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Product listing: Mili (D14F5) XP® Rabbit mAb, UniProt ID Q8CDG1 #5940 to MMP-2 (D8N9Y) Rabbit mAb, UniProt ID P08253 #13132

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: The Drosophila piwi gene was identified as being required for the self-renewal of germ-line stem cells (1). Piwi homologs are well conserved among various species including Arabidopsis, C. elegans, and human (1). Miwi and Mili proteins are both mouse homologs of Piwi and contain a C-terminal Piwi domain (2). Miwi and Mili bind to Piwi-interacting RNAs (piRNAs) in male germ cells and are essential for spermatogenesis in mouse (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The mTORC1 kinase complex plays a critical role in cell growth regulation (1,2). mTORC1 activity is modulated by energy levels, growth factors, and amino acids (3,4). Four related GTPases (RagA, RagB, RagC, and RagD) interact with raptor in mTORC1, which is necessary and sufficient for mTORC1 activation in response to amino acid signals (1,2). The GAP Activity Towards Rags (GATOR) complex interacts with Rag GTPases and is made up of a pair of protein subcomplexes (5). The GATOR1 subcomplex includes the proteins DEPDC5, Nprl2 and Nprl3, and is a RagA and RagB GTPase-activating protein (GAP) that negatively regulates mTORC1 signaling. Conversely, the GATOR2 subcomplex (including Mios, WDR24, WDR59, Seh1L and Sec13 proteins) is a positive regulator of mTORC1 signaling (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CENP-A, also known as the chromatin-associated protein CSE4 (capping-enzyme suppressor 4-p), is an essential histone H3 variant that replaces canonical histone H3 in centromeric heterochromatin. The inherited localization of the centromere is specified by CENP-A (1). CENP-A deposition to the correct chromosomal location in early G1 phase is regulated by the Mis18 complex, which consists of Mis18-alpha, Mis18-beta, Mis18BP1, RbAp48 and RbAp46 (2).Mis18-alpha deficiency in mice results in inappropriate localization of CENP-A, as well as DNA methylation defects (3). Localization of the Mis18 complex to centromeres is regulated by the mitotic kinase Plk1 (polo-like kinase 1) (4).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Class A basic helix-loop-helix protein 15 (MIST1, bHLHa15) is a highly conserved basic helix loop helix family transcription factor that binds E-box motifs and regulates the expression of developmentally regulated genes (1). MIST1 can bind DNA as a homodimer, or may heterodimerize with other bHLH proteins to regulate target gene expression (1). MIST1 is expressed in an array of tissues, including salivary glands, stomach, small intestine, and the pancreas, but is generally restricted to secretory cell subtypes (2). In the pancreas, MIST1 is essential for the maturation, maintenance, and function of acinar cells (3). In gastric chief cells, MIST1 regulates the expression of RAB26 and RAB3D, two GTPases that function to regulate secretory granule formation (4). Loss of MIST1 in gastric chief cells may be a potential marker of gastric epithelial neoplasia (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: Microphthalmia-associated transcription factor (MITF) is a basic helix-loop-helix leucine zipper transcription factor that is most widely known for its roles in melanocyte, ophthalmic, and osteoclast development (1-3). In humans, MITF can function as a melanoma oncogene (4) and mutations in the corresponding MITF gene are associated with Waardenburg syndrome type 2, an auditory-pigmentary syndrome characterized by developmental defects in cells derived from neural crest (5). At least 12 isoforms of MITF have been identified, which exhibit differential patterns of expression among cell and tissue types (6).

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

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

Background: Microphthalmia-associated transcription factor (MITF) is a basic helix-loop-helix leucine zipper transcription factor that is most widely known for its roles in melanocyte, ophthalmic, and osteoclast development (1-3). In humans, MITF can function as a melanoma oncogene (4) and mutations in the corresponding MITF gene are associated with Waardenburg syndrome type 2, an auditory-pigmentary syndrome characterized by developmental defects in cells derived from neural crest (5). At least 12 isoforms of MITF have been identified, which exhibit differential patterns of expression among cell and tissue types (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Mitofusins are mitochondrial transmembrane GTPases that function to regulate mitochondrial fusion, a process that occurs in concert with mitochondrial division and is necessary for the maintenance of structural and genetic mitochondrial integrity (1,2). Two mitofusins have been described in mammals, mitofusin-1 and -2, which share 60% amino acid identity and appear to function coordinately to regulate mitochondrial fusion (3). Mitochondrial fusion is widely recognized as important for normal cell growth and development (4), and may have evolved as a mechanism to offset the deleterious effects of mtDNA mutations (3). Null mutations in either mitofusin are embryonic lethal in mice, whereas conditional knockout studies have shown that combined deletion of mitofusin-1 and mitofusin-2 in skeletal muscle results in severe mitochondrial dysfunction (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey

