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Product listing: Stat5b Antibody, UniProt ID P51692 #34662 to LAIR-1 Antibody, UniProt ID Q6GTX8 #87923

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Stat5 is activated in response to a wide variety of ligands including IL-2, GM-CSF, growth hormone and prolactin. Phosphorylation at Tyr694 is obligatory for Stat5 activation (1,2). This phosphorylation is mediated by Src upon erythropoietin stimulation (3). Stat5 is constitutively active in some leukemic cell types (4). Phosphorylated Stat5 is found in some endothelial cells treated with IL-3, which suggests its involvement in angiogenesis and cell motility (5). Stat5a and Stat5b are independently regulated and activated in various cell types. For instance, interferon treatment predominantly activates Stat5a in U-937 cells and Stat5b in HeLa cells (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: Somatostatin receptors are part of the super family of G protein-coupled receptors. Five genes encoding six different somatostatin receptor subtypes (SSTR1, SSTR2A, SSTR2B, SSTR3, SSTR4, and SSTR5) have been cloned (1). Somatostatin receptors are activated by somatostatin, a neuropeptide that acts as a neurotransmitter in the brain that regulates hormone secretion from endocrine tissues (2). Somatostatin receptors are found to be highly expressed on human neuroendocrine tumors (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: SLAMF6 (CD352/NTB-A) is a type-I transmembrane glycoprotein belonging to the signaling lymphocytic activation molecule (SLAM) family of immunomodulatory receptors. Like other members of the SLAM receptor family, SLAMF6 contains Ig-like domains within its extracellular region and conserved tyrosine-based signaling motifs within its intracellular domain that, when phosphorylated, bind to the SAP and EAT-2 signaling adaptors (1). SLAMF6 is expressed on the surface of multiple types of immune cells, such as those of the B, T, and NK lineages. Its activation is triggered by homotypic interactions involving its extracellular domain (1-3). Indeed, research studies have shown that in T-cells, SLAMF6 engagement facilitates activation and cytokine production (4). Similarly, homotypic ligand-mediated engagement of SLAMF6 on NK cells activates signaling cascades that drive proliferation, cytotoxicity, and cytokine production (1,5-7).

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

Application Methods: Western Blotting

Background: p70 S6 kinase is a mitogen activated Ser/Thr protein kinase downstream of phosphoinositide-3 kinase (PI3K) and the target of rapamycin, FRAP/mTOR. p70 S6 kinase is required for cell growth and cell cycle progression (1,2). SKAR is a recently discovered substrate of S6K1. SKAR exists in two isoforms, α and β, the latter having a 29 amino acid truncation. Phosphorylation of SKAR is mitogen-induced and sensitive to rapamycin. Reduction in SKAR protein levels results in decreased cell size, further implicating SKAR in cell growth control (3).

