Supplier: Bioss

The coiled-coil domain is a structural motif found in proteins that are involved in a diverse array of biological functions such as the regulation of gene expression, cell division, membrane fusion and drug extrusion and delivery. CCDC69 (Coiled-coil domain-containing protein 69) is a 296 amino acid protein that is encoded by a gene which maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Chromosome 5 is associated with Cockayne syndrome through the ERCC8 gene and familial adenomatous polyposis through the adenomatous polyposis coli (APC) tumor suppressor gene. Treacher Collins syndrome is also chromosome 5-associated and is caused by insertions or deletions within the TCOF1 gene. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.

Supplier: Bioss

The coiled-coil domain is a structural motif found in proteins that are involved in a diverse array of biological functions such as the regulation of gene expression, cell division, membrane fusion and drug extrusion and delivery. CCDC69 (Coiled-coil domain-containing protein 69) is a 296 amino acid protein that is encoded by a gene which maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Chromosome 5 is associated with Cockayne syndrome through the ERCC8 gene and familial adenomatous polyposis through the adenomatous polyposis coli (APC) tumor suppressor gene. Treacher Collins syndrome is also chromosome 5-associated and is caused by insertions or deletions within the TCOF1 gene. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.

Supplier: Bioss

The coiled-coil domain is a structural motif found in proteins that are involved in a diverse array of biological functions such as the regulation of gene expression, cell division, membrane fusion and drug extrusion and delivery. CCDC69 (Coiled-coil domain-containing protein 69) is a 296 amino acid protein that is encoded by a gene which maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Chromosome 5 is associated with Cockayne syndrome through the ERCC8 gene and familial adenomatous polyposis through the adenomatous polyposis coli (APC) tumor suppressor gene. Treacher Collins syndrome is also chromosome 5-associated and is caused by insertions or deletions within the TCOF1 gene. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.

Supplier: ProSci Inc.

4E-BP1(eukaryotic translation Initiation Factor 4E Binding Protein 1),also called ELF4EBP1/BP-1/PHAS-I ,which is located on chromosome 8p12, with 118-amino acid protein (about 13 kDa). Binding of eIF4EBP1 to eIF4E is reversible and is dependent on the phosphorylation status of eIF4EBP1. Non phosphorylated eIF4EBP1 will bind strongly to eIF4E while(24 kDa), the phosphorylated form will not. Akt, TOR, MAP kinase, S6 kinase, and Cdc2 are known kinases capable of inactivating eIF4EBP1 binding to eIF4E by phosphorylating either threonines 35, 45, 69 or serine 64. Although, not all phosphorylation events equally block the eIF4EBP1-eIF4E interaction.

Supplier: ProSci Inc.

4E-BP1(eukaryotic translation Initiation Factor 4E Binding Protein 1),also called ELF4EBP1/BP-1/PHAS-I ,which is located on chromosome 8p12, with 118-amino acid protein (about 13 kDa). Binding of eIF4EBP1 to eIF4E is reversible and is dependent on the phosphorylation status of eIF4EBP1. Non phosphorylated eIF4EBP1 will bind strongly to eIF4E while(24 kDa), the phosphorylated form will not. Akt, TOR, MAP kinase, S6 kinase, and Cdc2 are known kinases capable of inactivating eIF4EBP1 binding to eIF4E by phosphorylating either threonines 35, 45, 69 or serine 64. Although, not all phosphorylation events equally block the eIF4EBP1-eIF4E interaction.

Supplier: Bioss

The coiled-coil domain is a structural motif found in proteins that are involved in a diverse array of biological functions such as the regulation of gene expression, cell division, membrane fusion and drug extrusion and delivery. CCDC69 (Coiled-coil domain-containing protein 69) is a 296 amino acid protein that is encoded by a gene which maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Chromosome 5 is associated with Cockayne syndrome through the ERCC8 gene and familial adenomatous polyposis through the adenomatous polyposis coli (APC) tumor suppressor gene. Treacher Collins syndrome is also chromosome 5-associated and is caused by insertions or deletions within the TCOF1 gene. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.

Supplier: Bioss

The coiled-coil domain is a structural motif found in proteins that are involved in a diverse array of biological functions such as the regulation of gene expression, cell division, membrane fusion and drug extrusion and delivery. CCDC69 (Coiled-coil domain-containing protein 69) is a 296 amino acid protein that is encoded by a gene which maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Chromosome 5 is associated with Cockayne syndrome through the ERCC8 gene and familial adenomatous polyposis through the adenomatous polyposis coli (APC) tumor suppressor gene. Treacher Collins syndrome is also chromosome 5-associated and is caused by insertions or deletions within the TCOF1 gene. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.

