Microsize antibodies for $99 | Learn More >>

Product listing: Aurora A (D3E4Q) Rabbit mAb (PE Conjugate), UniProt ID O14965 #50235 to Basic FGF (19A9) Rabbit mAb, UniProt ID P09038 #3196

$305
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. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Aurora A (D3E4Q) Rabbit mAb #14475.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Aurora A (AIK) is a cell cycle-regulated Ser/Thr protein kinase that is overexpressed in many tumor cell lines (1-3). Phosphorylation of Aurora A at Thr288 within the kinase activation loop results in a significant increase in its activity and may target the protein for proteasomal degradation during mitosis (4). The closely-related kinase Aurora B (AIM1) has been implicated in multiple mitotic events (5), and siRNA silencing of Aurora B expression results in reduced histone H3 phosphorylation, aberrant chromosome alignment/segregation, and altered survivin localization (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Aurora A (AIK) is a cell cycle-regulated Ser/Thr protein kinase that is overexpressed in many tumor cell lines (1-3). Phosphorylation of Aurora A at Thr288 within the kinase activation loop results in a significant increase in its activity and may target the protein for proteasomal degradation during mitosis (4). The closely-related kinase Aurora B (AIM1) has been implicated in multiple mitotic events (5), and siRNA silencing of Aurora B expression results in reduced histone H3 phosphorylation, aberrant chromosome alignment/segregation, and altered survivin localization (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Aurora kinases belong to a highly conserved family of mitotic serine/threonine kinases with three members identified among mammals: Aurora A, B, and C (1,2). Studies on the temporal expression pattern and subcellular localization of Aurora kinases in mitotic cells suggest an association with mitotic structure. Aurora kinase functional influences span from G2 phase to cytokinesis and may be involved in key cell cycle events such as centrosome duplication, chromosome bi-orientation and segregation, cleavage furrow positioning, and ingression (3). Aurora A is detected at the centrosomes, along mitotic spindle microtubules, and in the cytoplasm of mitotically proliferating cells. Aurora A protein levels are low during G1 and S phases and peak during the G2/M phase of the cell cycle. Phosphorylation of Aurora A at Thr288 in its catalytic domain increases kinase activity. Aurora A is involved in centrosome separation, maturation, and spindle assembly and stability. Expression of Aurora B protein also peaks during the G2/M phase of the cell cycle; Aurora B kinase activity peaks at the transition from metaphase to the end of mitosis. Aurora B associates with chromosomes during prophase prior to relocalizing to the spindle at anaphase. Aurora B regulates chromosome segregation through the control of microtubule-kinetochore attachment and cytokinesis. Expression of both Aurora A and Aurora B during the G2/M phase transition is tightly coordinated with histone H3 phosphorylation (4,5); research investigators have observed overexpression of these kinases in a variety of human cancers (2,4). Aurora C localizes to the centrosome from anaphase to cytokinesis and both mRNA and protein levels peak during G2/M phase. Although typical Aurora C expression is limited to the testis, research studies report overexpression of Aurora C is detected in various cancer cell lines (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Aurora A (AIK) is a cell cycle-regulated Ser/Thr protein kinase that is overexpressed in many tumor cell lines (1-3). Phosphorylation of Aurora A at Thr288 within the kinase activation loop results in a significant increase in its activity and may target the protein for proteasomal degradation during mitosis (4). The closely-related kinase Aurora B (AIM1) has been implicated in multiple mitotic events (5), and siRNA silencing of Aurora B expression results in reduced histone H3 phosphorylation, aberrant chromosome alignment/segregation, and altered survivin localization (6).

