27453 Results for: "Biotin-CF®&amp"

Supplier: Biotium

This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with all subclasses of Alpha heavy chain. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Supplier: Biotium

This MAb reacts with the HLA-DRB1 antigen, a member of MHC class II molecules. It does not cross react with HLA-DP and HLA-DQ. It binds a conformational epitope on HLA-DR, which depends on the correct folding of the α/β heterodimer. This MAb has been reported to block mixed lymphocyte reactions. The L243 antibody recognizes a different epitope than the LN3 monoclonal antibody, and these antibodies do not cross-block binding to each other's respective epitopes. HLA-DR is a heterodimeric cell surface glycoprotein comprised of a 36kD alpha (heavy) chain and a 28kD beta (light) chain. It is expressed on B-cells, activated T-cells, monocytes/macrophages, dendritic cells and other non-professional APCs. In conjunction with the CD3/TCR complex and CD4 molecules, HLA-DR is critical for efficient peptide presentation to CD4 T cells. It is an excellent histiocytic marker in paraffin sections producing intense staining. True histiocytic neoplasms are similarly positive. HLA-DR antigens also occur on a variety of epithelial cells and their corresponding neoplastic counterparts.

Supplier: Biotium

This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with both IgA1 and IgA2 subclasses of Alpha heavy chain. It reacts with the third constant domain (CH3) of the alpha chain of IgA molecules. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Supplier: Biotium

This MAb is specific to heavy chain of IgA and shows minimal cross-reaction with heavy chains of other immunoglobulins. It is reactive with all subclasses of Alpha heavy chain. Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through inter-chain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B-cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins.IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces. The most common feature of plasmacytomas, and certain non-Hodgkin's lymphomas is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Supplier: Biotium

Recognizes a protein of ~55 kDa, identified as SOX10. This MAb is highly specific and does not cross-react with other members of the SOX-family. SOX genes comprise a family of genes that are related to the mammalian sex-determining gene SRY. These genes similarly contain sequences that encode for the HMG-box domain, which is responsible for the sequence-specific DNA-binding activity. SOX-10 is a sensitive marker of melanoma, including conventional, spindled, and desmoplastic subtypes. It is expressed by metastatic melanomas and nodal capsular nevus in sentinel lymph nodes, but not by other lymph node components such as dendritic cells, which usually express S100 protein. Commonly used melanoma markers, such as anti-HMB-45 and anti-Melan-A, are poorly expressed in desmoplastic melanomas while SOX-10 is moderately to strongly expressed in desmoplastic melanomas. SOX-10 is considered as a very reliable marker for recognizing residual desmoplastic melanomas. In normal tissues, it is expressed in Schwann cells, melanocytes, and myoepithelial cells of salivary, bronchial and mammary glands. SOX-10 expression is also observed in mast cells.

Supplier: Biotium

Recognizes a protein of ~55 kDa, identified as SOX10. This MAb is highly specific and does not cross-react with other members of the SOX-family. SOX genes comprise a family of genes that are related to the mammalian sex-determining gene SRY. These genes similarly contain sequences that encode for the HMG-box domain, which is responsible for the sequence-specific DNA-binding activity. SOX-10 is a sensitive marker of melanoma, including conventional, spindled, and desmoplastic subtypes. It is expressed by metastatic melanomas and nodal capsular nevus in sentinel lymph nodes, but not by other lymph node components such as dendritic cells, which usually express S100 protein. Commonly used melanoma markers, such as anti-HMB-45 and anti-Melan-A, are poorly expressed in desmoplastic melanomas while SOX-10 is moderately to strongly expressed in desmoplastic melanomas. SOX-10 is considered as a very reliable marker for recognizing residual desmoplastic melanomas. In normal tissues, it is expressed in Schwann cells, melanocytes, and myoepithelial cells of salivary, bronchial and mammary glands. SOX-10 expression is also observed in mast cells.

Supplier: Biotium

Recognizes a protein of ~55 kDa, identified as SOX10. This MAb is highly specific and does not cross-react with other members of the SOX-family. SOX genes comprise a family of genes that are related to the mammalian sex-determining gene SRY. These genes similarly contain sequences that encode for the HMG-box domain, which is responsible for the sequence-specific DNA-binding activity. SOX-10 is a sensitive marker of melanoma, including conventional, spindled, and desmoplastic subtypes. It is expressed by metastatic melanomas and nodal capsular nevus in sentinel lymph nodes, but not by other lymph node components such as dendritic cells, which usually express S100 protein. Commonly used melanoma markers, such as anti-HMB-45 and anti-Melan-A, are poorly expressed in desmoplastic melanomas while SOX-10 is moderately to strongly expressed in desmoplastic melanomas. SOX-10 is considered as a very reliable marker for recognizing residual desmoplastic melanomas. In normal tissues, it is expressed in Schwann cells, melanocytes, and myoepithelial cells of salivary, bronchial and mammary glands. SOX-10 expression is also observed in mast cells.

