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Product listing: 4-1BB/CD137/TNFRSF9 Antibody, UniProt ID Q07011 #62634 to CMTM6 Antibody, UniProt ID Q9NX76 #34557

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: TNFRSF9 is a member of the tumor necrosis factor receptor superfamily (1, 2). It is also called 4-1BB or CD137 (1, 2). 4-1BB/CD137/TNFRSF9 is expressed in activated CD4+ and CD8+ T cells, natural killer cells and dendritic cells (2-5). The ligand 4-1BBL/CD137L/TNFSF9 on antigen presenting cells binds to 4-1BB/CD137/TNFRSF9 and costimulates the activation of T cells (5). The binding of agonistic antibodies to 4-1BB/CD137/TNFRSF9 also leads to costimulation for T cell activation (5). Studies have shown the effectiveness of targeting 4-1BB/CD137/TNFRSF9 by its agonistic antibodies in cancer immunotherapy (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: TNFRSF9 is a member of the tumor necrosis factor receptor superfamily (1, 2). It is also called 4-1BB or CD137 (1, 2). 4-1BB/CD137/TNFRSF9 is expressed in activated CD4+ and CD8+ T cells, natural killer cells and dendritic cells (2-5). The ligand 4-1BBL/CD137L/TNFSF9 on antigen presenting cells binds to 4-1BB/CD137/TNFRSF9 and costimulates the activation of T cells (5). The binding of agonistic antibodies to 4-1BB/CD137/TNFRSF9 also leads to costimulation for T cell activation (5). Studies have shown the effectiveness of targeting 4-1BB/CD137/TNFRSF9 by its agonistic antibodies in cancer immunotherapy (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: A20, also referred to as TNF-α-induced protein 3 (TNFAIP3), is cytokine-inducible protein that functions to inhibit apoptosis and activate NF-κB (1,2). It was first identified as a TNF-α inducible primary response gene in human umbilical vein endothelial cells, and encodes a 790-amino acid protein containing seven Cys2/Cys2-zinc finger motifs (3). Constitutive expression of A20 is observed in lymphoid tissues (4), but it is transiently expressed in a variety of cell types in response to inflammatory signals such as TNF-α (3,5), IL-1 (3,5), phorbol esters (6), and LPS (7). Expression of A20 can confer resistance to apoptosis and NF-κB activation triggered by these signals, probably through interference with TRAF (TNF receptor associated factor) family members (8,9), and interaction with the NF-κB inhibiting protein ABIN (10). Studies also show that A20 contains site-specific ubiquitin modifying activity that can contribute to its biological functions (11,12). The amino-terminus of A20 contains de-ubiquitinating (DUB) activity for Lys63 branches, such as those found in TRAF6 and RIP, while the carboxyl-terminus contains ubiquitin ligase (E3) activity for Lys48 branches of the same substrates and leads to their degradation (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The ABIN family (ABIN-1, -2, and -3) is a group of adaptor proteins that associate and cooperate with A20/TNFAIP3 (1), a ubiquitin editing protein that inhibits the key inflammatory transcription factor NF-κB (2-4). Mechanistically, A20 acts by regulating the ubiquitination of the kinase RIP, which leads to inhibition of the IKK complex (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: ADAP (adhesion and degranulation-promoting adaptor protein/SLAP-130/Fyb) is an SH3 domain-containing adaptor protein expressed by T cells, NK cells, and myeloid cells (1,2). There are two isoforms of ADAP with predicted molecular weights of 85 kDa and 90 kDa, but observed molecular weights of 120 kDa and 130 kDa (1-3). ADAP was identified as an adaptor protein that interacts with SLP-76 following T cell receptor (TCR) stimulation and was subsequently found to be important for several aspects of T cell activation (1,2). For example, ADAP is required for integrin-dependent clustering, signaling, and adhesion (4,5). In addition, ADAP interacts with CARMA1 and facilitates assembly of the CARMA1-Bcl10-MALT1 complex important for NF-κB activation downstream of TCR activation (6). Finally, following binding of a T cell to an antigen presenting cell, ADAP forms a ring at the immunological synapse that recruits dynein to enable microtubule-organizing center polarization (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Absent in melanoma 2 (AIM2) is an interferon-inducible protein containing an amino-terminal pyrin domain and carboxy-terminal HIN-200 domain that functions in innate immunity and tumor progression (1). Expression of AIM2 can inhibit cell growth and tumor formation (2,3). Furthermore, the AIM2 gene has a high frequency of mutations associated with microsatellite-unstable colorectal cancers (4). AIM2 has a critical role in the activation of caspase-1, the protease responsible for the processing of pro-inflammatory cytokines IL-1β and IL-18. Caspase-1 activation is regulated by multi-protein complexes referred to as “inflammasomes” (5,6). Distinct inflammasome complexes have been described containing NLRP1/NALP1, NLRP3/NALP3, IPAF, and AIM2. The HIN-200 domain of AIM2 is responsible for binding to cytoplasmic double stranded DNA, resulting in caspase-1 activation. (7-9). This inflammasome complex also involves binding of the pyrin domain of AIM2 to the CARD-domain protein ASC/TMS1, which then interacts directly with caspase-1. As a result, AIM2 has been demonstrated to be an important sensor for a number of different pathogens (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: AML1 (also known as Runx1, CBFA2, and PEBP2αB) is a member of the core binding factor (CBF) family of transcription factors (1,2). It is required for normal development of all hematopoietic lineages (3-5). AML1 forms a heterodimeric DNA binding complex with its partner protein CBFβ and regulates the expression of cellular genes by binding to promoter and enhancer elements. AML1 is commonly translocated in hematopoietic cancers: chromosomal translocations include t(8;21) AML1-ETO, t(12;21) TEL-AML, and t(8;21) AML-M2 (6). Phosphorylation of AML1 on several potential serine and threonine sites, including Ser249, is thought to occur in an Erk-dependent manner (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: AML1 (also known as Runx1, CBFA2, and PEBP2αB) is a member of the core binding factor (CBF) family of transcription factors (1,2). It is required for normal development of all hematopoietic lineages (3-5). AML1 forms a heterodimeric DNA binding complex with its partner protein CBFβ and regulates the expression of cellular genes by binding to promoter and enhancer elements. AML1 is commonly translocated in hematopoietic cancers: chromosomal translocations include t(8;21) AML1-ETO, t(12;21) TEL-AML, and t(8;21) AML-M2 (6). Phosphorylation of AML1 on several potential serine and threonine sites, including Ser249, is thought to occur in an Erk-dependent manner (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Chromosomal translocations result in misregulation of the proto-oncogene BCL6 in patients with B cell-derived non-Hodgkin's lymphoma (1). The BCL6 gene is selectively expressed in mature B cells and encodes a nuclear phosphoprotein that belongs to the BTB/POZ zinc finger family of transcription factors (2,3). BCL6 protein can bind to target DNA sequences of Stat6 and, analogous to Stat6, modulate the expression of interleukin-4-induced genes (4). Furthermore, BCL6 restrains p53-dependent senescence, making BCL6-active tumors functionally p53-negative (5). The mitogen-activated protein kinases, Erk1 and Erk2, but not JNK, phosphorylate BCL6 at multiple sites. Phosphorylation of BCL6 at Ser333 and Ser343 results in degradation of BCL6 by the ubiquitin/proteasome pathway in B cells (6,7). In addition, BCL6 is acetylated and its transcriptional repressor function is inhibited by the transcriptional co-activator p300 (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Blk is a Src family protein tyrosine kinase expressed in all stages of B cell development (1,2). Activation of B cells by various ligands is accompanied by activation of Blk (3). It has been suggested that Blk is involved in the control of B cell differentiation and proliferation (4,5). Blk transcripts have also been detected in human thymocytes, but not in mature T cells, implicating that Blk may play an important role in thymopoiesis (6). Blk function may be redundant, however, as mice that do not express Blk are not impaired with respect to B cell development and immune response (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: B-cell Oct binding factor-1 (BOB-1/OBF-1) is a B-cell restricted transcriptional coactivator. BOB-1 facilitates transactivation of immunoglobulins and other B-cell specific genes through the binding and activation of the transcription factors Oct-1 and Oct-2 (1-4). Research studies have demonstrated that BOB-1 expression is required for antigen-dependent B-cell maturation (5-7). In pathological conditions such as classical Hodgkin’s disease, loss of BOB-1 expression is thought, in part, to contribute to the defect in immunoglobulin gene expression by Hodgkin and Reed Sternberg cells (8,9). In the context of multiple myeloma, overexpression of BOB-1 has been shown to contribute to malignant plasma cell cell growth, in part, through enhanced transactivation of TNFRSF17/BCMA (10).