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

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

Background: Axin1 (Axis inhibition protein 1) and Axin2 are multidomain scaffold proteins that negatively regulate Wnt signaling. Axin1 interacts with APC, GSK-3β, Dvl, and β-catenin and promotes the GSK-3β-mediated phosphorylation and subsequent degradation of β-catenin (1,2). Upon stimulation of cells with Wnt, Axin1 is recruited to the membrane by phosphorylated LRP5/6, a process that is believed to be crucial for activation of Wnt signaling (3,4). In addition to its role in the Wnt signaling pathway, Axin1 forms a complex with MEKK1 and activates c-Jun amino-terminal kinase (JNK/SAPK) (5). Axin2 (also known as Conductin or Axil) can functionally substitute for Axin1 in mice (6). Axin2 itself is a direct target of the Wnt signaling pathway and therefore serves to control the duration and/or intensity of Wnt signaling through a negative feedback loop (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Axin1 (Axis inhibition protein 1) and Axin2 are multidomain scaffold proteins that negatively regulate Wnt signaling. Axin1 interacts with APC, GSK-3β, Dvl, and β-catenin and promotes the GSK-3β-mediated phosphorylation and subsequent degradation of β-catenin (1,2). Upon stimulation of cells with Wnt, Axin1 is recruited to the membrane by phosphorylated LRP5/6, a process that is believed to be crucial for activation of Wnt signaling (3,4). In addition to its role in the Wnt signaling pathway, Axin1 forms a complex with MEKK1 and activates c-Jun amino-terminal kinase (JNK/SAPK) (5). Axin2 (also known as Conductin or Axil) can functionally substitute for Axin1 in mice (6). Axin2 itself is a direct target of the Wnt signaling pathway and therefore serves to control the duration and/or intensity of Wnt signaling through a negative feedback loop (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Axin1 (Axis inhibition protein 1) and Axin2 are multidomain scaffold proteins that negatively regulate Wnt signaling. Axin1 interacts with APC, GSK-3β, Dvl, and β-catenin and promotes the GSK-3β-mediated phosphorylation and subsequent degradation of β-catenin (1,2). Upon stimulation of cells with Wnt, Axin1 is recruited to the membrane by phosphorylated LRP5/6, a process that is believed to be crucial for activation of Wnt signaling (3,4). In addition to its role in the Wnt signaling pathway, Axin1 forms a complex with MEKK1 and activates c-Jun amino-terminal kinase (JNK/SAPK) (5). Axin2 (also known as Conductin or Axil) can functionally substitute for Axin1 in mice (6). Axin2 itself is a direct target of the Wnt signaling pathway and therefore serves to control the duration and/or intensity of Wnt signaling through a negative feedback loop (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Axin1 (Axis inhibition protein 1) and Axin2 are multidomain scaffold proteins that negatively regulate Wnt signaling. Axin1 interacts with APC, GSK-3β, Dvl, and β-catenin and promotes the GSK-3β-mediated phosphorylation and subsequent degradation of β-catenin (1,2). Upon stimulation of cells with Wnt, Axin1 is recruited to the membrane by phosphorylated LRP5/6, a process that is believed to be crucial for activation of Wnt signaling (3,4). In addition to its role in the Wnt signaling pathway, Axin1 forms a complex with MEKK1 and activates c-Jun amino-terminal kinase (JNK/SAPK) (5). Axin2 (also known as Conductin or Axil) can functionally substitute for Axin1 in mice (6). Axin2 itself is a direct target of the Wnt signaling pathway and therefore serves to control the duration and/or intensity of Wnt signaling through a negative feedback loop (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Axin1 (Axis inhibition protein 1) and Axin2 are multidomain scaffold proteins that negatively regulate Wnt signaling. Axin1 interacts with APC, GSK-3β, Dvl, and β-catenin and promotes the GSK-3β-mediated phosphorylation and subsequent degradation of β-catenin (1,2). Upon stimulation of cells with Wnt, Axin1 is recruited to the membrane by phosphorylated LRP5/6, a process that is believed to be crucial for activation of Wnt signaling (3,4). In addition to its role in the Wnt signaling pathway, Axin1 forms a complex with MEKK1 and activates c-Jun amino-terminal kinase (JNK/SAPK) (5). Axin2 (also known as Conductin or Axil) can functionally substitute for Axin1 in mice (6). Axin2 itself is a direct target of the Wnt signaling pathway and therefore serves to control the duration and/or intensity of Wnt signaling through a negative feedback loop (7-9).

$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, Monkey

Application Methods: Flow Cytometry, Immunoprecipitation, 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).