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

Background: Mitofusins are mitochondrial transmembrane GTPases that function to regulate mitochondrial fusion, a process that occurs in concert with mitochondrial division and is necessary for the maintenance of structural and genetic mitochondrial integrity (1,2). Two mitofusins have been described in mammals, mitofusin-1 and -2, which share 60% amino acid identity and appear to function coordinately to regulate mitochondrial fusion (3). Mitochondrial fusion is widely recognized as important for normal cell growth and development (4), and may have evolved as a mechanism to offset the deleterious effects of mtDNA mutations (3). Null mutations in either mitofusin are embryonic lethal in mice, whereas conditional knockout studies have shown that combined deletion of mitofusin-1 and mitofusin-2 in skeletal muscle results in severe mitochondrial dysfunction (3).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Mitofusin-2 (D2D10) Rabbit mAb #9482.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Mitofusins are mitochondrial transmembrane GTPases that function to regulate mitochondrial fusion, a process that occurs in concert with mitochondrial division and is necessary for the maintenance of structural and genetic mitochondrial integrity (1,2). Two mitofusins have been described in mammals, mitofusin-1 and -2, which share 60% amino acid identity and appear to function coordinately to regulate mitochondrial fusion (3). Mitochondrial fusion is widely recognized as important for normal cell growth and development (4), and may have evolved as a mechanism to offset the deleterious effects of mtDNA mutations (3). Null mutations in either mitofusin are embryonic lethal in mice, whereas conditional knockout studies have shown that combined deletion of mitofusin-1 and mitofusin-2 in skeletal muscle results in severe mitochondrial dysfunction (3).

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

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

Background: Mitofusins are mitochondrial transmembrane GTPases that function to regulate mitochondrial fusion, a process that occurs in concert with mitochondrial division and is necessary for the maintenance of structural and genetic mitochondrial integrity (1,2). Two mitofusins have been described in mammals, mitofusin-1 and -2, which share 60% amino acid identity and appear to function coordinately to regulate mitochondrial fusion (3). Mitochondrial fusion is widely recognized as important for normal cell growth and development (4), and may have evolved as a mechanism to offset the deleterious effects of mtDNA mutations (3). Null mutations in either mitofusin are embryonic lethal in mice, whereas conditional knockout studies have shown that combined deletion of mitofusin-1 and mitofusin-2 in skeletal muscle results in severe mitochondrial dysfunction (3).

$293
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: The Drosophila piwi gene was identified as being required for the self-renewal of germline stem cells (1). Piwi homologs are well conserved among various species including Arabidopsis, C. elegans, and Homo sapiens (1). Both Miwi and Mili proteins are mouse homologs of Piwi and contain a C-terminal Piwi domain (2). Miwi and Mili bind to Piwi-interacting RNAs (piRNAs) in male germ cells and are essential for spermatogenesis in mice (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Miz-1 (Zbtb17) is a poxvirus and zinc finger (POZ) transcription factor with an amino-terminal BTB/POZ domain and 13 carboxy-terminal zinc finger domains. Miz-1 plays a key role in cell cycle control through activation of the cyclin-dependent kinase inhibitors p15, INK4B, and p21 Waf1/Cip1 (1-4). The transcriptional activity of Miz-1 is repressed through direct interaction with Myc (1-4). In the presence of DNA damage, Myc is recruited to the p21 Waf1/Cip1 promoter by Miz-1 and blocks p53-mediated induction of p21 Waf1/Cip1, ultimately resulting in p53-mediated apoptosis rather than cell cycle arrest (4). Miz-1 also plays a role during lymphocyte development. In developing B and T cells, Miz-1 represses suppressor of cytokine signaling 1 (SOCS1) expression, which enables signaling through the IL-7 receptor and upregulation of the pro-survival protein Bcl-2 (5,6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: MKK3 and MKK6 are two closely related dual-specificity protein kinases that activate p38 MAP kinase (1-5). MKK3 and MKK6 both phosphorylate and activate p38 MAP kinase at its activation site, Thr-Gly-Tyr, but do not phosphorylate or activate Erk1/2 or SAPK/JNK. Phosphorylation of p38 MAP kinase dramatically stimulates its ability to phosphorylate protein substrates such as ATF-2 and Elk-1. MKK3 and MKK6 are both activated by different forms of cellular stress and inflammatory cytokines (4,5). Activation of MKK3 and MKK6 occurs through phosphorylation at Ser189 and Thr222 on MKK3 (2) and Ser207 and Thr211 on MKK6 (4,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: MKK3 and MKK6 are two closely related dual-specificity protein kinases that activate p38 MAP kinase (1-5). MKK3 and MKK6 both phosphorylate and activate p38 MAP kinase at its activation site, Thr-Gly-Tyr, but do not phosphorylate or activate Erk1/2 or SAPK/JNK. Phosphorylation of p38 MAP kinase dramatically stimulates its ability to phosphorylate protein substrates such as ATF-2 and Elk-1. MKK3 and MKK6 are both activated by different forms of cellular stress and inflammatory cytokines (4,5). Activation of MKK3 and MKK6 occurs through phosphorylation at Ser189 and Thr222 on MKK3 (2) and Ser207 and Thr211 on MKK6 (4,5).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