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

Application Methods: Western Blotting

Background: p70 S6 kinase is a mitogen activated Ser/Thr protein kinase downstream of phosphoinositide-3 kinase (PI3K) and the target of rapamycin, FRAP/mTOR. p70 S6 kinase is required for cell growth and cell cycle progression (1,2). SKAR is a recently discovered substrate of S6K1. SKAR exists in two isoforms, α and β, the latter having a 29 amino acid truncation. Phosphorylation of SKAR is mitogen-induced and sensitive to rapamycin. Reduction in SKAR protein levels results in decreased cell size, further implicating SKAR in cell growth control (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: SGTA, small glutamine-rich tetratricopeptide repeat-containing protein A, is an ubiquitously expressed co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity (1,2). SGTA is a 34 kDa protein that is rich in glutamine residues at its C terminus and contains three tandemly repeated TPR motifs (3). The TPR domain of SGTA shows sequence similarity to the TPR domains of Hop, CHIP, and TOM70 (4). The TPR domain of SGTA also interacts with HSP90 and was recently found to be a pro-apoptotic factor (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: 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, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: RBM15 is an RNA binding protein that is part of the WTAP-METTL3 m6A methyltransferase complex. RBM15 and related RBM15B interact with WTAP to recruit the complex to target mRNAs, and are critical to XIST-mediated gene silencing (1). RBM15 can recruit splicing factors such as SF3B1 to mRNA to promote alternative splicing. Expression levels of RBM15 can be regulated by PRMT1, which can methylate R578, resulting in RBM15 ubiquitinylation and degradation (2). This process is critical in acute megakaryoblastic leukemia, a cancer type where RBM15 is fused to the MKL-1 gene and PRMT1 is overexpressed (3). RBM15 normally plays roles in hematopoietic development and myeloid differentiation, where it can regulate the levels of c-Myc (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: RALY is a member of the large family of heterogeneous nuclear ribonucleoproteins (hnRNPs). RALY was initially discovered in lethal yellow mice, a condition where heterozygotes display an all yellow coat, obesity, diabetes, and tumors. In this condition, mRNA to the 5’ untranslated region of RALY fuses to the agouti transcript (1,2). RALY binds to U-rich elements in coding and non-coding mRNAs undergoing translation (3). RALY has been implicated certain cancer types, as it can control transcriptional regulation and splicing of E2F1 and PRMT1 mRNAs (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Mitochondrial pyrroline-5-carboxylate reductase 1 (PYCR1) catalyzes the last step in proline biosynthesis (1). Research studies show that proline is a limiting amino acid to clear cell renal cell carcinoma (ccRCC). PYCR1 expression is induced in kidney cancer cells to compensate for the proline shortage and maintain cancer cell growth. Furthermore, PYCR1 knockdown inhibits ccRCC cell proliferation in the absence of proline, suggesting this enzyme as a potential cancer therapeutic target (2). In addition, breast cancer cells also express high levels of PYCR1 (2,3). Proline is restrictive to invasive ductal breast carcinoma cells, indicating proline vulnerability in the breast cancer formation (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Pitrilysin metalloproteinase 1 (PITRM1 or PreP) is a mitochondria-enriched presequence peptidase that processes the mitochondrial targeting sequence (MTS) of proteins imported across the inner mitochondrial membrane (1). Mitochondria normally function to regulate many cellular processes such as energy production and apoptosis, and its dysfunction may contribute indirectly or directly to human neurodegenerative diseases like Alzheimer’s and Parkinson’s disease (2, 3; AD and PD, respectively). Interestingly, Aβ, the pathological hallmark of AD, accumulates in mitochondria and inhibits Cym1, the PITRM1 yeast ortholog, leading to impaired MTS processing and accumulation of unprocessed mitochondrial proteins, suggesting an indirect role of Aβ and mitochondrial dysfunction via PITRM1 (4). In addition to biochemical association of PITRM1 with Aβ-dependent mitochondrial dysfunction, human genetics suggest a more direct link as PITRM1 genetic variants have been associated with AD (5, 6). The specific mechanism is currently poorly understood, but may involve impairment of PITRM1-dependent degradation of Aβ, directly resulting in pathological accumulation of Aβ in mitochondria (6).