$305
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. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Axl (C89E7) Rabbit mAb #8661.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

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, Monkey

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

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

Application Methods: Western Blotting

Background: A-Raf, B-Raf, and c-Raf (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway (1). Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites including Ser338, Tyr341, Thr491, Ser494, Ser497, and Ser499 (2). p21-activated protein kinase (PAK) has been shown to phosphorylate c-Raf at Ser338, and the Src family phosphorylates Tyr341 to induce c-Raf activity (3,4). Ser338 of c-Raf corresponds to similar sites in A-Raf (Ser299) and B-Raf (Ser445), although this site is constitutively phosphorylated in B-Raf (5). Inhibitory 14-3-3 binding sites on c-Raf (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6,7). While A-Raf, B-Raf, and c-Raf are similar in sequence and function, differential regulation has been observed (8). Of particular interest, B-Raf contains three consensus Akt phosphorylation sites (Ser364, Ser428, and Thr439) and lacks a site equivalent to Tyr341 of c-Raf (8,9). Research studies have shown that the B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301, and Ser642) become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to subsequent activation events (11).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: A-Raf, B-Raf, and c-Raf (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway (1). Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites including Ser338, Tyr341, Thr491, Ser494, Ser497, and Ser499 (2). p21-activated protein kinase (PAK) has been shown to phosphorylate c-Raf at Ser338, and the Src family phosphorylates Tyr341 to induce c-Raf activity (3,4). Ser338 of c-Raf corresponds to similar sites in A-Raf (Ser299) and B-Raf (Ser445), although this site is constitutively phosphorylated in B-Raf (5). Inhibitory 14-3-3 binding sites on c-Raf (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6,7). While A-Raf, B-Raf, and c-Raf are similar in sequence and function, differential regulation has been observed (8). Of particular interest, B-Raf contains three consensus Akt phosphorylation sites (Ser364, Ser428, and Thr439) and lacks a site equivalent to Tyr341 of c-Raf (8,9). Research studies have shown that the B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301, and Ser642) become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to subsequent activation events (11).

$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 B-Raf (D9T6S) Rabbit mAb #14814.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: A-Raf, B-Raf, and c-Raf (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway (1). Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites including Ser338, Tyr341, Thr491, Ser494, Ser497, and Ser499 (2). p21-activated protein kinase (PAK) has been shown to phosphorylate c-Raf at Ser338, and the Src family phosphorylates Tyr341 to induce c-Raf activity (3,4). Ser338 of c-Raf corresponds to similar sites in A-Raf (Ser299) and B-Raf (Ser445), although this site is constitutively phosphorylated in B-Raf (5). Inhibitory 14-3-3 binding sites on c-Raf (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6,7). While A-Raf, B-Raf, and c-Raf are similar in sequence and function, differential regulation has been observed (8). Of particular interest, B-Raf contains three consensus Akt phosphorylation sites (Ser364, Ser428, and Thr439) and lacks a site equivalent to Tyr341 of c-Raf (8,9). Research studies have shown that the B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301, and Ser642) become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to subsequent activation events (11).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: B7 homolog 3 (B7-H3, CD276) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses. B7-H3 protein contains two extracellular Ig-like V-type domains and two IgG-like C2-type domains, a transmembrane domain, and a short intracellular domain (1,2). Early research examining the biological process of B7-H3 suggested that B7-H3 is a positive regulator of T cell response (1). Subsequent research studies indicated that B7-H3 is a negative regulator of T cell response, and that the protein inhibits T cell proliferation (2,3). One possibility is that B7-H3 interacts with two distinct sets of receptors, resulting in seemingly opposite biological outcomes (2). B7-H3 is expressed by antigen presenting cells, activated T cells, and a few normal tissues, including placenta and prostate (1,4,5). Expression of B7-H3 is seen in several cancer types, including prostate, breast, colon, lung, and gastric cancers, and in endothelial cells from tumor associated vasculature (6-8).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: B7 homolog 4 (B7-H4, VTCN1) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses (1-3). B7-H4 protein contains two extracellular Ig-like V-type domains, a transmembrane domain, and a short, two amino acid intracellular domain (3). The B7-H4 protein is shown to inhibit T cell activation, proliferation, and cytokine production (1,4,5). Although B7-H4 mRNA is widely expressed, B7-H4 protein is restricted to antigen presenting cells and B cells (1). The B7-H4 protein is also found in several tumor types, including ovarian cancer and breast cancer (6). Research studies indicate that B7-H4 protein is present on the surface of ovarian tumor cells, and that targeted inhibition of B7-H4 using recombinant antibodies restores T cell activation pathways. These studies suggest some potential therapeutic value in blocking B7-H4 function and restoring T cell function in cancer patients (7,8).