Supplier: Bioss

The coiled-coil domain is a structural motif found in proteins that are involved in a diverse array of biological functions such as the regulation of gene expression, cell division, membrane fusion and drug extrusion and delivery. CCDC69 (Coiled-coil domain-containing protein 69) is a 296 amino acid protein that is encoded by a gene which maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Chromosome 5 is associated with Cockayne syndrome through the ERCC8 gene and familial adenomatous polyposis through the adenomatous polyposis coli (APC) tumor suppressor gene. Treacher Collins syndrome is also chromosome 5-associated and is caused by insertions or deletions within the TCOF1 gene. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.

Supplier: Bioss

The coiled-coil domain is a structural motif found in proteins that are involved in a diverse array of biological functions such as the regulation of gene expression, cell division, membrane fusion and drug extrusion and delivery. CCDC69 (Coiled-coil domain-containing protein 69) is a 296 amino acid protein that is encoded by a gene which maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Chromosome 5 is associated with Cockayne syndrome through the ERCC8 gene and familial adenomatous polyposis through the adenomatous polyposis coli (APC) tumor suppressor gene. Treacher Collins syndrome is also chromosome 5-associated and is caused by insertions or deletions within the TCOF1 gene. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.

Supplier: Biotium

This antibody recognizes a protein of HMW, identified as mucin 3 glycoprotein (MUC3). Its epitope localizes between aa SITTTE. This MAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. MUC3 is distributed in colon and rectum, and is also present to a lesser extent in breast, lung and salivary gland tissues. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.

Supplier: Biotium

This antibody recognizes a protein of HMW, identified as mucin 3 glycoprotein (MUC3). Its epitope localizes between aa SITTTE. This MAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. MUC3 is distributed in colon and rectum, and is also present to a lesser extent in breast, lung and salivary gland tissues. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.

Supplier: Biotium

This antibody recognizes a protein of HMW, identified as mucin 3 glycoprotein (MUC3). Its epitope localizes between aa SITTTE. This MAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. MUC3 is distributed in colon and rectum, and is also present to a lesser extent in breast, lung and salivary gland tissues. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.

Supplier: Biotium

This antibody recognizes a protein of HMW, identified as mucin 3 glycoprotein (MUC3). Its epitope localizes between aa SITTTE. This MAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. MUC3 is distributed in colon and rectum, and is also present to a lesser extent in breast, lung and salivary gland tissues. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.

Supplier: Biotium

This antibody recognizes a protein of HMW, identified as mucin 3 glycoprotein (MUC3). Its epitope localizes between aa SITTTE. This MAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. MUC3 is distributed in colon and rectum, and is also present to a lesser extent in breast, lung and salivary gland tissues. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.

Supplier: Biotium

This antibody recognizes a protein of HMW, identified as mucin 3 glycoprotein (MUC3). Its epitope localizes between aa SITTTE. This MAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. MUC3 is distributed in colon and rectum, and is also present to a lesser extent in breast, lung and salivary gland tissues. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.

Supplier: Biotium

This antibody recognizes a protein of HMW, identified as mucin 3 glycoprotein (MUC3). Its epitope localizes between aa SITTTE. This MAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. MUC3 is distributed in colon and rectum, and is also present to a lesser extent in breast, lung and salivary gland tissues. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.

Supplier: Biotium

This antibody recognizes a protein of HMW, identified as mucin 3 glycoprotein (MUC3). Its epitope localizes between aa SITTTE. This MAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. MUC3 is distributed in colon and rectum, and is also present to a lesser extent in breast, lung and salivary gland tissues. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.

Supplier: Biotium

This antibody recognizes a protein of HMW, identified as mucin 3 glycoprotein (MUC3). Its epitope localizes between aa SITTTE. This MAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. MUC3 is distributed in colon and rectum, and is also present to a lesser extent in breast, lung and salivary gland tissues. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.

Supplier: ProSci Inc.