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

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

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: CARD11/Carma1/Bimp3 belongs to the MAGUK (membrane-associated guanylate kinase) family that typically function as molecular scaffolds in the assembly of multiprotein complexes (1,2). MAGUK family members contain an SH3 domain, a PDZ domain and a GuK domain homologous to guanylate kinase. In addition, CARD11 contains an amino-terminal CARD domain (caspase recruitment domain). This domain plays an important role in forming interactions with a number of proteins containing CARD domains that are involved in regulating apoptosis and NF-κB activation. CARD11 is predominately expressed in lymphocytes (1,2) and associates with the CARD domain of Bcl10. When overexpressed, CARD11 leads to the phosphorylation of Bcl10 and activation of NF-κB (1,2). CARD11 is constitutively associated with lipid rafts and is thought to function by recruiting Bcl10 and MALT1 and triggering the phosphorylation of IKKs (3,4). Several studies using the genetic disruption of CARD11 or dominant-negative mutations have demonstrated that it plays a critical role in NF-κB activation and lymphocyte signaling (4-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CARD9 is a caspase recruitment domain (CARD)-containing adaptor protein expressed by myeloid cells (1,2). It is required for antifungal immunity downstream of pathogen detection by C-type lectin receptors (CLRs) such as Dectin-1 (3,4). Recognition of carbohydrates on fungal cell walls by CLRs leads to activation of the tyrosine kinase Syk, followed by activation of PKCδ (5,6). PKCδ phosphorylates CARD9, enabling the assembly of a complex containing CARD9 and Bcl10 (6). This complex activates NF-κB, resulting in upregulation of inflammatory cytokines important for initiation of adaptive immunity (3,4,6,7). CARD9 was also shown to be important for the induction of IL-1β, downstream of the viral nucleic acid sensor RIG-I, as well as for the generation of reactive oxygen species important for bacterial killing by macrophages (2,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CARD9 is a caspase recruitment domain (CARD)-containing adaptor protein expressed by myeloid cells (1,2). It is required for antifungal immunity downstream of pathogen detection by C-type lectin receptors (CLRs) such as Dectin-1 (3,4). Recognition of carbohydrates on fungal cell walls by CLRs leads to activation of the tyrosine kinase Syk, followed by activation of PKCδ (5,6). PKCδ phosphorylates CARD9, enabling the assembly of a complex containing CARD9 and Bcl10 (6). This complex activates NF-κB, resulting in upregulation of inflammatory cytokines important for initiation of adaptive immunity (3,4,6,7). CARD9 was also shown to be important for the induction of IL-1β, downstream of the viral nucleic acid sensor RIG-I, as well as for the generation of reactive oxygen species important for bacterial killing by macrophages (2,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: CD19 is a 95 kDa coreceptor, which amplifies the signaling cascade in B cells (1). On the B cell surface, CD19 associates with CD21, CD81 and Leu-13 to exert its function. The cytoplasmic tail of CD19 has nine conserved tyrosine residues playing critical roles in CD19 mediated function by coupling signaling molecules to the receptor (1). After B cell receptor or CD19 ligation, Tyr531 and Tyr500 of CD19 are progressively phosphorylated. This phosphorylation enables the coupling of PI3 kinase and Src family tyrosine kinase to CD19 and activates the PI3K and Src signaling pathways (2,3). Coligation of B cell receptor and CD19 also promotes Tyr409 phosphorylation in CD19. The phosphorylation at these sites enables its binding to Vav and mediates elevated intracellular calcium response, as well as the JNK pathway (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: B-lymphocyte antigen CD20 (also known as MS4A1; Membrane-spanning 4-domains subfamily A member 1) is a cell surface phosphoprotein involved in the regulation of B cell activation and proliferation (1,2). It is commonly used as a marker to identify B cells and is expressed throughout B cell development, up until their differentiation into plasma cells. CD20 has no known ligand, and its expression and function are largely conserved between human and mouse (1-3). Evidence suggests that CD20 is necessary for store operated calcium (SOC) entry, which leads to elevated cytoplasmic calcium levels required for B cell activation (4-5). Anti-CD20 antibody immunotherapy depletes B cells by activation of the innate monocytic network and is a common treatment for B cell lymphomas, leukemias, and autoimmune diseases (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Cyclic