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

Application Methods: Western Blotting

Background: Plant homeodomain-like finger 6 (PHF6) is a 41 kDa transcriptional repressor that was first identified as a mutated gene in Börjeson-Forssman-Lehmann syndrome (BFLS), an X-linked intellectual disability disorder (1,2). Somatic loss-of-function mutations in the PHF6 gene have also been linked to T-cell acute lymphoblastic leukemia (T-ALL) and acute myeloid leukemia (AML) (3-5). Structurally, PHF6 contains two nuclear localization sequences, one nucleolar localization sequence, and two plant homeodomain (PHD)-like zinc fingers (6,7). Unlike other PHD proteins, the PHD domains of PHF6 are considered to be imperfect and have not been shown to directly bind to histones; however, the isolated second PHD domain (PHD2) has been shown to bind dsDNA directly (7). A more recent study finds that PHF6 interacts with histones via protein-protein interactions, and that this association is independent of DNA and enriched in the presence of the activating marks H3K27ac and H3K4me3 (8). PHF6 interacts with PAF1 and other subunits of the PAF1 transcription elongation complex, and knockdown of either PHF6 or PAF1 adversely affects proper neuronal positioning and migration in mouse cerebral cortex (9). PHF6 has also been shown to associate with members of the nucleosome remodeling and deacetylation (NuRD) chromatin remodeling complex, including CHD4, HDAC1, and RBBP4, where it is likely involved in transcriptional repression of developmental genes (10). PHF6 plays a critical role in regulating hematopoiesis, particularly by regulating chromatin accessibility to lineage-specific transcription factors. Studies suggest that PHF6 promotes B-cell lineage differentiation through the expression of B-cell specific genes, while simultaneously suppressing T-cell lineage differentiation (8). Indeed, a CRISPR-Cas9 knockout study shows that PHF6 is required for growth of B-ALL cells, while mice transplanted with PHF6-deficient B-ALL cells develop T-ALL phenotypes (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The tumor suppressor protein p21 Waf1/Cip1 acts as an inhibitor of cell cycle progression. It functions in stoichiometric relationships forming heterotrimeric complexes with cyclins and cyclin-dependent kinases. In association with CDK2 complexes, it serves to inhibit kinase activity and block progression through G1/S (1). However, p21 may also enhance assembly and activity in complexes of CDK4 or CDK6 and cyclin D (2). The carboxy-terminal region of p21 is sufficient to bind and inhibit PCNA, a subunit of DNA polymerase, and may coordinate DNA replication with cell cycle progression (3). Upon UV damage or during cell cycle stages when cdc2/cyclin B or CDK2/cyclin A are active, p53 is phosphorylated and upregulates p21 transcription via a p53-responsive element (4). Protein levels of p21 are downregulated through ubiquitination and proteasomal degradation (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Nuclear Receptor Binding Factor-2 (NRBF-2), also referred to as Comodulator of PPAR and RXRα-2 (COPR-2), has been shown to interact with the AF-2 region of several nuclear hormone receptors with varying affinities such as PPARα, RARα, RARγ, and RXRα (1,2). NRBF-2 contains a LLYLL motif, which matches the LXXLL NR box consensus and is required for functional NRBF-2/nuclear receptor complex formation and repression of receptor function. NRBF-2 also contains a unique autonomous activation domain and, thus, does not completely abrogate nuclear receptor function, suggesting that NRBF-2 might serve as a molecular rheostat to fine-tune the transcriptional activity of liganded nuclear receptors (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Nicotinamide N-methyltransferase (NNMT) is a metabolic enzyme expressed primarily in liver and adipose tissue. It catalyzes the transfer of a methyl group from S-Adenosyl-methionine (SAM) to nicotinamide, yielding 1-methylnicotinamide (MNAM) and S-Adenosyl-L-homocysteine (SAH) (1). This N-methylation enzymatic activity plays an important role in the biotransformation of drugs and xenobiotics, and also contributes to the metabolism of vitamin B3 (2). Knockdown of NNMT was shown to increase both SAM and NAD+ levels in white adipose tissue of high-fat diet-fed mice, resulting in increased energy expenditure and protection against diet-induced obesity (3). In contrast, increased liver NNMT expression in humans and mice correlated with an improved metabolic profile, through MNAM-mediated SIRT1 protein stabilization (4). In cancer cells, overexpression of NNMT resulted in excess consumption of methyl units from SAM, leading to histone hypomethylation that substantially altered the epigenetic landscape (5). These and other research studies have suggested that NNMT expression may have utility as a diagnostic and prognostic biomarker in cancer (6-8).

