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Product listing: GPNMB (E4D7P) XP® Rabbit mAb, UniProt ID Q14956 #38313 to MMP-9 (D6O3H) XP® Rabbit mAb (Biotinylated), UniProt ID P14780 #15561

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Glycoprotein non-metastatic gene B (GPNMB) is a type I transmembrane glycoprotein over expressed in many types of cancer. The GPNMB glycoprotein is involved in many physiological processes, including mediating transport of late melanosomes to keratinocytes (1), regulating osteoblast and osteoclast differentiation and function (2), stimulating dendritic cell maturation, promoting adhesion of dendritic cells to endothelial cells (3), enhancing autophagosome fusion to lysomes in tissue repair, and regulating degradation of cellular debris (4,5).While typical GPNMB expression is seen in tissues including skin, heart, kidney, lung, liver, and skeletal muscle (3,6), research studies show elevated GPNMB expression often contributes to the metastatic phenotype in numerous cancers (reviewed in 7). GPNMB is typically localized to intracellular compartments in normal cells (1,8), but investigators found it primarily on the cell surface of tumor cells (9,10). Differential localization and expression, and the role of GPNMB as a tumor promoter in many cancer types make this protein a viable therapeutic target (11).The GPNMB ectodomain can be cleaved by matrix metalloproteinases and shed from the cell surface (12). Research studies identify the sheddase ADAM10 as one peptidase responsible for cleavage of the GPNMB ectodomain at the surface of breast cancer cells. Shedded GPNMB ectodomains may promote angiogenesis by inducing endothelial cell migration (13).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Integrin-linked kinases (ILKs) couple integrins and growth factors to downstream pathways involved in cell survival, cell cycle control, cell-cell adhesion and cell motility (1). ILK functions as a scaffold bridging the extracellular matrix (ECM) and growth factor receptors to the actin cytoskeleton through interactions with integrin, PINCH (which links ILK to the RTKs via Nck2), CH-ILKBP and affixin (1). ILK phosphorylates Akt at Ser473, GSK-3 on Ser9, myosin light chain 2 (MLC2) on Ser18/Thr19, as well as affixin (2-5). These phosphorylation events are key regulatory steps in modulating the activities of the targets. ILK activity is stimulated by PI3 kinase and negatively regulated by the tumor suppressor PTEN and a PP2C protein phosphatase, ILKAP (1,3,6). It has been suggested that the conserved Ser343 residue in the activation loop plays a key role in the activation of ILK1 (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2).

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

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

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2).A pair of important α4 integrins, α4β1 and α4β7, interact with VCAM-1, fibronectin, and MAdCAM-1 at cell adhesions (3). Gene knockout and antibody blocking research reveal that α4 integrins play important roles in embryonic liver and heart development and in fetal lymphocyte homing (4-6). Phosphorylation at Ser988 within the cytoplasmic tail of integrin α4 blocks binding to paxillin and promotes leading edge migration (7,8).On SDS-PAGE, integrin α4 can migrate at several different apparent molecular sizes, a 150 kDa mature protein and a 140 kDa precursor protein (a 180 kDa protein also exists under mild non-reducing conditions) (9). Integrin α4 has a cleavage site at Arg558, which results in a small portion of the protein as either an 80 kDa N-terminal or 70 kDa C-terminal fragment (10).