ADP-ribose hydrolase 1 (CD38) is a transmembrane protein involved in several important biological processes, including immune response, insulin secretion, and social behavior. Originally described as a glycosylated immune cell surface marker, additional research determined that CD38 is a multifunctional enzyme that catalyzes the synthesis and hydrolysis of cyclic ADP ribose (cADPR) from NAD (1,2). Under acidic conditions, CD38 also catalyzes the synthesis of nicotinic acid adenine dinucleotide phosphate (NAADP) from NADP+. Both cADPR and NAADP act as calcium ion mobilizing messengers that target different intracellular Ca2+ stores (3-6). Since CD38 is the primary mammalian NAD+ glycohydrolase responsible for NAD+ metabolism, CD38 may be a valuable therapeutic target for treatment of metabolic diseases regulated by NAD+-dependent pathways (7,8). CD38 has also been considered a possible therapeutic target for antibody-mediated therapy for myeloma and chronic lymphocytic leukemia (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CD44 is a type I transmembrane glycoprotein that mediates cell-cell and cell-matrix interaction through its affinity for hyaluronic acid (HA) and possibly through other parts of the extracellular matrix (ECM). CD44 is highly polymorphic, possesses a number of alternative splice variants and undergoes extensive post-translational modifications (1,2). Increased surface levels of CD44 are characteristic of T cell activation, and expression of the protein is upregulated during the inflammatory response. Research studies have shown that interactions between CD44 and HER2 are linked to an increase in ovarian carcinoma cell growth (1-3). CD44 interacts with ezrin, radixin and moesin (ERM), linking the actin cytoskeleton to the plasma membrane and the ECM (4-6). CD44 is constitutively phosphorylated at Ser325 in resting cells. Activation of PKC results in phosphorylation of Ser291, dephosphorylation of Ser325, disassociation of ezrin from CD44, and directional motility (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CD59 is a GPI-anchored membrane protein that functions as inhibitor of the complement membrane attack complex (MAC). CD59 binds to complement components C8 and C9, preventing C9 polymerization and insertion into membranes, therefore inhibiting the complement-dependent cytolysis (CDC) (1). CD59 is a ubiquitously expressed cell membrane protein that protects cells from CDC. Rare cases of CD59 deficiency have been reported to cause paroxysmal nocturnal hemoglobinuria in human patients (2,3). Expression of CD59 on tumor cells and viral infected cells makes them resist antibody-dependent complement-mediated lysis. Potent inhibitors for CD59 have been actively pursued for therapeutic applications (4,5). In addition, CD59 may regulate insulin secretion by modulating exocytosis (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CD7 is a type-I transmembrane glycoprotein belonging to the immunoglobulin superfamily. CD7 is one of the earliest surface markers to be expressed on the surface of developing T cells and its expression is maintained throughout maturation of multiple T cell subsets and NK cells (1-3). Engagement of CD7 through binding its ligand, SECTM1, has been shown to promote tyrosine phosphorylation of its cytoplasmic domain, recruitment of PI3K, and delivery of costimulatory signals for T cell activation (4-6). While CD7 is expressed on normal T cells, it is also highly expressed in a variety of T cell malignancies, which has poised it as a potential target of immunotherapy (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CD70 is a type II transmembrane glycoprotein and a member of the tumor necrosis factor ligand superfamily (TNFSF), also known as CD27L and TNFSF7. It is normally expressed on the medullary thymic epithelial cells. Its expression is induced on activated lymphoid cells (B cells, T cells, and NK cells) and dendritic cells. CD70 is a ligand for CD27, a co-stimulatory receptor that plays an important role in T cell activation and proliferation (1,2). CD70 overexpression has been reported in various tumors such as renal cell carcinoma, glioblastoma, and non-small cell lung carcinoma and it’s being actively pursued as a therapeutic target (3-6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Antigen receptors found on the surface of B cells contain a heterodimeric signaling component composed of CD79A and CD79B, also known as Ig α and Ig β, respectively (1,2). Presence of this receptor complex is essential for B-cell development and function (3). Together these two proteins and the associated B cell receptor initiate intracellular signaling following antigen binding (4,5). An immunoreceptor tyrosine-based activation motif (ITAM) found in the CD79A intracellular region appears to