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Product listing: SATB1 (D41G7) Rabbit mAb, UniProt ID Q01826 #8067 to SET1A (D3V9S) Rabbit mAb, UniProt ID O15047 #61702

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Special AT-rich binding protein 1 (SATB1) functions as both a global chromatin organizer and a gene-specific transcription factor (1). SATB1 cooperates with promyelocytic leukemia protein (PML) to regulate global chromatin architecture by organizing chromatin into distinct loops via periodic anchoring of matrix attachment regions (MARs) in DNA to the nuclear matrix (1-3). In addition, SATB1 recruits multiple chromatin-remodeling proteins that contribute to specific gene activation and repression, including the chromatin remodeling enzymes ACF and ISWI, the histone deacetylase HDAC1, and the histone acetyltransferases PCAF and p300/CBP (4-6). Phosphorylation of SATB1 on Ser185 by protein kinase C regulates its interaction with HDAC1 and PCAF. While unphosphorylated SATB1 binds to PCAF, phosphorylated SATB1 preferentially binds to HDAC1 (6). Acetylation of SATB1 on Lys136 by PCAF impairs its DNA binding activity, thereby removing SATB1 from gene promoters (6). SATB1 is expressed predominantly in thymocytes and is involved in gene regulation during T cell activation (1). SATB1 is also expressed in metastatic breast cancer cells and is a potential prognostic marker and therapeutic target for metastatic breast cancer (7). In a mouse model system, RNAi-mediated knockdown of SATB1 reversed tumorigenesis by inhibiting tumor growth and metastasis, while ectopic expression of SATB1 in non-metastatic breast cancer cells produced invasive tumors.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Special AT-rich binding protein 2 (SATB2) is a close homolog to SATB1 that functions as a transcription factor. It binds to nuclear matrix attachment regions (MARS); regulatory DNA sequences important for chromatin structure. SATB2 was initially identified when bound to the MARS of the immunoglobulin μ gene in pre-B cells, enhancing its expression (1). SATB2 plays a role in osteoblast differentiation by repressing the HoxA2 gene and enhancing the activity of Runx2 and ATF4 (2). SATB2 also plays a role in the developing cerebral cortex by changing chromatin structure surrounding the Ctip2 regulatory regions (3). In erythroid cells, SATB2 activates the γ-globin locus by recruiting PCAF and reordering the chromatin structure (4). Downregulation of SATB2 is linked to colorectal cancer and head and neck squamous carcinomas (5,6).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Special AT-rich binding protein 2 (SATB2) is a close homolog to SATB1 that functions as a transcription factor. It binds to nuclear matrix attachment regions (MARS); regulatory DNA sequences important for chromatin structure. SATB2 was initially identified when bound to the MARS of the immunoglobulin μ gene in pre-B cells, enhancing its expression (1). SATB2 plays a role in osteoblast differentiation by repressing the HoxA2 gene and enhancing the activity of Runx2 and ATF4 (2). SATB2 also plays a role in the developing cerebral cortex by changing chromatin structure surrounding the Ctip2 regulatory regions (3). In erythroid cells, SATB2 activates the γ-globin locus by recruiting PCAF and reordering the chromatin structure (4). Downregulation of SATB2 is linked to colorectal cancer and head and neck squamous carcinomas (5,6).