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

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

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

Background: Mismatch repair (MMR), a conserved process that involves correcting errors made during DNA synthesis, is crucial to the maintenance of genomic integrity. MLH1 is the human homologue of the E. coli MMR gene mutL. MMR requires recognition of a base mismatch or insertion/deletion loop by a MutS homolog followed by recruitment of a MutL heterodimeric complex consisting of MLH1 and PMS1 (MutL-γ), PMS2 (MutL-α) or MLH3 (MutL-γ). Other factors required for MMR in eukaryotes are EXO1, PCNA, RFC, RPA, DNA polymerases and DNA ligase (reviewed in 1). Inactivation of the MLH1 gene causes genome instability and predisposition to cancer (2-5). The MLH1 gene is frequently mutated in hereditary nonpolyposis colon cancer (HNPCC) (6). MLH1 also plays a role in meiotic recombination (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Mismatch repair (MMR), a conserved process that involves correcting errors made during DNA synthesis, is crucial to the maintenance of genomic integrity. MLH1 is the human homologue of the E. coli MMR gene mutL. MMR requires recognition of a base mismatch or insertion/deletion loop by a MutS homolog followed by recruitment of a MutL heterodimeric complex consisting of MLH1 and PMS1 (MutL-γ), PMS2 (MutL-α) or MLH3 (MutL-γ). Other factors required for MMR in eukaryotes are EXO1, PCNA, RFC, RPA, DNA polymerases and DNA ligase (reviewed in 1). Inactivation of the MLH1 gene causes genome instability and predisposition to cancer (2-5). The MLH1 gene is frequently mutated in hereditary nonpolyposis colon cancer (HNPCC) (6). MLH1 also plays a role in meiotic recombination (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Mixed-lineage kinases (MLKs) belong to the mitogen activated kinase kinase kinase (MAPKKK) family of dual-specificity protein kinases. While not particularly well conserved at the sequence level, MLK1, 2 and 3 share a conserved domain structure consisting of a catalytic core and two isoleucine/leucine zipper motifs among other protein-protein binding domains (1). MLK1 preferentially stimulates the JNK (c-Jun amino-terminal kinase) pathway in response to agonists and stress (2). Although multiple phosphorylation events are required for full activation of MLK1, two autophosphorylation sites within the activation loop (Ser308 and Thr312) appear to be the predominant activation residues (3). In neuronal cells, MLK1 appears to function downstream of the small G-proteins Rac1 and Cdc42 and upstream of MKK4 and MKK7 to promote apoptosis (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Necroptosis, a regulated pathway for necrotic cell death, is triggered by a number of inflammatory signals including cytokines in the tumor necrosis factor (TNF) family, pathogen sensors such as toll-like receptors (TLRs), and ischemic injury (1,2). The process is negatively regulated by caspases and is initiated through a complex containing the RIP1 and RIP3 kinases, typically referred to as the necrosome. Mixed lineage kinase domain-like protein (MLKL) is a pseudokinase that was identified as downstream target of RIP3 in the necroptosis pathway (3,4). During necroptosis RIP3 is phosphorylated at Ser227, which recruits MLKL and leads to its phosphorylation at Thr357 and Ser358 (3). Knockdown of MLKL through multiple mechanisms results in inhibition of necroptosis (3-5). While the precise mechanism for MLKL-induced necroptosis is unclear, some studies have shown that necroptosis leads to oligomerization of MLKL and translocation to the plasma membrane, where it effects membrane integrity (6-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Necroptosis, a regulated pathway for necrotic cell death, is triggered by a number of inflammatory signals including cytokines in the tumor necrosis factor (TNF) family, pathogen sensors such as toll-like receptors (TLRs), and ischemic injury (1,2). The process is negatively regulated by caspases and is initiated through a complex containing the RIP1 and RIP3 kinases, typically referred to as the necrosome. Mixed lineage kinase domain-like protein (MLKL) is a pseudokinase that was identified as downstream target of RIP3 in the necroptosis pathway (3,4). During necroptosis RIP3 is phosphorylated at Ser227, which recruits MLKL and leads to its phosphorylation at Thr357 and Ser358 (3). Knockdown of MLKL through multiple mechanisms results in inhibition of necroptosis (3-5). While the precise mechanism for MLKL-induced necroptosis is unclear, some studies have shown that necroptosis leads to oligomerization of MLKL and translocation to the plasma membrane, where it effects membrane integrity (6-9).