be important for its function (6). Antigen binding precedes formation of the CD79A and CD79B heterodimer and subsequent activation of receptor associated kinases (7). Research has shown that CD79A is a marker for B-lineage lymphoblastic leukemia (8). Additionally, investigators have found that mutations in the CD79A (MB1) gene are associated with abnormally low levels of functional B cell receptors in some cases of chronic B cell lymphocytic leukemia (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: CD99 is a transmembrane protein involved in many cellular functions, including cell adhesion and migration, endocytosis and exocytosis, and intracellular protein trafficking. It is highly expressed in all leukocyte lineages, Sertoli cells, granulosa cells, and pancreatic islet cells (1,2). Due to alternative splicing, there are two isoforms of CD99 that differ at the carboxy-terminus. CD99 Type I (CD99wt) is the full-length form containing 185 amino acids and CD99 Type II (CD99sh) contains 161 amino acids. Their expression is differentially regulated and they may have opposite functions in different contexts (3,4). CD99 is expressed in many types of tumors and has been used for differential diagnosis of conventional Ewing sarcoma. It has been actively pursued as a therapeutic target (5,6). On the other hand, CD99 may also play a tumor suppressor role in other tumors, such as Hodgkin’s lymphomas, osteosarcomas, and pancreatic tumors (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MHC class II (MHC-II) proteins play critical roles in cellular immune responses and their expression is mainly regulated by the non-DNA binding transcription factor CIITA (MHC class II transactivator) (1,2). CIITA expression is upregulated by IFN-γ and it in turn enchances MHC-II expression and represses collagen expression (3,4). CIITA has a limited number of transcriptional targets, most of which are involved in MHC-mediated antigen presentation (5). Mutations in the CIITA are associated with the hereditary immunodeficiency disease Bare Lymphocyte Syndrome (BLS) which is characterized by a nearly complete absence of MHC-II expression (also referred to as MHC-II deficiency) (6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Interleukin-1β (IL-1β), one of the major caspase-1 targets, is a multifunctional cytokine that is involved in a host of immune and proinflammatory responses (1). It is produced primarily by activated monocytes and macrophages. It signals through various adaptor proteins and kinases that lead to activation of numerous downstream targets (2-6). Human IL-1β is synthesized as a 31 kDa precursor. To gain activity, the precursor must be cleaved by caspase-1 between Asp116 and Ala117 to yield a 17 kDa mature form (7,8). Detection of the 17 kDa mature form of IL-1β is a good indicator of caspase-1 activity.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: CKLF-like MARVEL transmembrane domain-containing protein 4 (CMTM4) is a member of the chemokine-like factor (CKLF)-like MARVEL transmembrane domain-containing family (1). CMTM4 acts as a tumor suppressor in various malignancies, and regulates cell growth and transition through the cell cycle in HeLa cells (1-4). CMTM4 plays an important role in angiogenesis, enabling internalization of membrane-bound vascular endothelial cadherin at adherens junctions, mediating endothelial barrier function, and controlling vascular sprouting (5). In the immune system, CMTM4 acts as a backup for CMTM6 to regulate plasma membrane expression of PD-L1, an immune inhibitory ligand critical for immune tolerance to self and anti-tumor immunity (6-8). CMTM4 may also protect PD-L1 from being polyubiquitinated and targeted for degradation (8). Due to the roles of CMTM4 in the immune system and as a tumor suppressor, it is being investigated as a therapeutic target for the treatment of cancer.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: CKLF-like MARVEL transmembrane domain-containing protein 6 (CMTM6) is a member of the chemokine-like factor (CKLF)-like MARVEL transmembrane domain-containing family (1). CMTM6 stabilizes plasma membrane expression of PD-L1, an immune inhibitory ligand critical for immune tolerance to self and anti-tumor immunity (2,3). CMTM6 associates with PD-L1 at recycling endosomes, where it protects PD-L1 from being targeted for lysosomal degradation by preventing STUB1-mediated PD-L1 ubiquitination (2,3). CMTM6 may stabilize PD-L1 expression on antigen presenting cells and potentiate inhibitory signaling by PD-1 on T cells, triggering T cell inhibition and exhaustion. CMTM6 has also been shown to interact with with CD58, ARG1, ENO1, and TMPO (2). Due to the role of CMTM6 in regulating the immune system, it is being investigated as an immunotherapeutic target for the treatment of cancer.