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

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

Background: β-secretase (BACE) is an aspartic acid proteinase that catalyses the initial step in APP processing by cleaving and releasing a soluble, extracellular APP-β (sAPPβ) ectodomain and generating a membrane-bound, carboxy-terminal fragment consisting of 99 amino acids (CTF99). Additional processing of CTF99 by γ-secretase generates the amyloid β-peptide (Aβ) that forms aggregates in the brains of Alzheimer disease (AD) patients. BACE is an attractive target for inhibitors in AD therapy since it catalyses the first and rate limiting step in amyloidogenic APP processing (1). Pro-BACE-1 is synthesized in the ER before it is transported to the trans-Golgi network to undergo maturation (2). BACE-1 functions as a dimer and is phosphorylated at Ser498 by casein kinase 1, which is necessary for recycling back to the membrane from the early endosome (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The transcription regulator BTB and CNC homolog 2 (BACH2) is a bZIP domain-containing transcriptional repressor that dimerizes with MafK and binds Maf recognition elements (MAREs) to regulate transcription (1,2). BACH2 is part of a network of transcription factors that controls the transition of activated B cells into either antibody-producing plasma cells or memory B cells (3-5). Plasma cell differentiation requires the transcription factor Blimp1 (6). BACH2 suppresses expression of Blimp1 in activated B cells, which delays plasma cell differentiation and allows time for class switch recombination and somatic hypermutation (3-5). Genome-wide association studies have linked the genetic locus containing BACH2 to several immune-related disorders including type 1 diabetes, celiac disease, Crohn’s disease, and the skin condition known as vitiligo (7-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, 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).

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

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Bag1 belongs to the Bcl-2 associated athanogene (BAG) family of multifunctional proteins and was the first of six related proteins isolated from humans (1,2). This widely expressed protein interacts with a number of signaling molecules (including Bcl2, HGF receptor and Raf1) as it regulates signaling molecules in pathways involving cell survival, growth and differentiation. The most common role played by Bag1 protein is as an inhibitor of proteins favoring apoptosis (2-4). Bag1 also plays a role in Raf1 signaling and binds DNA as a transcription activator (4). Bag1 protein is a well-characterized inhibitor of its binding partner HSP70 (5). A conserved carboxy-terminal BAG domain within Bag1 interacts with the ATPase domain of HSP70 to negatively regulate heat shock protein chaperone activity (6,7). The multiple isoforms of Bag1 protein generated from a single transcript share a common ubiquitin homology domain and a carboxy-terminal Hsp70 binding region but differ in length and cellular localization. The 50 kDa long (Bag1-L) isoform also contains a nuclear localization signal and is often found in the nucleus where it activates transcription. The 46 kDa intermediate (Bag1-M) isoform is found mainly in the cytoplasm but can also translocate to the nucleus when associated with other proteins. The shorter 29-33 kDa isoforms (Bag1-S, Bag-1) isoforms are found primarily in the cytoplasm (8). High expression of the anti-apoptotic Bag1 protein correlates with increased survival in patients with particular forms of cancer, leading researchers to study possible therapeutic roles for Bag1 protein (9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Bak is a proapoptotic member of the Bcl-2 family (1). This protein is located on the outer membrane of mitochondria and is an essential component for transduction of apoptotic signals through the mitochondrial pathway (2,3). Upon apoptotic stimulation, an upstream stimulator like truncated BID (tBID) induces conformational changes in Bak to form oligomer channels in the mitochondrial membrane for cytochrome c release. The release of cytochrome c to the cytosol activates the caspase-9 pathway and eventually leads to cell death (4,5).

