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ECM Biosciences 2016年10月最新抗体产品

2016/10/30 华泰昕生物|HyperCyte 已读

P-Cadherin (N-terminal region) M596,货号:CM5961    

Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. Cadherins cluster to form foci of homophilic binding units. A key determinant to the strength of the cadherin-mediated adhesion may be by the juxtamembrane region in cadherins. This region induces clustering and also binds to the protein p120 catenin. The cytoplasmic region is highly conserved in sequence and has been shown experimentally to regulate the cell-cell binding function of the extracellular domain of E-cadherin, possibly through interaction with the cytoskeleton. Many cadherins are regulated by phosphorylation, including N-cadherin and E-cadherin. P-Cadherin (Cadherin-3) is localized in placenta while E-Cadherin (Cadherin-1) and N-Cadherin (Cadherin-2) are found in epithelial and neural tissues, respectively. P-Cadherin is expressed in normal epithelial cells and some cancer cells, and its sequence contains 5 cadherin domains in the extracellular region. 



CD44 (Extracellular region) M588,货号:CM5881

Cell surface adhesion protein CD44 is a ubiquitously expressed type I transmembrane protein that has important functions related to cell-cell adhesion and extracellular matrix interactions. The transmembrane protein is post-translationally modified at multiple sites by glycosylation and phosphorylation. CD44 ligands include hyaluronic acid, collagens, laminins, osteopontin, serglycin, and fibronectin. CD44 has been implicated in inflammatory cell functions, as well as in tumor growth and metastasis. CD44 is overexpressed in many types of cancer; the interaction between CD44 and HER2 has been linked to an increase in ovarian carcinoma cell growth. CD44 interacts with ezrin, radixin, and moesin to link the actin cytoskeleton to the plasma membrane and the extracellular matrix. These interactions are critical for CD44 function in cell-cell adhesion and cell motility.

 


CD44 (Extracellular region) M591,    货号:CM5911    

Cell surface adhesion protein CD44 is a ubiquitously expressed type I transmembrane protein that has important functions related to cell-cell adhesion and extracellular matrix interactions. The transmembrane protein is post-translationally modfied at multiple sites by glycosylation and phosphorylation. CD44 ligands include hyaluronic acid, collagens, laminins, osteopontin, serglycin, and fibronectin. CD44 has been implicated in inflammatory cell functions as well as in tumor growth and metastasis. CD44 is overexpressed in many types of cancer; the interaction between CD44 and HER2 has been linked to an increase in ovarian carcinoma cell growth. CD44 interacts with ezrin, radixin, and moesin to link the actin cytoskeleton to the plasma membrane and the extracellular matrix. These interactions are critical for CD44 function in cell-cell adhesion and cell motility.



Desmoglein-1 (C-terminal region) M593,    货号:DM5931

The Desmoglein family of transmembrane glycoproteins include desmoglein 1, 2, and 3. Desmoglein-1 (Dsg1, CDHF4) is found in specialized plasma membrane junctions known as desmosome junctions. These junctions serve as membrane anchorage domains for intermediate filaments and microfilaments. Actin microfilaments anchor at adherens junctions to form an array of junction sizes, shapes, and positions. These junctions generally contain E- or N-Cadherins whose cytoplasmic regions are associated with cytoplasmic proteins such as α- and β- catenins, vinculin, α-actinin, and radixin. Intermediate filaments (IFs) are anchored at desmosomes by the desmosome-specific cadherin family members, desmocollin and desmoglein. These proteins associate with cytoplasmic proteins such as desmoplakin and plakoglobin (γ-Catenin). Plakoglobin is the only junctional protein found at both desmosomes and adherens junctions and, therefore, plays a crucial role in cell adhesion.    

 


Integrin α5 (Extracellular region) M595,    货号:IM5951

Integrins are cell adhesion molecules that can mediate bidirectional transfer of signals across the plasma membrane. The cytoplasmic domains of integrin family members interact with components of the signal transduction apparatus within cells. Integrin receptors contain noncovalently associated α and β subunits that consist of a large extracellular region (the ligand-binding domain), a short transmembrane region, and a cytoplasmic domain of varying length. In mammals, at least 17 α subunits and 8 β subunits have been identified and these proteins can heterodimerize to form at least 22 different receptors. Integrin α5 and integrin β1 form a receptor for fibronectin and fibrinogen. This receptor is important for vascular development. Both integrin subunits of the fibronectin receptor are heavily glycosylated in their extracellular domains. This modification is essential for proper cell attachment to basal membranes. Integrin α5 has been reported to suppress apoptosis by a Bcl-2 pathway and the C-terminal region is critical for cell motility and cytoskeletal rearrangements.    



Integrin αL (Extracellular region) M594,    货号:IM5941

Integrins are cell adhesion molecules that can mediate bidirectional transfer of signals across the plasma membrane. The cytoplasmic domains of integrin family members interact with components of the signal transduction apparatus within cells. Integrin receptors contain noncovalently associated α and β subunits that consist of a large extracellular region (the ligand-binding domain), a short transmembrane region, and a cytoplasmic domain of varying length. In mammals, at least 17 α subunits and 8 β subunits have been identified and these proteins can heterodimerize to form at least 22 different receptors. The integrin β2 subunit associates with integrin αL to form a receptor for ICAM family members. Integrin β2/αL is involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes.    