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

Application Methods: Western Blotting

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2).Integrin α5/β1 is involved in multiple biological processes including embryonic development, angiogenesis and tumor metastasis (4,5). By interaction with its fibronectin ligand, α5/β1 transduces signals that regulate cell adhesion, migration, matrix assembly and cytoskeletal organization (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2).The β1 subfamily includes 12 distinct integrin proteins that bind to different extracellular matrix molecules (4). Control of extracellular integrin binding influences cell adhesion and migration, while intracellular signaling messages relayed by the β1 cytoplasmic tail help to regulate cell proliferation, cytoskeletal reorganization, and gene expression (4). Research studies have implicated β1 integrin in various activities including embryonic development, blood vessel, skin, bone, and muscle formation, as well as tumor metastasis and angiogenesis (4,5).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2).The β1 subfamily includes 12 distinct integrin proteins that bind to different extracellular matrix molecules (4). Control of extracellular integrin binding influences cell adhesion and migration, while intracellular signaling messages relayed by the β1 cytoplasmic tail help to regulate cell proliferation, cytoskeletal reorganization, and gene expression (4). Research studies have implicated β1 integrin in various activities including embryonic development, blood vessel, skin, bone, and muscle formation, as well as tumor metastasis and angiogenesis (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Integrins are transmembrane glycoproteins that form heterodimers consisting of one α and one β subunit. Integrin dimers act as receptors for extracellular matrix proteins and cell-surface ligands. Integrin signaling to (inside-out) and from (outside-in) extracellular molecules regulates multiple cellular processes, such as development, wound healing, immune response, invasion, metastasis, and angiogenesis (1,2). Integrin β2 (CD18) is the β subunit of the leukocyte-specific integrin family. Leukocyte integrins include Integrin β2 (CD18)/αL (CD11a) (LFA-1, lymphocyte function associated antigen 1), Integrin β2 (CD18)/αM (CD11b) (Mac-1), Integrin β2(CD18)/αX (CD11c), and Integrin β2 (CD18)/αD (CD11d). These integrins bind to immunoglobulin superfamily members, such as ICAM-1 and VCAM-1 on endothelial cells, to mediate firm adhesion and transendothelial migration of leukocytes (3). Integrin β2 (CD18) deficiency results in LAD (leukocyte adhesion deficiency), a disease characterized by impairment of leukocyte recruitment resulting in inability to fight infection (4).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Integrins are heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2). αIIβ3 and αVβ3 are the two β3 containing integrins which are prominently expressed in hematopoietic cells and angiogenic endothelic cells and perform adhesive functions in hemostasis, wound healing and angiogenesis (1,4). Tyr773 and Tyr785 (usually referred to as Tyr747 and Tyr759 based on the chicken sequence) are phosphorylated upon ligand binding (5). Phosphorylation of these tyrosine residues is required for certain ligand-induced signaling (6). Thr779 (corresponding to Thr753 of the chicken sequence) of integrin β3 in the platelet specific αIIβ3 is phosphorylated by PKD and/or Akt, which may modulate integrin association with other signaling molecules (7).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with extracellular environment (inside-out signaling) (1,2).Integrin β4 pairs with integrin α6 on the cell surface membrane to form the integrin α6β4 heterodimer, an important laminin receptor that is essential for hemidesmosome formation and the support of stable adhesions between basal epithelial cells and the basement membrane (4,5). Integrin β4 is an important component in several growth factor induced signaling pathways that are involved in tumorigenesis and invasive cell growth (6,7).

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

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

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins having distinct tissue distribution and overlapping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with extracellular environment (inside-out signaling) (1,2).The αVβ5 integrin is expressed in various tissues and cell types, including endothelia, epithelia and fibroblasts (4). It plays a role in matrix adhesion to VN, FN, SPARC and bone sialoprotein (5) and functions in the invasion of gliomas and metastatic carcinoma cells (6,7). αVβ5 integrin plays a major role in growth-factor-induced tumor angiogenesis, where cooperative signaling by the αVβ5 integrin and growth factors regulates endothelial cell proliferation and survival (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Integrin α5β8 facilitates activation and release of TGF-β, which has immunosuppressive effects (1). Deletion of integrin β8 from dendritic cells led to development of inflammatory bowl disease and autoimmunity in mice, as well as failure to induce regulatory T cells that require TGF-β for development (2). TGF-β is also involved in Th17 cell differentiation. Mice lacking expression of integrin β8 on dendritic cells fail to develop Th17 cells and are protected from Th17-mediated autoimmune disease (3). Regulatory T cells express high levels of integrin α5β8, which enables them to suppress pathogenic T cell activation by activating latent TGF-β (4). Integrin β8 is also essential for vascular morphogenesis as integrin β8-deficient mice are embryonic or perinatal lethal and exhibit insufficient and abnormal vascular morphogenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The kindlin family of focal adhesion proteins is involved in multiple biological processes, including integrin signaling, adhesion, migration, angiogenesis, differentiation, and mitotic spindle formation (1,2). Kindlin family members 1, 2, and 3 (FERM1, FERM2, and URP2) are differentially expressed in tissues. Kindlin-1 is primarily expressed in epithelial cells, kindlin-2 is ubiquitously expressed, and kindlin-3 expression is restricted to the hematopoietic system (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The kindlin family of focal adhesion proteins is involved in multiple biological processes, including integrin signaling, adhesion, migration, angiogenesis, differentiation, and mitotic spindle formation (1,2). Kindlin family members 1, 2, and 3 (FERM1, FERM2, and URP2) are differentially expressed in tissues. Kindlin-1 is primarily expressed in epithelial cells, kindlin-2 is ubiquitously expressed, and kindlin-3 expression is restricted to the hematopoietic system (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Leupaxin is a member of the paxillin family of scaffold proteins whose functions include regulation of cell adhesion, migration and metastasis (1). Leupaxin suppresses integrin-dependent tyrosine phosphorylation of paxillin and affects the regulation of cell-matrix adhesion (2). Researchers have implicated leupaxin in the progression of human hepatocellular carcinoma through its regulation of beta-catenin-mediated transcription (3). Researchers have also shown that leupaxin regulates actin dynamics and migration of prostate cancer cells through its interaction with caldesmon (4) and down-regulation of p120-catenin (5). Studies in breast cancer implicate leupaxin in the regulation of ER-alpha transcription and invasiveness (6).