Supplier: Biotium

This MAb is specific to Complement 4d (C4d) and it reacts with the secreted as well as cell-bound C4d.C4d is a degradation product of the activated complement factor C4b. Complement 4b is typically activated by binding of Abs to specific target molecules. Following activation and degradation of the C4 molecule, thio-ester groups are exposed, which allow transient, covalent binding of the degradation product Complement 4d to endothelial cell surfaces and extracellular matrix components of vascular basement membranes near the sites of C4 activation. The presence of C4d in peritubular capillaries is a key indicator for acute humoral (i.e. antibody-mediated) rejection of kidney, heart, pancreas and lung allografts. As an established marker of antibody-mediated acute renal allograft rejection and its proclivity for endothelium, this component can be detected in peritubular capillaries in chronic renal allograft rejection as well as hyperacute rejection, acute vascular rejection, acute cellular rejection, and borderline rejection. It has been shown to be a significant predictor of transplant kidney graft survival. Anti-C4d, combined with anti-C3d, can be utilized as a tool for diagnosis of allograft rejection that may warrant a prompt and aggressive anti-rejection treatment.

Supplier: Biotium

Recognizes a protein of ~55 kDa, identified as SOX10. This MAb is highly specific and does not cross-react with other members of the SOX-family. SOX genes comprise a family of genes that are related to the mammalian sex-determining gene SRY. These genes similarly contain sequences that encode for the HMG-box domain, which is responsible for the sequence-specific DNA-binding activity. SOX-10 is a sensitive marker of melanoma, including conventional, spindled, and desmoplastic subtypes. It is expressed by metastatic melanomas and nodal capsular nevus in sentinel lymph nodes, but not by other lymph node components such as dendritic cells, which usually express S100 protein. Commonly used melanoma markers, such as anti-HMB-45 and anti-Melan-A, are poorly expressed in desmoplastic melanomas while SOX-10 is moderately to strongly expressed in desmoplastic melanomas. SOX-10 is considered as a very reliable marker for recognizing residual desmoplastic melanomas. In normal tissues, it is expressed in Schwann cells, melanocytes, and myoepithelial cells of salivary, bronchial and mammary glands. SOX-10 expression is also observed in mast cells.

Supplier: Biotium

Recognizes a protein of ~55 kDa, identified as SOX10. This MAb is highly specific and does not cross-react with other members of the SOX-family. SOX genes comprise a family of genes that are related to the mammalian sex-determining gene SRY. These genes similarly contain sequences that encode for the HMG-box domain, which is responsible for the sequence-specific DNA-binding activity. SOX-10 is a sensitive marker of melanoma, including conventional, spindled, and desmoplastic subtypes. It is expressed by metastatic melanomas and nodal capsular nevus in sentinel lymph nodes, but not by other lymph node components such as dendritic cells, which usually express S100 protein. Commonly used melanoma markers, such as anti-HMB-45 and anti-Melan-A, are poorly expressed in desmoplastic melanomas while SOX-10 is moderately to strongly expressed in desmoplastic melanomas. SOX-10 is considered as a very reliable marker for recognizing residual desmoplastic melanomas. In normal tissues, it is expressed in Schwann cells, melanocytes, and myoepithelial cells of salivary, bronchial and mammary glands. SOX-10 expression is also observed in mast cells.

Supplier: Biotium

Recognizes a protein of ~55 kDa, identified as SOX10. This MAb is highly specific and does not cross-react with other members of the SOX-family. SOX genes comprise a family of genes that are related to the mammalian sex-determining gene SRY. These genes similarly contain sequences that encode for the HMG-box domain, which is responsible for the sequence-specific DNA-binding activity. SOX-10 is a sensitive marker of melanoma, including conventional, spindled, and desmoplastic subtypes. It is expressed by metastatic melanomas and nodal capsular nevus in sentinel lymph nodes, but not by other lymph node components such as dendritic cells, which usually express S100 protein. Commonly used melanoma markers, such as anti-HMB-45 and anti-Melan-A, are poorly expressed in desmoplastic melanomas while SOX-10 is moderately to strongly expressed in desmoplastic melanomas. SOX-10 is considered as a very reliable marker for recognizing residual desmoplastic melanomas. In normal tissues, it is expressed in Schwann cells, melanocytes, and myoepithelial cells of salivary, bronchial and mammary glands. SOX-10 expression is also observed in mast cells.