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

Application Methods: Western Blotting

Background: The NDK/NME/NM23 kinase family (encoded by the NME gene family) consists of at least eight distinct proteins that exhibit different cellular localization (1). Members of this group inhibit metastasis in a variety of tumor cell types (2). All NDK/NME/NM23 proteins possess nucleoside diphosphatase kinase (NDK) activity and catalyze the phosphorylation of nucleoside diphosphate to the corresponding nucleoside triphosphate to regulate a diverse array of cellular events (3). At least four classes of NDK biochemical activities have been described, including protein-protein interactions (4-6), regulation of GTP-binding protein function (7-9), DNA-associated activities (10,11), and histidine-dependent protein phosphotransferase activity (12). NDK/NME proteins participate in the regulation of a broad spectrum of cellular responses, including development, differentiation, proliferation, endocytosis, and apoptosis (13). Because of its role in metastasis suppression and oncogenesis, NDKA (NME1/NM23-H1) has been widely studied (14). NDKA (NM23-H1) and NDKB (NM23-H2) are encoded by adjacent NME1 and NME2 genes and share 90% sequence identity. Two serine residues (Ser122 and Ser144) on NDKA/NM23-H1 can be phosphorylated by AMPKα1, but only phosphorylation at Ser122 determines whether NDKA channels ATP to AMPKα1. This regulates AMPKα1 activity towards ACC1, an important regulator of fatty acid metabolism (15). Mutation of NDKB/NM23-H2 at Ser122 (S122P) in melanoma cells results in altered phosphoryl transfer activity (16).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: NIPA (nuclear interaction partner of ALK) is an F-box-containing protein that is an essential component of the SCF-type E3 ligase (SCFNIPA) complex, a complex that controls the completion of S-phase and mitotic entry (1). This control is mediated by the ubiquitination and subsequent degradation of cell cycle regulatory proteins, whose oscillation of protein levels is required for proper cell cycle progression (2).Expression levels of NIPA are low in G0/G1 phases and upregulated in S and G2/M phases. The SCFNIPA complex targets nuclear cyclin B1 for ubiquitination in interphase, whereas phosphorylation of NIPA in late G2 phase and mitosis inactivates the complex to allow for accumulation of cyclin B1 (3). NIPA may have an anti-apoptotic role in NPM-ALK-mediated signaling events (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Na+/H+ exchanger regulatory factor (NHERF1 or EBP-50) is one of several related PDZ domain-containing proteins (1). NHERF1 was first identified as a necessary cofactor for cyclic AMP-associated inhibition of Na+/ H+ exchanger isoform 3 (NHE3) (2). NHERF1 is a multifunctional adaptor protein that interacts with receptors and ion transporters via its PDZ domains, and with the ERM family of proteins, including merlin, via its carboxy-terminus (2,3). NHERF1 may play an important role in breast cancer. Estrogen has been found to induce NHERF1 in estrogen receptor-positive breast cancer cells (2,3). Furthermore, NHERF1 has been shown to bind to PDGFR, which is activated in breast carcinomas. NHERF1 has been found to promote the formation of a ternary complex containing PTEN, NHERF1, and PDGFR. Therefore, NHERF1 may function to recruit PTEN to PDGFR to inhibit the activation of PI3K/Akt signaling in normal cells; this mechanism may be disrupted in cancer (4). NHERF1 also binds to the cystic fibrosis transmembrane conductance regulator (CFTR), which functions as an ion channel and has disease-causing mutations in cystic fibrosis (5). Other proposed functions of NHERF1 include testicular differentiation, endosomal recycling, membrane targeting, protein sorting, and trafficking (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The chondroitin sulfate proteoglycan NG2 is a type I membrane protein expressed by subpopulations of glia including oligodendroglial precursor cells and a variety of tumor cells. Normal precursor cells and malignant tumor cells migrate and proliferate, but there is evidence that cells may not be able to engage in both activities at the same time. However, NG2 is involved in promoting both proliferation and motility (1). The extracellular domain of NG2 sequesters growth factors and binds to both growth factor receptors and extracellular matrix ligands such as fibronectin, collagens and laminin. The cytoplasmic domain is involved in activating Rac, Cdc42 and p130 Cas (2). PKCα phosphorylates NG2 at Thr2256, triggering the redistribution of NG2 from apical microprocesses to lamellipodia accompanied by enhanced cell motility (3). ERK phosphorylates NG2 at Thr2314, stimulating cell proliferation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Chromatin IP, Western Blotting