Hepatocyte growth factor regulates cell growth, cell motility, and morphogenesis by activating a tyrosine kinase signaling cascade after binding to the proto-oncogenic c-Met receptor. Hepatocyte growth factor is secreted by mesenchymal cells and acts as a multi-functional cytokine on cells of mainly epithelial origin. Its ability to stimulate mitogenesis, cell motility, and matrix invasion gives it a central role in angiogenesis, tumorogenesis, and tissue regeneration. It is secreted as a single inactive polypeptide and is cleaved by serine proteases into a 69-kDa alpha-chain and 34-kDa beta-chain. A disulfide bond between the alpha and beta chains produces the active, heterodimeric molecule. The protein belongs to the plasminogen subfamily of S1 peptidases but has no detectable protease activity.Hepatocyte growth factor regulates cell growth, cell motility, and morphogenesis by activating a tyrosine kinase signaling cascade after binding to the proto-oncogenic c-Met receptor. Hepatocyte growth factor is secreted by mesenchymal cells and acts as a multi-functional cytokine on cells of mainly epithelial origin. Its ability to stimulate mitogenesis, cell motility, and matrix invasion gives it a central role in angiogenesis, tumorogenesis, and tissue regeneration. It is secreted as a single inactive polypeptide and is cleaved by serine proteases into a 69-kDa alpha-chain and 34-kDa beta-chain. A disulfide bond between the alpha and beta chains produces the active, heterodimeric molecule. The protein belongs to the plasminogen subfamily of S1 peptidases but has no detectable protease activity. Alternative splicing of this gene produces multiple transcript variants encoding different isoforms.

Supplier: ProSci Inc.

TLR6 Antibody: Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR6 was first identified as a close homolog of TLR1, sharing 69% sequence identify. Like TLR1, TLR6 can form heterodimers with TLR2, and these TLR6:TLR2 dimers coordinate macrophage activation by Gram-positive bacteria and the yeast cell wall particle zymosan. Activation of these complexes not only initiates pro-inflammatory cascades, but also can lead to apoptotic responses.

Supplier: ProSci Inc.

TLR6 Antibody: Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR6 was first identified as a close homolog of TLR1, sharing 69% sequence identify. Like TLR1, TLR6 can form heterodimers with TLR2, and these TLR6:TLR2 dimers coordinate macrophage activation by Gram-positive bacteria and the yeast cell wall particle zymosan. Activation of these complexes not only initiates pro-inflammatory cascades, but also can lead to apoptotic responses.

Supplier: ProSci Inc.

It recognises a protein of HMW, identified as mucin 3 glycoprotein (MUC3). This mAb shows no cross-reaction with human milk fat globule membranes, MUC1, or MUC2. The Mucins are a family of highly glycosylated, secreted proteins with a basic structure consisting of a variable number of tandem repeats (VNTRs) encoded by 60 base pairs (Mucin 1), 69 base pairs (Mucin 2) and 51 base pairs (Mucin 3). The number of repeats is highly polymorphic and varies among different alleles. Mucin 1 proteins are expressed as type I membrane proteins in addition to secreted forms. Mucin 1 is aberrantly expressed in epithelial tumors including breast carcinomas. Mucin 2 coats the epithelia of the intestines and airways and is associated with colonic tumors. Mucin 3 is a major component of various mucus gels and is broadly expressed in normal and tumor cells.

Supplier: Bioss

Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-69 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).

Supplier: Bioss

Mutations in the mouse Tub gene gradually lead to obesity, strongly resembling the late-onset obesity observed in the human population. In addition to excessive deposition of adipose tissue, mice with the Tub phenotype also suffer retinal degeneration and neurosensory hearing loss. A human homolog of the Tub gene has been identified, as have three related proteins, called Tubby-like protein 1 (TULP1), TULP2 and TULP3. When compared to TULP1 and TULP2, TULP3 has a wider tissue expression and is phylogenetically more similar to Tub than either TULP1 or TULP2. TULP1, expressed specifically in the retina, maps to the chromosomal region known to be involved in retinitis pigmentosa, while TULP2 maps within the minimal interval for the rod-cone dystrophy. TULP3 maps to human chromosome 12p13, and shares 69% homology to mouse TULP3. Human RNA from testis, ovary, thyroid and spinal cord contain highly detectable levels of TULP3 transcripts. In the retina, TULP3 is expressed specifically in the inner nuclear layer and ganglion cell layer. TULP1, TULP2 and TULP3 may comprise a unique family of bipartite transcription factors.

Supplier: Bioss

Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-69 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).

Supplier: Bioss

Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-69 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).

Supplier: Bioss

Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-69 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).

Supplier: Bioss

Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-69 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).

Supplier: Bioss

Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-69 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).

Supplier: Bioss

Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-69 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).