Supplier: Biotium

Recognizes a protein of ~55 kDa, identified as SOX10. This MAb is highly specific and does not cross-react with other members of the SOX-family. SOX genes comprise a family of genes that are related to the mammalian sex-determining gene SRY. These genes similarly contain sequences that encode for the HMG-box domain, which is responsible for the sequence-specific DNA-binding activity. SOX-10 is a sensitive marker of melanoma, including conventional, spindled, and desmoplastic subtypes. It is expressed by metastatic melanomas and nodal capsular nevus in sentinel lymph nodes, but not by other lymph node components such as dendritic cells, which usually express S100 protein. Commonly used melanoma markers, such as anti-HMB-45 and anti-Melan-A, are poorly expressed in desmoplastic melanomas while SOX-10 is moderately to strongly expressed in desmoplastic melanomas. SOX-10 is considered as a very reliable marker for recognizing residual desmoplastic melanomas. In normal tissues, it is expressed in Schwann cells, melanocytes, and myoepithelial cells of salivary, bronchial and mammary glands. SOX-10 expression is also observed in mast cells.

Supplier: Biotium

Recognizes an 85-115 kDa protein (variation with cell type), identified as intercellular adhesion molecule (ICAM-1) (Workshop IV). It has 7 potential N-linked glycosylation sites. ICAM-1 is a single chain glycoprotein of Ig supergene family, present on unstimulated endothelial cells (EC) and on a variety of other cell types including activated fibroblasts, EC, macrophages, and lymphocytes. ICAM-1 mediates cell adhesion by binding to integrins CD11a/CD18 (leukocyte adhesion molecule, LFA-1) and to CD11b/CD18 (Mac-1). This interaction enhances antigen-specific T-cell activation. ICAM-1 also binds to CD43 and to Plasmodium falciparum infected RBCs. W-CAM-1 MAb blocks aggregation of cell lines mediated by the ICAM-1 and blocks homotypic binding of purified populations of activated T- and B-lymphocytes and also aggregation of mixed T- and B-cell blasts. It inhibits T-cell adhesion to normal human endothelial cells. Activation induced by cell-cell contact (mixed lymphocyte reaction, T-cell mediated B-cell activation) is significantly inhibited. This MAb blocks elements of both effector arms of immune system (cytotoxic cell function and Ig production).

Supplier: Biotium

The family of EF-hand type Ca2 -binding proteins includes calbindin, S-100 alpha and beta, calgranulins, B and C, and the parvalbumin family members, including parvalbumin alpha and parvalbumin beta. The S-100 protein is involved in the regulation of cellular processes such as cell cycle progression and differentiation. S-100 protein may function in the activation of Ca2 induced Ca2 release, inhibition of microtubule assembly and inhibition of protein kinase C mediated phosphorylation. Two S-100 subunits, sharing 60% sequence identity, have been described as S-100 alpha chain and S-100 beta chain. Three S-100 dimeric forms have been characterized, differing in their subunit composition of two alpha chains, two beta chains or one alpha and one beta chain. S-100 localizes to the cytoplasm and nuclei of astrocytes, Schwann s cells, ependymomas and astrogliomas. S-100 is also detected in almost all benign naevi, malignant melanocytic tumours and in Langerhans cells in the skin. Calbindin, S-100 proteins and parvalbumin proteins are each expressed in neural tissues. In addition, S-100 alpha and beta are present in a variety of other tissues and calbindin is present in intestine and kidney.

Supplier: Biotium

This MAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, PML and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Biotium

This MAb is specific to Complement 4d (C4d) and it reacts with the secreted as well as cell-bound C4d.C4d is a degradation product of the activated complement factor C4b. Complement 4b is typically activated by binding of Abs to specific target molecules. Following activation and degradation of the C4 molecule, thio-ester groups are exposed, which allow transient, covalent binding of the degradation product Complement 4d to endothelial cell surfaces and extracellular matrix components of vascular basement membranes near the sites of C4 activation. The presence of C4d in peritubular capillaries is a key indicator for acute humoral (i.e. antibody-mediated) rejection of kidney, heart, pancreas and lung allografts. As an established marker of antibody-mediated acute renal allograft rejection and its proclivity for endothelium, this component can be detected in peritubular capillaries in chronic renal allograft rejection as well as hyperacute rejection, acute vascular rejection, acute cellular rejection, and borderline rejection. It has been shown to be a significant predictor of transplant kidney graft survival. Anti-C4d, combined with anti-C3d, can be utilized as a tool for diagnosis of allograft rejection that may warrant a prompt and aggressive anti-rejection treatment.