Background: MYST3, also known as Monocytic leukemia zinc finger protein (MOZ) and lysine acetyltransferase 6A (KAT6), is a member of the MYST (MOZ, YBF2, SAS2, and TIP60) family of histone acetyltransferases (1,2). First discovered as a fusion partner of CREBBP in acute myeloid leukemia, MYST3 contributes to Hox gene expression and segment identity during development (3-6). MYST3 forms an evolutionarily conserved complex with ING5, EAF6, and BRD1 and has been shown to be a coactivator for many different transcription factors including PU.1, NRF2, and Runx family members (7-9). MYST3 is critical in hematopoietic stem cell maintenance, where it acts synergistically with polycomb member BMI1 (10). Inhibitors of MYST3 are being investigated for therapeutic value as they can induce senescence and decrease tumor growth (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Msh homeobox 1 (Msx1) is a Muscle Segment Homeobox (Msh) gene family member that acts as a transcriptional repressor during embryonic development, playing an important role in limb pattern formation, craniofacial development, and tooth development (1-3). Msx1 is expressed in the mesenchyme of the developing nail bed (2) and in fetal hair follicles, epidermis and fibroblasts; reduced expression is seen in adult epithelial-derived tissues (4). Msx1 acts in concert with the Wnt1 network to establish the midbrain dopaminergic progenator domain, a region that gives rise to neurons that are critical for normal brain function and are the cells affected in Parkinson disease (5). Mutation in the corresponding Msx1 gene correlates with abnormal tooth development in patients diagnosed with Wolf-Hirschhorn syndrome (6). Other genetic changes in the Msx1 gene result in Witkop Syndrome ("tooth and nail syndrome") and cases of abnormal tooth development associated with non-syndromic orofacial clefting (2,7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: METTL16 is an N6-adenosine methyltransferase responsible for the regulation of the MAT2A gene, which encodes S-Adenosylmethionine (SAM) synthase. Upon SAM depletion, MAT2A expression increases due to a splicing event of a retained intron. Alternative splicing and mRNA stability is governed by adenosine methylation in the 3’ UTR of the MAT2A mRNA by METTL16. These marks are then read by YTHDC1, and knockdown of either METTL16 or YTHDC1 results in decreased response to lack of SAM (1,2). The METTL16 methyltransferase domain differs from METTL3 and METTL14, having an extra N-terminal module suggesting a different set of target mRNAs (3,4). Lack of METTL16 during development has been shown to be embryonically lethal, resulting in a dysregulated transcriptome that cannot proceed past the 64-cell blastocyst stage (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Mitochondrial Calcium Uniporter Regulator 1 (MCUR1) is a mitochondrial inner membrane protein involved in the uptake of calcium. This multi-pass protein contains two transmembrane domains with both amino- and carboxy-termini projecting into the same mitochondrial intermembrane space (1). Research studies indicate that reduction in MCUR1 activity results in decreased mitochondrial Ca2+ uptake, while overexpression of MCUR1 results in increased mitochondrial calcium levels (1). MCUR1 protein directly interacts with mitochondrial calcium uniporter (MCU) and plays an essential role in the regulation of calcium uptake and maintenance of mitochondrial calcium homeostasis (1). Regulation of MCU by MCUR1 may be critical for a variety of cellular functions, including signal transduction, bioenergetics, and cell death and survival (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Melanoma cell adhesion molecule (MCAM, MUC18, CD146) is an immunoglobulin superfamily member originally described as a cell surface adhesion protein and marker of the progression and metastasis of melanoma (1,2). Expression of MCAM protein is seen in vascular endothelial cells, activated T lymphocytes, smooth muscle, and bone marrow stromal cells. Research studies demonstrate increased MCAM expression in endothelial cells from angiogenesis-related disorders, including inflammatory bowel disease, Crohn’s disease, rheumatoid arthritis, tumors, and chronic renal failure (3). MCAM-expressing human mesenchymal stromal cells (hMSC) in the hematopoietic microenvironment are responsible for maintaining the self-renewal of hematopoietic stem and progenitor cells (HSPC) through direct contact between hMSC and those cells (2). Related studies suggest that activation of the Notch signaling pathway may also, in part, play a role in HSPC maintenance (4). Additional research indicates that MCAM may play a role in multiple