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

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

Background: Salvador homolog (SAV1), originally named WW45, was first identified as a 45 kDa protein containing a pair of WW domains and a coiled-coil region (1). SAV1 was subsequently shown to function as a scaffold protein, in a protein complex that includes the kinases MST2 and LATS1, and the transcriptional co-activator YAP (2). This protein complex comprises the core components of the Hippo signaling pathway, which regulates important cellular functions, including contact inhibition and apoptosis, that function to regulate tissue growth and organ size (3,4). A genetic screen in Drosophila identified a role for SAV1 in cell cycle regulation and apoptosis (5), while embryonic mice lacking Sav1 displayed hyperplastic growth and epithelial differentiation effects (6). These findings, together with the observation that SAV1 is mutated a number of human cancer cell lines, suggest that SAV1 functions as a tumor suppressor in the Hippo signaling pathway (5, 7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The serum response factor (SRF) is a ubiquitous protein that modulates transcription of genes containing serum response elements (SRE) at their promoters. SRF regulates cellular processes such as cell proliferation and cytoskeletal signaling in conjunction with a variety of cofactors (1-3).Suppressor of cancer cell invasion (SCAI) is a highly conserved transcriptional cofactor that inhibits the activity of myocardin-related transcription factor (MRTF) family members MAL (MRTF-A), myocardin and OTT-MAL (4,5). SCAI controls the expression of integrin β1 and regulates cell migration and invasion in vitro (4). SCAI has also been shown to play a role in transcriptional regulation in neurons by regulating dendritic morphology through inhibition of the megakaryoblastic leukemia (MKL) family of transcription cofactors (6). Research studies have implicated SCAI in the regulation of the epithelial-to-mesenchymal transition (EMT) as well as in renal fibrosis (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Stearoyl-CoA desaturase 1 (SCD1) is a key lipogenic enzyme found in the endoplasmic reticulum that catalyzes the conversion of palmitoyl–CoA and stearoyl–CoA to palmitoleoyl–CoA (16:1) and oleoyl–CoA (18:1) (1-3). Palmitoleate and oleate are the major components of triglycerides, membrane phospholipids and cholesterol esters (1). SCD1-knockout mice show improved insulin sensitivity and reduced body fat (1). Disruption of SCD1 in mouse brown adipose tissue strengthens insulin signaling and results in increased translocation of Glut4 to plasma membrane and enhanced uptake of glucose (4). Furthermore, SCD1 is essential for the onset of diet-induced body weight gain (1) and insulin resistance in the liver (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Stem cell factor (SCF) is a growth factor that is essential for hematopoiesis, melanogenesis and fertility. SCF is also known as mast cell growth factor (MCGF), steel factor (SLF), or kit ligand (KL) (1-3). SCF mediates its biological effects by binding to and activating c-Kit (4). SCF induces dimerization of c-Kit followed by trans-autophosphorylation of the cytoplasmic protein tyrosine kinase domain, leading to subsequent recruitment of signaling proteins, tyrosine phosphorylation of substrates and activation of multiple signaling pathways (5,6). SCF/c-Kit may take part in the growth control of human malignancies (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The stromal cell derived factor 1 (SDF1/CXCL12) is a small, pro-inflammatory chemoattractant cytokine that regulates leukocyte trafficking through interactions with its cognate 7-transmembrane G protein-coupled receptors (1). The SDF1/CXCL12 receptor, CXCR4, also serves as a coreceptor for the entry of human immunodeficiency virus into target cells (2). SDF1/CXCL12 may regulate homing and maintenance of CXCR4-expressing stem or progenitor cells, including embryonic and many somatic stem cells (3,4). Many cancer cells express CXCR4, suggesting that SDF1/CXCL12 plays a role in cancer metastasis (5,6). Alternative splicing and differential processing during maturation produce a pair of SDF1/CXCL12 isoforms (SDF1/CXCL12α and SDF1/CXCL12β) that have different properties and biological activities (7). Additional isoforms of SDF1/CXCL12 have been reported (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin)

Background: The stromal cell derived factor 1 (SDF1/CXCL12) is a small, pro-inflammatory chemoattractant cytokine that regulates leukocyte trafficking through interactions with its cognate 7-transmembrane G protein-coupled receptors (1). The SDF1/CXCL12 receptor, CXCR4, also serves as a coreceptor for the entry of human immunodeficiency virus into target cells (2). SDF1/CXCL12 may regulate homing and maintenance of CXCR4-expressing stem or progenitor cells, including embryonic and many somatic stem cells (3,4). Many cancer cells express CXCR4, suggesting that SDF1/CXCL12 plays a role in cancer metastasis (5,6). Alternative splicing and differential processing during maturation produce a pair of SDF1/CXCL12 isoforms (SDF1/CXCL12α and SDF1/CXCL12β) that have different properties and biological activities (7). Additional isoforms of SDF1/CXCL12 have been reported (8,9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Succinate dehydrogenase subunit 5 (SDH5, SDHAF2) is a subunit of the succinate dehydrogenase (SDH) protein complex responsible for the oxidation of succinate during the citric acid cycle. Mitochondrial SDH5 associates with the catalytic subunit of succinate dehydrogenase and is required for adding FAD cofactor to the SDH catalytic subunit (1). Mutations in the corresponding SDHAF2 gene are associated with hereditary head and neck paragangliomas, an autosomal disorder characterized by the development of tumors with increased penetrance over time (1). Additional research studies show that SDH5 is involved in the regulation of lung cancer metastasis mediated by the glycogen synthase kinase 3β and β-catenin signaling pathways (2).

