Rac/Cdc42 to the CRIB (or PBD) domain near the amino terminus of PAK causes autophosphorylation and conformational changes in PAK (1). Phosphorylation of PAK1 at Thr423 by PDK induces activation of PAK1 (3). Several autophosphorylation sites have been identified, including Ser199 and Ser204 of PAK1 and Ser192 and Ser197 of PAK2 (4,5). Because the autophosphorylation sites are located in the amino-terminal inhibitory domain, it has been hypothesized that modification in this region prevents the kinase from reverting to an inactive conformation (6). Research indicates that phosphorylation at Ser144 of PAK1 or Ser139 of PAK3 (located in the kinase inhibitory domain) affects kinase activity (7). Phosphorylation at Ser21 of PAK1 or Ser20 of PAK2 regulates binding with the adaptor protein Nck (8). PAK4, PAK5, and PAK6 have lower sequence similarity with PAK1-3 in the amino-terminal regulatory region (9). Phosphorylation at Ser474 of PAK4, a site analogous to Thr423 of PAK1, may play a pivotal role in regulating the activity and function of PAK4 (10).

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

Application Methods: Western Blotting

Background: High temperature requirement protein A2 (HtrA2)/Omi is a serine protease with homology to the E. coli HtrA protein (DegP) and is thought to be involved in apoptosis and stress-induced degradation of misfolded proteins (1). While HtrA2 was orignally identified to be present in either the nucleus (1) or endoplasmic reticulum (2), subsequent studies have shown that it localizes in mitochondria and is released during apoptosis (3-8). HtrA2 is produced as a 50 kDa zymogen that is cleaved to generate a 36 kDa mature protein that exposes an amino terminal motif (AVPS) resembling that of the IAP inhibitor Smac/Diablo (3-8). Like Smac, interaction between HtrA2 and IAP family members, such as XIAP, antagonizes their inhibition of caspase activity and protection from apoptosis (3-8). Interestingly, HtrA2 knock-out mice did not show signs of reduced apoptosis, but rather had a loss of neurons in the striatum and a Parkinson's-like phenotype, suggesting that HtrA2 might have a neuroprotective function (9-11). This activity is associated with the protease activity of HtrA2 (9). Furthermore, research studies have shown that loss of function mutations in the HtrA2 gene are associated with Parkinson's disease (12).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for immunofluorescence in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated β-Catenin (L54E2) Mouse mAb (IF Preferred) #2677.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

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

Application Methods: Western Blotting

Background: The sequence-specific transcription factor activator protein 2α (AP-2α) is required for normal growth and morphogenesis during mammalian development (1,2). Decreased or loss of AP-2α expression has been observed in many different types of human cancers including breast cancer (3,4), ovarian cancer (5), melanoma (6) and prostate cancer (7). These findings suggest that AP-2α expression plays a crucial role in tumorigenicity. Studies have also shown that p53 overexpression in human breast carcinoma cells induces the level of AP-2α expression. Furthermore, p53 binds to the cis-element in the AP-2α promoter, suggesting that AP-2α is a target of p53. AP-2α may mediate the effect of p53 to inhibit cell proliferation (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MLANA, also known as MART-1, is a member of a melanocyte lineage-specific family of proteins. It is expressed in melanocytes, retinal pigment epithelium, and melanoma cells. Its function is not entirely understood, but it is believed to be involved in the stability of GPR143, as well as the stability, trafficking, and processing of PMEL; both proteins are involved in the formation of stage II melanosomes (1). In melanosomes, MLANA is specifically located in the trans-Golgi network, however conformational changes to the protein or a sub-population of the protein causes it to localize back to the ER and small endosomal vesicles (2). In the context of melanoma cells, the conformational change is thought to be caused by aberrant exposure of epitopes, which are recognized by cytolytic T-lymphocytes (3). MLANA may be useful as a marker of metastatic melanoma (4). MHC-II restricted phospho-MLANA peptides, which are recognized by CD4 cells, are being investigated as potential candidates for cancer immunotherapy (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Pig