sclerosis, an autoimmune inflammatory disease that affects central nervous system neurons. Endothelial MCAM within the blood-brain barrier act as adhesion receptors that permit lymphocytes to transmigrate across the barrier and produce the inflammatory lesions that characterize the disorder (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MAFB belongs to the musculoaponeurotic fibrosarcoma (MAF) family of basic leucine-zipper transcription factors (1). In mouse embryo, MAFB expression is first detected at E10.5 (2, 3). Early in development, MAFB drives differentiation of both glucagon-producing α-cells and insulin-producing β-cells in the pancreas, but later plays a more decisive role in the maturation and maintenance of functional α-cells (4, 5). Consistent with MAFB playing a critical role in mature α-cells, MAFB is enriched in α-cells within 2 weeks of birth in the pancreas (6). Glucagon and insulin secretion is tightly regulated, and imbalances in these hormones contribute to metabolic conditions. Therefore, understanding the role of MAFB in α-cell development, maintenance, and physiological function may contribute to developing deeper insights into how these cells contribute to metabolic diseases like diabetes. MAFB also regulates monocyte differentiation, indicating MAFB functions beyond the pancreas (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Lysozymes are secreted proteins that have bacteriolytic function which are critical for mammalian innate immune function. All lysozymes function to defend host animals from microbial infection by hydrolyzing bacterial cell wall peptidoglycan (1). Conventional-type lysozymes (Lysozyme C) are one of three types of lysozymes; each family member is categorized based on amino acid sequence and biochemical properties. Lysozyme C is expressed in mammalian secretions like tears, urine, and milk, but are also expressed by phagocytes such as macrophages, neutrophils, and dendritic cells. Lysozyme C is encoded in humans by a single LYZ gene. The mouse orthologs of Lysozyme C are encoded by two genes, Lyz1 and Lyz2, which encode Lysozyme C-1 and Lysozyme C-2 (Lysozyme C-1/2). Interestingly, Lyz2 is upregulated in microglia of Alzheimer's disease mouse model brains that have been stimulated by specific forms of activity (2). Lyz1 and Lyz2 are uniquely expressed in microglia, and increased Lyz2 correlates with microglia-mediated β-amyloid (Aβ) clearance, suggesting that Lysozyme C-1/2 may directly contribute to microglial-clearance of Aβ or act as a marker for certain microglial activity states in the brain (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Cancer/testis antigens (CTAs) are a family of more than 100 proteins whose normal expression is largely restricted to immune privileged germ cells of the testis, ovary, and trophoblast cells of the placenta. Although most normal somatic tissues are void of CTA expression, due to epigenetic silencing of gene expression, their expression is upregulated in a wide variety of human solid and liquid tumors (1,2). As such, CTAs have garnered much attention as attractive targets for a variety of immunotherapy-based approaches to selectively attack tumors (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Lu/BCAM (CD239) is a transmembrane cell adhesion molecule belonging to the immunoglobulin superfamily (1). The protein mediates cell adhesion by binding to basal membrane laminin α5, and cell surface integrin α4β1 (2,3). The interaction between Lu/BCAM and its ligands can be activated via phosphorylation in its cytoplasmic tail by either PKA or Akt signaling (4,5). In sickle cell disease, Lu/BCAM was reported to promote abnormal red blood cell adhesion to endothelium, and thus may contribute to vaso-occlusive crisis (6). Overexpression of Lu/BCAM has also been reported in breast cancer, skin cancer, colon cancer, and ovarian cancer (7, 8). Antibody-drug conjugates targeting Lu/BCAM on tumor cells surface has been proposed as a potential approach for cancer therapy (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: LAIR-1 is an inhibitory receptor that belongs to the Immunoglobulin superfamily. It has one extracellular Ig-like domain and an intracellular C-terminus with two ITIM (immunoreceptor tyrosine-based inhibitory motif) domains. It is found on peripheral mononuclear cells, including NK, T, and B cells, and is thought to play a negative regulatory role on the cytolytic function of these cells through signaling through collagen ligation (1). LAIR1 has been noted to be upregulated in renal cell carcinoma (2), and may play a role in expansion of Th17 cell populations in collagen-rich environments, such as in graft rejection tissue (3).