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

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

Background: Succinate dehydrogenase (SDH), also known as Complex II or succinate:quinone oxidoreductase, is a key component of the citric acid cycle and the electron transport chain (1). Specifically, it is involved in the oxidation of succinate (2). SDH consists of four subunits: SDHA, SDHB, SDHC, and SDHD (3). Research studies have shown that defects in SDHA cause complex II deficiency (2). In addition, investigators have observed reduction of SDHA in the striatum of patients with Huntington’s disease (3), and reduction of SDHB, SDHC, and SDHD in paragangliomas and phenochromocytomas (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Coat Protein Complex II (COPII) is composed of five cytosolic proteins: Sec23/24 complex, Sec13/31 complex, and Sar1. COPII coat is located at the ER/Golgi interface and is involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (1). COPII formation is initiated through the binding of the activated G protein, Sar1, to the Sec23/24 complex, thereby forming a prebudding complex that directly binds target molecules (1-3). The prebudding complex further recruits Sec13/31 to form mature COPII coat (4,5). The Sec24 subunit of COPII coat is thought to play a critical role in cargo selection (2,6). It binds directly to cargo proteins at the ER and brings them to COPII vesicles through interaction with Sec23. There are four Sec24 isoforms in human cells: Sec24A, Sec24B, Sec24C, and Sec24D (7). In mice, mutations in Sec24B have been linked to developmental defects (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Coat Protein Complex II (COPII) is composed of five cytosolic proteins: Sec23/24 complex, Sec13/31 complex, and Sar1. COPII coat is located at the ER/Golgi interface and is involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (1). COPII formation is initiated through the binding of the activated G protein, Sar1, to the Sec23/24 complex, thereby forming a prebudding complex that directly binds target molecules (1-3). The prebudding complex further recruits Sec13/31 to form mature COPII coat (4,5). The Sec24 subunit of COPII coat is thought to play a critical role in cargo selection (2,6). It binds directly to cargo proteins at the ER and brings them to COPII vesicles through interaction with Sec23. There are four Sec24 isoforms in human cells: Sec24A, Sec24B, Sec24C, and Sec24D (7). In mice, mutations in Sec24B have been linked to developmental defects (8,9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Coat Protein Complex II (COPII) is composed of five cytosolic proteins: Sec23/24 complex, Sec13/31 complex, and Sar1. COPII coat is located at the ER/Golgi interface and is involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (1). COPII formation is initiated through the binding of the activated G protein, Sar1, to the Sec23/24 complex, thereby forming a prebudding complex that directly binds target molecules (1-3). The prebudding complex further recruits Sec13/31 to form mature COPII coat (4,5). The Sec24 subunit of COPII coat is thought to play a critical role in cargo selection (2,6). It binds directly to cargo proteins at the ER and brings them to COPII vesicles through interaction with Sec23. There are four Sec24 isoforms in human cells: Sec24A, Sec24B, Sec24C, and Sec24D (7). In mice, mutations in Sec24B have been linked to developmental defects (8,9).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The coat protein complex II (COPII) is composed of five cytosolic proteins and includes the Sec23/24 complex, the Sec13/31 complex, and Sar1. The COPII coat is located at the ER/Golgi interface and is involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (1). COPII formation is initiated through the binding of the activated G protein, Sar1, to the Sec23/24 complex to form a pre-budding complex that directly binds target molecules (1-3). This pre-budding complex further recruits Sec13/31 to form mature COPII coat (4,5). The Sec31 subunit of COPII coat interacts with Sec13 at the ER exit and is required for both vesicle formation and ER-Golgi transport. Two isoforms of human Sec31 have been identified, Sec31A and Sec31B, which share a sequence homology of 47.3% (6-8). Sec31A is ubiquitously expressed in tissues and organs, whereas Sec31B is enriched in brain and testis (7,8). In classical Hodgkin lymphoma, a novel fusion of Jak2 with Sec31A renders Jak2 constitutively active and subject to Jak2 inhibitor effects (9).