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

Application Methods: 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, mammals contain six Set1-related proteins: 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, which 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).MLL1 functions as a master regulator of both embryogenesis and hematopoiesis, and is required for proper expression of Hox genes (7,8). MLL1 is a large, approximately 4000 amino acid, protein that is cleaved by the taspase 1 threonine endopeptidase to form N-terminal (MLL1-N) and C-terminal MLL1 (MLL1-C) fragments, both of which are subunits of the functional MLL1/COMPASS complex (9,10). MLL1-N, MLL1-C, WDR5, RBBP5 and ASH2L define the core catalytic component of the MLL1/COMPASS complex, which is recruited to target genes and methylates histone H3 lysine 4 to regulate transcriptional initiation (11). At least 60 different MLL1 translocation partners have been molecularly characterized and associated with various hematological malignancies. The most common translocation partners include AF4, AF9, ENL, AF10, ELL and AF6 (8,12,13). With the exception of AF6, all of these partners are nuclear proteins that function to positively regulate transcriptional elongation. AF4, AF9 and ENL are all components of the super elongation complex (SEC), while AF4, AF9, AF10 and ENL all interact with the histone H3 lysine 79 methyltransferase DOT1L. Many MLL1 target genes are normally regulated by promoter-proximal pausing, with the release of RNA polymerase and transcriptional elongation occurring in response to proper stimuli (14). The association of MLL1 translocation partners with SEC and DOT1L suggest that MLL1-fusion proteins may function to sustain specific gene expression programs by constitutively activating transcriptional elongation.

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

Application Methods: Immunofluorescence (Immunocytochemistry), 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, mammals contain six Set1-related proteins: 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, which 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).MLL1 functions as a master regulator of both embryogenesis and hematopoiesis, and is required for proper expression of Hox genes (7,8). MLL1 is a large, approximately 4000 amino acid, protein that is cleaved by the taspase 1 threonine endopeptidase to form N-terminal (MLL1-N) and C-terminal MLL1 (MLL1-C) fragments, both of which are subunits of the functional MLL1/COMPASS complex (9,10). MLL1-N, MLL1-C, WDR5, RBBP5 and ASH2L define the core catalytic component of the MLL1/COMPASS complex, which is recruited to target genes and methylates histone H3 lysine 4 to regulate transcriptional initiation (11). At least 60 different MLL1 translocation partners have been molecularly characterized and associated with various hematological malignancies. The most common translocation partners include AF4, AF9, ENL, AF10, ELL and AF6 (8,12,13). With the exception of AF6, all of these partners are nuclear proteins that function to positively regulate transcriptional elongation. AF4, AF9 and ENL are all components of the super elongation complex (SEC), while AF4, AF9, AF10 and ENL all interact with the histone H3 lysine 79 methyltransferase DOT1L. Many MLL1 target genes are normally regulated by promoter-proximal pausing, with the release of RNA polymerase and transcriptional elongation occurring in response to proper stimuli (14). The association of MLL1 translocation partners with SEC and DOT1L suggest that MLL1-fusion proteins may function to sustain specific gene expression programs by constitutively activating transcriptional elongation.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), 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, mammals contain six Set1-related proteins: 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, which 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).MLL2, also known as histone-lysine N-methyltransferase 2B (KMT2B), functions to activate gene expression by mediating tri-methylation of histone H3 lysine 4 at the promoters of genes involved in embryogenesis and hematopoiesis, and is required for histone H3 lysine 4 tri-methylation at bivalent promoters in embryonic stem cells (7). Like MLL1, MLL2 is a large protein made up of approximately 2700 amino acids that is cleaved by the Taspase 1 threonine endopeptidase to form N-terminal (MLL2-N) and C-terminal (MLL2-C) fragments, both of which are subunits of the functional MLL2/COMPASS complex. MLL2-N, MLL2-C, WDR5, RBBP5, and ASH2L define the core catalytic component of the MLL2/COMPASS complex, which is recruited to target genes to regulate transcription. MLL1 gene translocations are often associated with various hematological malignancies and thought to be a driving component of these types of leukemia. MLL2 is required for memory formation, proper glucose homeostasis, and cardiac lineage differentiation of mouse embryonic stem cells (8-11). A recent study has shown that MLL2 is required for survival of MLL-AF9-transformed cells, implicating MLL2 as a potential modulator of MLL1-rearranged leukemias (12). Mutations in MLL2 cause complex early-onset dystonia, and overexpression of MLL2 is associated with gastrointestinal diffuse large B-cell lymphoma (13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: 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, mammals contain six Set1-related proteins: 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, which 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).MLL3, also known as histone-lysine N-methyltransferase 2C (KMT2C), is a large 540 kDa protein that functions as part of the MLL3/COMPASS-like complex to activate gene expression by mediating mono-methylation of histone H3 lysine 4 at gene enhancers (7). Enhancer-specific H3 lysine 4 mono-methylation (H3K4me1) correlates with increased levels of chromatin interactions between gene enhancers and promoters, while loss of this modification results in a reduction of enhancer-promoter interactions (8). Furthermore, H3K4me1 facilitates recruitment of the Cohesin complex, which may function to promote the interactions between gene enhancers and promoters (8). MLL3 is found to be mutated or have altered expression in a number of different cancers (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Western Blotting