Laminin γ1 subunit (Domain IV) M597,    货号:LM5971    

The basal lamina contains Collagen Type IV, proteoglycans, and glycoproteins. Laminin is a high molecular weight (850 kDa) oligomer, consisting of three different chains (α, β, and γ) joined by disulfide bonds. The structure of laminins include two helical domains (I & II) at the COOH-terminal, a laminin IV domain, multiple EGF-like repeats, and a laminin globular domain (G), as well as an N-terminal domain VI. Domains IV and VI are the binding sites for collagen and heparan sulfate, respectively. Several isoforms have been identified for the genes of each chain. Laminin γ1 (laminin B2) contains 14 glycosylation sites and 12 cysteine repeat domains. The expression of the Laminin subunits is found in the basal lamina of tissues. Here, the protein interacts with other extracellular matrix components to mediate cell attachment, migration and organization during embryonic development.    



Osteopontin (N-terminal region) M574    ,货号:    OM5741    

TRPM7 (Ser-1493), phospho-specific    ,货号:    TP5661    The transient receptor potential melastatin (TRPM) subfamily of cation-permeable TRP channels is ubiquitously expressed in mammalian tissues. This family includes TRPM1-8. In addition to acting as a calcium-permeant channel, TRPM6 and TRPM7 possess an inherent serine/threonine kinase activity. TRPM7 specifically is involved with cellular magnesium homeostasis and neurotransmitter release. Due to the magnesium inhibition, TRPM7’s ion channel activity is very low. TRPM7 has been implicated in cell proliferation and migration during cancer progression, and its expression levels correlate with prognosis in breast cancer. TRPM7 kinase activation leads to massive autophosphorylation of the C-terminal region, including phosphorylation of Ser-1493, Ser-1513, and Ser-1569. Both Ser-1513 and Ser-1569 phosphorylation is required for kinase activity, and  phosphorylation of Ser-1513 may inhibit Caspase-mediated cleavage of the C-terminal tail. Thus, TRPM7 is a multifunctional transmembrane protein with roles in cell signaling, proliferation, migration, and death.    


TRPM7 (Ser-1513), phospho-specific, 货号:TP5671    

The transient receptor potential melastatin (TRPM) subfamily of cation-permeable TRP channels is ubiquitously expressed in mammalian tissues. This family includes TRPM1-8. In addition to acting as a calcium-permeant channel, TRPM6 and TRPM7 possess an inherent serine/threonine kinase activity. TRPM7 specifically is involved with cellular magnesium homeostasis and neurotransmitter release. Due to the magnesium inhibition, TRPM7’s ion channel activity is very low. TRPM7 has been implicated in cell proliferation and migration during cancer progression, and its expression levels correlate with prognosis in breast cancer. TRPM7 kinase activation leads to massive autophosphorylation of the C-terminal region, including phosphorylation of Ser-1493, Ser-1513, and Ser-1569. Both Ser-1513 and Ser-1569 phosphorylation is required for kinase activity, and  phosphorylation of Ser-1513 may inhibit Caspase-mediated cleavage of the C-terminal tail. Thus, TRPM7 is a multifunctional transmembrane protein with roles in cell signaling, proliferation, migration, and death.    



TRPM7 (Ser-1569), phospho-specific,货号:    TP5681    

The transient receptor potential melastatin (TRPM) subfamily of cation-permeable TRP channels is ubiquitously expressed in mammalian tissues. This family includes TRPM1-8. In addition to acting as a calcium-permeant channel, TRPM6 and TRPM7 possess an inherent serine/threonine kinase activity. TRPM7 specifically is involved with cellular magnesium homeostasis and neurotransmitter release. Due to the magnesium inhibition, TRPM7’s ion channel activity is very low. TRPM7 has been implicated in cell proliferation and migration during cancer progression, and its expression levels correlate with prognosis in breast cancer. TRPM7 kinase activation leads to massive autophosphorylation of the C-terminal region, including phosphorylation of Ser-1493, Ser-1513, and Ser-1569. Both Ser-1513 and Ser-1569 phosphorylation is required for kinase activity, and  phosphorylation of Ser-1513 may inhibit Caspase-mediated cleavage of the C-terminal tail. Thus, TRPM7 is a multifunctional transmembrane protein with roles in cell signaling, proliferation, migration, and death.  



TRPM7 Phospho-Regulation    ,货号:    TK6990    

 The transient receptor potential melastatin (TRPM) subfamily of cation-permeable TRP channels is ubiquitously expressed in mammalian tissues. This family includes TRPM1-8. In addition to acting as a calcium-permeant channel, TRPM6 and TRPM7 possess an inherent serine/threonine kinase activity. TRPM7 specifically is involved with cellular magnesium homeostasis and neurotransmitter release. Due to the magnesium inhibition, TRPM7’s ion channel activity is very low. TRPM7 has been implicated in cell proliferation and migration during cancer progression, and its expression levels correlate with prognosis in breast cancer. TRPM7 kinase activation leads to massive autophosphorylation of the C-terminal region, including phosphorylation of Ser-1493, Ser-1513, and Ser-1569. Both Ser-1513 and Ser-1569 phosphorylation is required for kinase activity, andphosphorylation of Ser-1513 may inhibit Caspase-mediated cleavage of the C-terminal tail. Thus, TRPM7 is a multifunctional transmembrane protein with roles in cell signaling, proliferation, migration, and death.


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