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The coat protein complex II (COPII) is composed of five cytosolic proteins and includes the Sec23/24 complex, the Sec13/31 complex, and Sar1. The COPII coat is located at the ER/Golgi interface and is involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (1). COPII formation is initiated through the binding of the activated G protein, Sar1, to the Sec23/24 complex to form a pre-budding complex that directly binds target molecules (1-3). This pre-budding complex further recruits Sec13/31 to form mature COPII coat (4,5). The Sec31 subunit of COPII coat interacts with Sec13 at the ER exit and is required for both vesicle formation and ER-Golgi transport. Two isoforms of human Sec31 have been identified, Sec31A and Sec31B, which share a sequence homology of 47.3% (6-8). Sec31A is ubiquitously expressed in tissues and organs, whereas Sec31B is enriched in brain and testis (7,8). In classical Hodgkin lymphoma, a novel fusion of Jak2 with Sec31A renders Jak2 constitutively active and subject to Jak2 inhibitor effects (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Sec61 translocon is a channel complex located on the endoplasmic reticulum (ER) membrane to mediate membrane protein insertion into the organelle (1). There are three components in the complex, Sec61A, Sec61B, and Sec61G (2). Sec61A is the main component of the channel on the ER membrane and directly contacts nascent synthesized polypeptide TMD (transmembrane domain) for insertion (3). Sec61G functions in stablizing the channel (3). In addition to TMD insertion, Sec61 translocon has also been shown to be involved in ER calcium leakage (4,5). Both Bip and calmodulin can inhibit this leakage by their interaction with Sec61A (6,7). Sec61B has no obvious function related to target protein ER membrane insertion, but is involved in other vesicle trafficking processes such as EGFR and Her2 trafficking from the cytosol to nucleus (8,9), Gurken trafficking from Golgi to plasma membrane (10), and copper-transporting ATPase membrane distribution (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Sec61 translocon is a channel complex located on the endoplasmic reticulum (ER) membrane to mediate membrane protein insertion into the organelle (1). There are three components in the complex, Sec61A, Sec61B, and Sec61G (2). Sec61A is the main component of the channel on the ER membrane and directly contacts nascent synthesized polypeptide TMD (transmembrane domain) for insertion (3). Sec61G functions in stablizing the channel (3). In addition to TMD insertion, Sec61 translocon has also been shown to be involved in ER calcium leakage (4,5). Both Bip and calmodulin can inhibit this leakage by their interaction with Sec61A (6,7). Sec61B has no obvious function related to target protein ER membrane insertion, but is involved in other vesicle trafficking processes such as EGFR and Her2 trafficking from the cytosol to nucleus (8,9), Gurken trafficking from Golgi to plasma membrane (10), and copper-transporting ATPase membrane distribution (11).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Sec61 translocon is a channel complex located on the endoplasmic reticulum (ER) membrane to mediate membrane protein insertion into the organelle (1). There are three components in the complex, Sec61A, Sec61B, and Sec61G (2). Sec61A is the main component of the channel on the ER membrane and directly contacts nascent synthesized polypeptide TMD (transmembrane domain) for insertion (3). Sec61G functions in stablizing the channel (3). In addition to TMD insertion, Sec61 translocon has also been shown to be involved in ER calcium leakage (4,5). Both Bip and calmodulin can inhibit this leakage by their interaction with Sec61A (6,7). Sec61B has no obvious function related to target protein ER membrane insertion, but is involved in other vesicle trafficking processes such as EGFR and Her2 trafficking from the cytosol to nucleus (8,9), Gurken trafficking from Golgi to plasma membrane (10), and copper-transporting ATPase membrane distribution (11).

