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Product listing: Miwi (D92B7) XP® Rabbit mAb, UniProt ID Q9JMB7 #6915 to MOB1 (E1N9D) Rabbit mAb, UniProt ID Q7L9L4 #13730

$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

Application Methods: Western Blotting

Background: MMP-13 (collagenase 3) belongs to the matrix metalloproteinase (MMP) superfamily of enzymes that targets many extracellular proteins, including other proteases, growth factors, cell surface receptors, and adhesion molecules (1, 2). MMP-13 is a member of a subgroup of collagenases (including MMP-1, MMP-8, and MMP-18) that play an even more important function targeting fibrillar collagen. MMP-13 is synthesized as a latent proenzyme, and proteolytic removal of the inhibitory propeptide domain is required for enzyme activation. MMP-13 protein levels are regulated at the transcriptional level, via specific transcription factors and via promoter DNA methylation (3, 4). MMP-13 preferentially cleaves Type II collagen, and research studies have shown that aberrant upregulation of MMP-13 activity can lead to cartilage loss and osteoarthritis (5, 6). In addition, MMP-13 has been shown to promote cancer development, in part through enhancing tumor angiogenesis and metastases (7-9), suggesting that collagenase activity may serve as a useful marker of tumor progression (10).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

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).

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

Application Methods: Immunohistochemistry (Paraffin), 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).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated MMP-9 (D6O3H) XP® Rabbit mAb #13667.
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).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated MMP-9 (D6O3H) XP® Rabbit mAb #13667.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

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).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: MNDA (myeloid cell nuclear differentiation antigen) is a transcription factor constitutively expressed in peripheral blood granulocytes and monocytes; low expression is also found in a subset of B cells (1,2). MNDA is a member of the interferon (IFN)-regulated 200 family of genes, which contain one or more copies of a partially conserved domain of 200 amino acid residues thought to mediate protein-protein interaction (3). MNDA may play a role in apoptosis and its expression is reduced in myelodysplastic syndromes (MDS) (4). MNDA has been proposed to be a marker for nodal marginal zone lymphoma (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Mitogen-activated protein kinases (MAPKs) are activated by various extracellular signals and play crucial roles in regulating cell proliferation, differentiation, survival, and apoptosis (1). MAPK-interacting kinases (Mnks or MKNKs) are direct downstream substrates of MAPK and were first discovered independently by the work of Fukunaga and Hunter (2) and Waskiewicz and Cooper (3). There are 2 Mnks in human, termed Mnk1 and Mnk2. Both Mnks possess a MAPK-binding domain that allows them to bind to and then to be phosphorylated by Erk and p38. The phosphorylation in the T-loop of Mnks stimulates their in vitro kinase activity toward a substrate, eukaryotic initiation factor-4E (eIF4E) (2,3). eIF4E is a key component of the translational machinery mediating the initiation of translation, but how phosphorylation of eIF4E regulates translation initiation is still under investigation (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: AMPK (AMP-activated protein kinase) is a key cellular component that regulates energy homeostasis (1,2). When the AMP/ATP ratio is increased due to energy depletion, AMPK is phosphorylated at its α1 and α2 catalytic subunits and activated (3). Studies showed that the tumor suppressor LKB1 phosphorylates and activates AMPK in mammals (4,5). MO25α (mouse protein 25α), also called CAB39 (calcium binding protein 39), is a component of the LKB1 complex in vivo (5,6). MO25α/CAB39 does not directly interact with LKB1; instead, it is physically associated with STRADα (6). Together MO25α/CAB39 and STRADα help anchor LKB1 in the cytoplasm (6). MO25α/CAB39 stablizes the LKB1-STRADα complex and further increases the catalytic activity of LKB1 (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: MOB1 was first identified in yeast as a protein that binds to Mps with essential roles in the completion of mitosis and the maintenance of ploidy (1). Its Drosophila and mammalian homologs, Mats and MOB1, respectively, are involved in the Hippo signaling tumor suppressor pathway, which plays a critical role in organ size regulation and which has been implicated in cancer development (2-5). There are two MOB1 proteins in humans, MOB1α and MOB1β, that are encoded by two different genes but which have greater than 95% amino acid sequence identity (6). Both forms bind to members of the nuclear Dbf2-related (NDR) kinases, such as LATS1/2 and NDR1/2, thereby stimulating kinase activity (7-9). This binding is promoted by the phosphorylation of MOB1 at several threonine residues by MST1 and/or MST2 (5,10).