$305
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 Bak (D4E4) Rabbit mAb #12105.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: Bak is a proapoptotic member of the Bcl-2 family (1). This protein is located on the outer membrane of mitochondria and is an essential component for transduction of apoptotic signals through the mitochondrial pathway (2,3). Upon apoptotic stimulation, an upstream stimulator like truncated BID (tBID) induces conformational changes in Bak to form oligomer channels in the mitochondrial membrane for cytochrome c release. The release of cytochrome c to the cytosol activates the caspase-9 pathway and eventually leads to cell death (4,5).

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

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

Background: Bak is a proapoptotic member of the Bcl-2 family (1). This protein is located on the outer membrane of mitochondria and is an essential component for transduction of apoptotic signals through the mitochondrial pathway (2,3). Upon apoptotic stimulation, an upstream stimulator like truncated BID (tBID) induces conformational changes in Bak to form oligomer channels in the mitochondrial membrane for cytochrome c release. The release of cytochrome c to the cytosol activates the caspase-9 pathway and eventually leads to cell death (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: BRCA1-Associated Protein 1 (BAP1) was originally identified as a BRCA1 associated, nuclear localized ubiquitin hydrolase that suppresses cell growth (1). The protein belongs to the UCH family of deubiquitinases, with a UCH domain in its amino-terminal segment and a BRCA1 interaction domain as well as a nuclear localization signal in its carboxy-terminal segment (1). Frequent gene locus rearrangement, deletion, and null mutation of BAP1 have been found in lung and breast cancers (1,2). In vivo mutation analysis of cancer cell line survival and animal tumorigenesis indicates that both the deubiquitinase activity and the nuclear localization signal are required for BAP1 function as a tumor suppressor (3). BAP1 does not have direct deubiquitination activity towards the autoubiquitinated BRCA1/BARD1 E3 complex (4), but its interaction with BARD1 inhibits BRCA1/BARD1 E3 activity by interfering with the complex dimerization process (5). In addition to its interaction with BRCA1/BARD1, BAP1 has also been shown to interact with and deubiquitinate HCF-1, thereby controlling its stability (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: BRCA1-Associated Protein 1 (BAP1) was originally identified as a BRCA1 associated, nuclear localized ubiquitin hydrolase that suppresses cell growth (1). The protein belongs to the UCH family of deubiquitinases, with a UCH domain in its amino-terminal segment and a BRCA1 interaction domain as well as a nuclear localization signal in its carboxy-terminal segment (1). Frequent gene locus rearrangement, deletion, and null mutation of BAP1 have been found in lung and breast cancers (1,2). In vivo mutation analysis of cancer cell line survival and animal tumorigenesis indicates that both the deubiquitinase activity and the nuclear localization signal are required for BAP1 function as a tumor suppressor (3). BAP1 does not have direct deubiquitination activity towards the autoubiquitinated BRCA1/BARD1 E3 complex (4), but its interaction with BARD1 inhibits BRCA1/BARD1 E3 activity by interfering with the complex dimerization process (5). In addition to its interaction with BRCA1/BARD1, BAP1 has also been shown to interact with and deubiquitinate HCF-1, thereby controlling its stability (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Fibroblast growth factors are a family of broad-spectrum growth factors influencing a plethora of cellular activities. The interaction of at least 23 ligands, 4 receptors and multiple coreceptors provides a dramatic complexity to a signaling system capable of effecting a multitude of responses (1,2). Basic fibroblast growth factor (bFGF or FGF2), initially identified as a mitogen with prominent angiogenic properties, is now recognized as a multifunctional growth factor (3). It is clear that bFGF produces its biological effects in target cells by signaling through cell-surface FGF receptors. bFGF binds to all four FGF receptors. Ligand binding induces receptor dimerization and autophosphorylation, allowing binding and activation of cytoplasmic downstream target proteins, including FRS-2, PLC and Crk (4,5). The FGF signaling pathway appears to play a significant role not only in normal cell growth regulation but also in tumor development and progression (6).Acidic FGF (aFGF or FGF1) is another extensively investigated protein of the FGF family. aFGF shares 55% DNA sequence homology with bFGF. These two growth factors are ubiquitously expressed and exhibit a wide spectrum of similiar biological activities with quantitative differences likely due to variation in receptor affinity or binding (7).