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

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

Background: Calcium-binding proteins of different subfamilies regulate the second messenger calcium. Calbindin, calmodulin, S-100, parvalbumin and troponin C are members of the low molecular weight calcium-binding protein family (1). Calbindin is expressed in discrete neuronal populations within the CNS and is thought to act as an intracellular calcium buffering protein. Most Purkinje cells express calbindin, which is expressed when neurons start to migrate and differentiate. In contrast, other calcium buffering proteins, such as parvalbumin, are expressed later during development and in parallel with increasing neuronal activity (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Securin is a regulatory protein that contributes to mitotic checkpoint control, p53 activity, DNA repair, and cell migration. The securin protein prevents premature separation of sister chromatids by inhibiting the protease separase, which cleaves the cohesin complex at the onset of anaphase to allow for sister chromatid segregation (1,2). In mouse oocytes, securin regulates cyclin B stability and G2/M transition (3). Securin negatively affects the transcriptional activity of p53, preventing p53-regulated apoptosis (4). Research studies indicate that securin plays a role in microtubule nucleation, cell polarization, and cell migration (5). Additional research indicates that securin expression may be useful as a biomarker for human breast cancer (6-8). The pituitary tumor-transforming gene 1 (PTTG1) encodes for securin protein, while the highly homologous securin 2 protein is transcribed from the related PTTG2 gene. Securin 2 (PTTG2) protein lacks the ability to inhibit separase activity and may function primarily in cell adhesion and migration (9,10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: SAPK/Erk kinase (SEK1), also known as MKK4 or Jun kinase kinase (JNKK), activates the MAP kinase homologues SAPK and JNK in response to various cellular stresses and inflammatory cytokines (1-3). Activation of SEK1 occurs through MEKK phosphorylation of serine and threonine residues at positions 257 and 261, respectively. Like MEK, SEK is a dual-specificity protein kinase that phosphorylates SAPK/JNK at a conserved T*PY* site in its activation loop (4). Phosphorylation by Akt at Ser80 inhibits SEK1 and suppresses stress-activated signal transduction (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Semaphorins are a family of cell surface and secreted proteins initially recognized as axon guidance factors that control the development of the central nervous system (1). They are involved in cell migration, angiogenesis, and immune responses (2-6). Based on protein structure, there are eight classes of semaphorins. Class 3-7 semaphorins are expressed in vertebrates. Semaphorin 3 subfamily members are the only secreted semaphorins in vertebrates. There are seven semaphorin 3 proteins and their receptors include neuropilins and the type A/D family plexins (7-9).Semaphorin 3B functions as a tumor suppressor, as research studies have shown that it is deleted or inactivated in lung and breast cancer (10,11). Overexpression of semaphorin 3B inhibits tumor cell proliferation and causes apoptosis (12,13). Semaphorin 3B also inhibits angiogenesis (14). Semaphorin 3B loses its activity upon cleavage by furin-like pro-protein convertases (14).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Semaphorin-4D/CD100 (Sema4D) is a disulfide-linked homodimeric type 1 transmembrane glycoprotein belonging to the class IV family of membrane bound semaphorins. The extracellular domain of Sema4D contains a cysteine-rich semaphorin-like domain, an Ig-like domain, and a PSI domain (1). Research studies have suggested that the cytoplasmic domain has a signaling function as it is phosphorylated on serine residues (2). Initial studies involving Sema4D revealed that it was implicated in axon guidance within the central nervous system through binding its high affinity receptor, plexin-B1 (3). Sema4D function has also been extensively characterized in the immune system and is the first semaphorin found to be expressed on the surface of many types of immune cells (4-6). In the immune system, CD72 serves as a low-affinity receptor for Sema4D (7) and research studies have shown that Sema4D not only regulates T-cell activation (8,9) but is also involved in the regulation of B-cell survival and differentiation (10). Many of the physiologic effects of Sema4D in the immune system are regulated by a soluble extracellular domain-containing fragment generated through proteolytic cleavage (11).Sema4D has also been implicated in oncogenesis as research studies have demonstrated overexpression in multiple types of solid tumors (12,13). The role of Sema4D in oncogenesis, in part, has been linked to its ability to promote tumor angiogenesis (14), cell invasion (15), and immunosuppression through enhancement of myeloid derived suppressor cell function (16).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Semaphorin-4D/CD100 (Sema4D) is a disulfide-linked homodimeric type 1 transmembrane glycoprotein belonging to the class IV family of membrane bound semaphorins. The extracellular domain of Sema4D contains a cysteine-rich semaphorin-like domain, an Ig-like domain, and a PSI domain (1). Research studies have suggested that the cytoplasmic domain has a signaling function as it is phosphorylated on serine residues (2). Initial studies involving Sema4D revealed that it was implicated in axon guidance within the central nervous system through binding its high affinity receptor, plexin-B1 (3). Sema4D function has also been extensively characterized in the immune system and is the first semaphorin found to be expressed on the surface of many types of immune cells (4-6). In the immune system, CD72 serves as a low-affinity receptor for Sema4D (7) and research studies have shown that Sema4D not only regulates T-cell activation (8,9) but is also involved in the regulation of B-cell survival and differentiation (10). Many of the physiologic effects of Sema4D in the immune system are regulated by a soluble extracellular domain-containing fragment generated through proteolytic cleavage (11).Sema4D has also been implicated in oncogenesis as research studies have demonstrated overexpression in multiple types of solid tumors (12,13). The role of Sema4D in oncogenesis, in part, has been linked to its ability to promote tumor angiogenesis (14), cell invasion (15), and immunosuppression through enhancement of myeloid derived suppressor cell function (16).