Application Methods: Western Blotting

Background: Axl, Sky, and Mer are three members of a receptor tyrosine kinase (RTK) family that share a conserved intracellular tyrosine kinase domain and an extracellular domain similar to those seen in cell adhesion molecules. These RTKs bind the vitamin K-dependent protein growth-arrest-specific 6 (Gas6), which is structurally related to the protein S anticoagulation factor (1). Upon binding to its receptor, Gas6 activates phosphatidylinositol 3-kinase (PI3K) and its downstream targets Akt and S6K, as well as NF-κB (2,3). A large body of evidence supports a role for Gas6/Axl signaling in cell growth and survival in normal and cancer cells (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: PHD1 (Egln2), PHD-2 (Egln1), and PHD3 (Egln3) are members of the Egln family of proline hydroxylases. They function as oxygen sensors that catalyze the hydroxylation of HIF on prolines 564 and 402, initiating the first step of HIF degradation through the VHL/ubiquitin pathway (1,2). PHD1 is highly expressed in a wide array of tissues whereas PHD2 and PHD3 are expressed mainly in heart and skeletal muscle (1,3). The mRNA levels of PHD are upregulated by HIF through the hypoxia-response element under low oxygen conditions (4-7). These three enzymes also exhibit different peptide specificity target proteins, PHD1 and PHD2 can hydroxylate both proline 402 and proline 564, but PHD3 can only hydroxylate proline 564 (2,8). In addition to HIF, PHD enzymes have also has been shown to catalyze the hydroxylation of RNA polymerase subunits and myogenin (3,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Despite their relatively small size (8-12 kDa) and uncomplicated architecture, S100 proteins regulate a variety of cellular processes such as cell growth and motility, cell cycle progression, transcription, and differentiation. To date, 25 members have been identified, including S100A1-S100A18, trichohyalin, filaggrin, repetin, S100P, and S100Z, making it the largest group in the EF-hand, calcium-binding protein family. Interestingly, 14 S100 genes are clustered on human chromosome 1q21, a region of genomic instability. Research studies have demonstrated that significant correlation exists between aberrant S100 protein expression and cancer progression. S100 proteins primarily mediate immune responses in various tissue types but are also involved in neuronal development (1-4).Each S100 monomer bears two EF-hand motifs and can bind up to two molecules of calcium (or other divalent cation in some instances). Structural evidence shows that S100 proteins form antiparallel homo- or heterodimers that coordinate binding partner proximity in a calcium-dependent (and sometimes calcium-independent) manner. Although structurally and functionally similar, individual members show restricted tissue distribution, are localized in specific cellular compartments, and display unique protein binding partners, which suggests that each plays a specific role in various signaling pathways. In addition to an intracellular role, some S100 proteins have been shown to act as receptors for extracellular ligands or are secreted and exhibit cytokine-like activities (1-4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Various steps in gene expression, such as mRNA processing, surveillance, export, and synthesis are coupled to transcription elongation (1,2). The C-terminal domain (CTD) of the large subunit of RNA polymerase II plays an important role in the integration of these different steps (1,2). IWS1 interacts with Spt6, a CTD-binding transcription elongation factor and H3 chaperone (1,2). IWS1 also recruits another CTD-binding protein, HYPB/Setd2 histone methyltransferase, to the RNA polymerase II complex for elongation-coupled H3K36 trimethylation (2). Thus, IWS1 links Spt6 and HYPB/Setd2 in a large complex and regulates mRNA synthesis and histone methylation at the co-transcriptional level (2).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The receptor-interacting protein (RIP) family of serine-threonine kinases (RIP, RIP2, RIP3, and RIP4) are important regulators of cellular stress that trigger pro-survival and inflammatory responses through the activation of NF-κB, as well as pro-apoptotic pathways (1). In addition to the kinase domain, RIP contains a death domain responsible for interaction with the death domain receptor Fas and recruitment to TNF-R1 through interaction with TRADD (2,3). RIP-deficient cells show a failure in TNF-mediated NF-κB activation, making the cells more sensitive to apoptosis (4,5). RIP also interacts with TNF-receptor-associated factors (TRAFs) and can recruit IKKs to the TNF-R1 signaling complex via interaction with NEMO, leading to IκB phosphorylation and degradation (6,7). Overexpression of RIP induces both NF-κB activation and apoptosis (2,3). Caspase-8-dependent cleavage of the RIP death domain can trigger the apoptotic activity of RIP (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: BAP31 (B-cell receptor-association protein 31) is a transmembrane protein associated with the endplasmic reticulum (ER) and ER-Golgi intermediates and has been implicated in protein trafficking and apoptosis (1,2). During apoptosis Bap31 is cleaved by caspase-8 at two carboxy-terminal sites which can then direct apoptotic signals between the ER and mitochondria (2-4). Association of BAP31 with the anti-apoptotic proteins Bcl-2 or Bcl-xL could function to regulate this ER-mitochondrial pathway (2,5). Several studies have shown that BAP31 can control the trafficking of select proteins between the ER and Golgi apparatus and can affect the transport of proteins to the cell surface (6-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Peroxiredoxin 6 (Prdx6) belongs to an antioxidant enzyme family of non-seleno peroxidases (prdx). It is a unique member of the Prdx family exhibiting both glutathione peroxidase and phospholipase A2 activities (1,2). Prdx6 regulates phospholipid turnover as well as protects cells against oxidative injury. Prdx6 is expressed in all major organs with a particularly high level in lung where it regulates lung surfactant phospholipid synthesis and turnover (3-5). Studies show Prdx6 is aberrantly expressed in various cancers and promotes cancer cell metastasis and invasion (6,7). Elevated expression of Prdx6 and other prdx family members contributes to drug resistance in cancer cells (8,9). Prdx6 is also expressed in neutrophils, where it regulates the function of these cells and activates NADPH oxidase (Nox2) ( 10-12).

$132
100 µl
Rabbit (DA1E) mAb IgG XP® Isotype Control (Biotinylated) antibody was conjugated to biotin under optimal conditions and tested in-house for direct flow cytometry and western blot.
APPLICATIONS

Application Methods: Immunoprecipitation

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.