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

Application Methods: Western Blotting

Background: Liprins are a family of proteins known to function as LAR (leukocyte common antigen-related) transmembrane protein tyrosine phosphatase-interacting proteins (1). This interaction has been studied in connection to both axon guidance and mammary gland development (1,2). Liprin β1, a member of this family, is a widely expressed, multivalent cytosolic protein. Liprin β1 has been found to homodimerize at the N terminus and to heterodimerize with Liprin α1 and the metastasis-associated protein S100A4 at the C terminus (1,2). The interaction with S100A4 is believed to both inhibit its phosphorylation and to modulate complex formation with Liprin α1, resulting in a change in LAR cell adhesion properties, thus promoting cell motility and tumor metastasis (2). Liprin β1 has also been shown to have higher expression levels and to associate with KANK proteins in melanoma and to be a potential regulator of lymphatic vessel integrity (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: LOX (lysyl oxidase) is a secreted copper-dependent amine oxidase and a member of the lysyl oxidase family (1). It primarily catalyzes the oxidation of lysine (or hydroxylysine) residues in collagen and elastin to form peptidyl aldehyde derivatives (2). These modifications are required for further cross-linking of target proteins to enhance ECM (extracellular matrix) stiffness. LOX plays critical roles in vascular, lung, and skin development, and tissue damage repair (3-5). Upregulation of LOX is associated with various diseases, including cancer progression and tissue fibrosis. Aberrant LOX activity creates a favorable tumor microenvironment to promote tumor metastasis and distal colonization (6-8).

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

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

Background: LIM-containing lipoma-preferred partner (LPP) belongs to the zyxin family, members of which include LIMD1, ajuba, trip6 and zyxin. Three LIM domains at the carboxy-terminus characterize this family of proteins. Zyxin family members associate with the actin cytoskeleton and are components of both the cell-cell junction adhesive complex and the integrin-mediated adhesive complex (1). They shuttle in and out of the nucleus where they may function in transcriptional activation (1).LPP binding partners at cell-cell contacts include the actin regulator α-actinin (2) and the human tumor suppressor scrib which regulates cell migration and polarity (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Lyric/AEG-1 (Astrocyte Elevated Gene 1)/MTDH (Metadherin) was identified as a tight junction (TJ) protein based on its localization to TJ proteins in polarized epithelium (1).Differential subcellular localization and overexpression of Lyric/AEG-1/MTDH has been seen in multiple human cancers. Lyric/AEG-1/MTDH is involved in signaling pathways related to various cellular functions including proliferation and apoptosis/survival, and its alteration in cancer is associated with poor prognosis (reviewed in 2). In breast cancer, increased Lyric/AEG-1/MTDH may confer increased chemoresistance as well as metastasis (3,4). Lyric/AEG-1/MTDH expression is important in signaling and disease progression of hepatocellular carcinoma (HCC) (5) and glioblastoma multiforme (GBM) (6).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Lyric/AEG-1 (Astrocyte Elevated Gene 1)/MTDH (Metadherin) was identified as a tight junction (TJ) protein based on its localization to TJ proteins in polarized epithelium (1).Differential subcellular localization and overexpression of Lyric/AEG-1/MTDH has been seen in multiple human cancers. Lyric/AEG-1/MTDH is involved in signaling pathways related to various cellular functions including proliferation and apoptosis/survival, and its alteration in cancer is associated with poor prognosis (reviewed in 2). In breast cancer, increased Lyric/AEG-1/MTDH may confer increased chemoresistance as well as metastasis (3,4). Lyric/AEG-1/MTDH expression is important in signaling and disease progression of hepatocellular carcinoma (HCC) (5) and glioblastoma multiforme (GBM) (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The MSLN gene encodes a 69 kDa precursor protein that is proteolytically cleaved to yield Megakaryocyte Potentiating Factor (MPF) and a GPI-anchored membrane protein termed mesothelin (1). Expression of (cleaved) mesothelin is largely confined to mesothelial cells of normal pleura, pericardium, and peritoneum, but has been reported to be overexpressed in some cancers, including mesothelioma, and some pancreatic and ovarian adenocarcinomas (1,2). Although suggested to be involved in cell adhesion, the physiological functions of mesothelin have not been determined. It is known, however, that mesothelin can be shed from the cell surface following cleavage by TNF-α converting enzyme. Research studies show that serum levels of mesothelin are markedly increased in patients with mesothelioma and ovarian cancer (1), suggesting that serum mesothelin levels may have utility as a cancer biomarker (1-3).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: The MSLN gene encodes a 69 kDa precursor protein that is proteolytically cleaved to yield Megakaryocyte Potentiating Factor (MPF) and a GPI-anchored membrane protein termed mesothelin (1). Expression of (cleaved) mesothelin is largely confined to mesothelial cells of normal pleura, pericardium, and peritoneum, but has been reported to be overexpressed in some cancers, including mesothelioma, and some pancreatic and ovarian adenocarcinomas (1,2). Although suggested to be involved in cell adhesion, the physiological functions of mesothelin have not been determined. It is known, however, that mesothelin can be shed from the cell surface following cleavage by TNF-α converting enzyme. Research studies show that serum levels of mesothelin are markedly increased in patients with mesothelioma and ovarian cancer (1), suggesting that serum mesothelin levels may have utility as a cancer biomarker (1-3).

$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).

$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).