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: SENP1 is a member of the sentrin/SUMO-specific protease (SENP) family. SENP1 localizes to the nucleoplasm and catalyzes the release of SUMO1, SUMO2, and SUMO3 monomers from sumoylated substrates (1,2). SENP1 has been reported to be responsible for intracellular SUMO homeostasis in the control of normal cellular function (2). The removal of sumoylation by SENP1 from many important target proteins, such as HDAC1, HIF-1α, Stat5, p300, Elk-1, and SirT1, leads to the regulation of the related biological pathways (3-8). SENP1-induced desumoylation of HIF-1α stabilizes the target during hypoxia (5), activating downstream VEGF expression and angiogenesis (9). SENP1 desumoylates Stat5 and contributes to Stat5 acetylation and subsequent signaling during normal lymphocyte development (6). Under stress conditions, SENP1 interacts with and inactivates SirT1 by desumoylation, protecting cells from apoptosis (8). SENP1 has been reported to target the progesterone and androgen receptors, either directly or indirectly through HDAC1, thereby upregulating their transcriptional function and potentially affecting receptor-related cancer progression (3,10-13).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: SENP3 is a member of the SENP (sentrin/SUMO-specific protease) family. The SUMO protease localizes to the nucleolus and catalyzes the release of SUMO2 and SUMO3 monomers from sumoylated substrates (1,2). SENP3 has been reported responsible for the removal of SUMO2/3 from many important target proteins, and regulates their function and stability. Desumoylation of MEF2D (removal of SUMO2/3) leads to an increase of MEF2D transcriptional activation (3). SENP3 enhances the binding of HIF-1α to p300 by deconjugation of SUMO2/3 from p300, leading to the upregulation of HIF-1α transcriptional activity and angiogenesis (4). SENP3 localizes to nucleolus through its binding to the nucleolar protein nucleophosmin (NPM1) (5), and its deconjugation activity towards NPM1 is required for rRNA processing during ribosomal biogenesis (6). Under mild oxidative stress, SENP3 colocalizes with PML, and desumoylates and inhibits the function of PML to promote cell proliferation (7). SENP3 levels are tightly controlled in cells; NPM1, Arf, CHIP, and HSP90 have been shown to regulate the stability of SENP3, either by direct or indirect interaction (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Serine racemase, also called SRR, is an enzyme that is highly expressed in the brain and converts L-serine to D-serine (1,2). D-serine is a co-agonist of the NMDA receptor. NMDA receptor activation requires the binding of glutamate to its GluN2 subunit and the concomitant binding of either glycine or D-serine to its glycine binding site on the GluN1 subunit (3). Decreased activation of NMDA receptors is a typical feature of impaired synaptic plasticity in age-related memory deficits. Therefore, D-serine availability makes serine racemase an important therapeutic target for memory deficit associated with nonpathological aging (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The Sestrin family of proteins, which comprises sestrin-1 (PA26), sestrin-2 (Hi95), and sestrin-3, plays an important role in regulating the cellular response to oxidative stress. Sestrin-1 and -2, both transcriptional targets of p53, have been shown to activate AMPK activity toward TSC2, ultimately resulting in the inhibition of mTOR (1). Thus, sestrin-1 and -2 link p53 signaling to the regulation of cellular growth (2). Sestrins have also been shown to function as modulators of cellular hydrogen peroxide concentration. Hydrogen peroxide is an important signaling molecule that is highly genotoxic and must therefore be tightly regulated (3). 2-Cys peroxiredoxins are metabolizing enzymes that maintain low cellular concentrations of hydrogen peroxide, but are hyperoxidized to an inactive state by a rapid increase in concentration (4) before quickly being reduced back to their active state by sestrins (5). This allows a hydrogen peroxide signal to temporarily circumvent the protective activity of 2-Cys peroxiredoxins, while minimizing oxidative damage.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Chromatin IP-seq, Immunoprecipitation, Western Blotting

Background: The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 at Lys4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, six Set1-related proteins exist in mammals: SET1A, SET1B, MLL1, MLL2, MLL3, and MLL4, all of which assemble into COMPASS-like complexes and methylate histone H3 at Lys4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common subunits WDR5, RBBP5, ASH2L, CXXC1 and DPY30. These subunits are required for proper complex assembly and modulation of histone methyltransferase activity (2-6). MLL1 and MLL2 complexes contain the additional protein subunit, menin (6). Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 at Lys4 (2-6). MLL translocations are found in a large number of hematological malignancies, suggesting that Set1/COMPASS histone methyltransferase complexes play a critical role in leukemogenesis (6).