Background: The super elongation complex (SEC) plays a critical role in regulating RNA polymerase II (RNAPII) transcription elongation (1). The SEC is composed of AFF4, AFF1/AF4, MLLT3/AF9, and MLLT1/ENL proteins. The pathogenesis of mixed lineage leukemia is often associated with translocations of the SEC subunits joined to the histone H3 Lys4 methyltransferase mixed lineage leukemia (MLL) gene (1-4). The SEC has been found to contain RNAPII elongation factors eleven-nineteen lysine-rich leukemia (ELL), ELL2, and ELL3, along with the associated factors EAF1 and EAF2, which can increase the catalytic rate of RNAPII transcription in vitro, (1,2,5-7). The SEC positive transcription elongation factor b (P-TEFb) phosphorylates the carboxy-terminal domain within the largest subunit of RNAP II at Ser2 of the heptapeptide repeat. The SEC negative transcription elongation factors, DRB-induced stimulating factor (DSIF) and negative elongation factor (NELF), signal the transition from transcription initiation and pausing to productive transcription elongation (2,8-10). The chromosomal translocation of MLL with the members of the SEC leads to SEC recruitment to MLL regulated genes, such as the highly developmentally regulated Hox genes, implicating the misregulation and overexpression of these genes as underlying contributors to leukemogenesis (1,2,9,11).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Max-like protein X (MLX), also known as transcription factor-like protein 4 (TCFL4), is a member of the Myc/Max/Mad network of transcriptional regulator proteins that share a common basic-helix-loop-helix zipper (bHLH-ZIP) motif required for dimerization and DNA-binding (1,2). MLX is ubiquitously expressed in most cell lines and functions as a binding partner for MLXIP (also known as MondoA) and MLXIPL (also known as ChREBP) (1,2). MLX/MLXIP and MLX/MLXIPL heterodimers function to regulate glucose homeostasis by sensing glucose metabolites in the cell. These heterodimeric protein complexes reside mainly in the cytoplasm and mitochondria of cells grown in low glucose, and translocate to the nucleus upon increased intracellular glucose levels to activate transcription of downstream target genes (1,2). MLX/MLXIP is required for the deregulated Myc-induced reprogramming of multiple metabolic pathways during oncogenesis (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The matrix metalloproteinase (MMP) family of proteases is a group of zinc-dependent enzymes that target extracellular proteins, including growth factors, cell surface receptors, adhesion molecules, matrix structural proteins, and other proteases (1, 2). Within this family, MMP1, MMP8, and MMP13 have been characterized as a collagenase sub-family of MMPs targeting fibrillar collagen (collagen type I, II, and III) for degradation. In addition to collagen, MMP1 also has activity toward a broad array of other ECM proteins such as fibronectin, gelatin, aggrecan (etc.), as well as growth factors, chemokines, and cytokines (3). MMP1 is widely involved in tissue remodeling during wound healing, tumor growth, invasion and metastasis, and arthritis (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors, and adhesion molecules (1). Among the family members, MMP-2, MMP-3, MMP-7, and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (2-4). Research studies have shown that MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein (5).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors, and adhesion molecules (1). Among the family members, MMP-2, MMP-3, MMP-7, and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (2-4). Research studies have shown that MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors, and adhesion molecules (1). Among the family members, MMP-2, MMP-3, MMP-7, and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (2-4). Research studies have shown that MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein (5).