Supplier: Biotium

This MAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, PML and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Biotium

Recognizes the L1 or Calprotectin molecule, an intra-cytoplasmic antigen comprising of a 12 kDa alpha chain and a 14 kDa beta chain expressed by granulocytes, monocytes and by tissue macrophages. Macrophages usually arise from hematopoietic stem cells in the bone marrow. Under migration into tissues, the monocytes undergo further differentiation to become multifunctional tissue macrophages. They are classified into normal and inflammatory macrophages. Normal macrophages include macrophages in connective tissue (histiocytes), liver (Kupffer's cells), lung (alveolar macrophages), lymph nodes (free and fixed macrophages), spleen (free and fixed macrophages), bone marrow (fixed macrophages), serous fluids (pleural and peritoneal macrophages), skin (histiocytes, Langerhans's cell) and in other tissues. Inflammatory macrophages are present in various exudates. Macrophages are part of the innate immune system, recognizing, engulfing and destroying many potential pathogens including bacteria, pathogenic protozoa, fungi and helminthes. This MAb reacts with neutrophils, monocytes, macrophages, and squamous mucosal epithelia and has been shown as an important marker for identifying macrophages in tissue sections.

Supplier: Biotium

This MAb reacts with MUC1. The dominant epitope of this MAb has not yet been determined. MUC1 is a large cell surface mucin glycoprotein expressed by most glandular and ductal epithelial cells and some hematopoietic cell lineages. It is expressed on most secretory epithelium, including mammary gland and some hematopoietic cells. It is expressed abundantly in lactating mammary glands and over expressed abundantly in >90% breast carcinomas and metastases. Transgenic MUC1 has been shown to associate with all four c-erbB receptors and localize with c-erbB1 (EGFR) in lactating glands. The MUC1 gene contains seven exons and produces several different alternatively spliced variants. The major expressed form of MUC1 uses all seven exons and is a type 1 transmembrane protein with a large extracellular tandem repeat domain. The tandem repeat domain is highly O glycosylated and alterations in glycosylation have been shown in epithelial cancer cells. Antibody to EMA is useful as a pan-epithelial marker for detecting early metastatic loci of carcinoma in bone marrow or liver.

Supplier: Biotium

This MAb reacts with MUC1. The dominant epitope of this MAb has not yet been determined. MUC1 is a large cell surface mucin glycoprotein expressed by most glandular and ductal epithelial cells and some hematopoietic cell lineages. It is expressed on most secretory epithelium, including mammary gland and some hematopoietic cells. It is expressed abundantly in lactating mammary glands and over expressed abundantly in >90% breast carcinomas and metastases. Transgenic MUC1 has been shown to associate with all four c-erbB receptors and localize with c-erbB1 (EGFR) in lactating glands. The MUC1 gene contains seven exons and produces several different alternatively spliced variants. The major expressed form of MUC1 uses all seven exons and is a type 1 transmembrane protein with a large extracellular tandem repeat domain. The tandem repeat domain is highly O glycosylated and alterations in glycosylation have been shown in epithelial cancer cells. Antibody to EMA is useful as a pan-epithelial marker for detecting early metastatic loci of carcinoma in bone marrow or liver.

Supplier: Biotium

The family of EF-hand type Ca2 -binding proteins includes calbindin, S-100 alpha and beta, calgranulins, B and C, and the parvalbumin family members, including parvalbumin alpha and parvalbumin beta. The S-100 protein is involved in the regulation of cellular processes such as cell cycle progression and differentiation. S-100 protein may function in the activation of Ca2 induced Ca2 release, inhibition of microtubule assembly and inhibition of protein kinase C mediated phosphorylation. Two S-100 subunits, sharing 60% sequence identity, have been described as S-100 alpha chain and S-100 beta chain. Three S-100 dimeric forms have been characterized, differing in their subunit composition of two alpha chains, two beta chains or one alpha and one beta chain. S-100 localizes to the cytoplasm and nuclei of astrocytes, Schwann s cells, ependymomas and astrogliomas. S-100 is also detected in almost all benign naevi, malignant melanocytic tumours and in Langerhans cells in the skin. Calbindin, S-100 proteins and parvalbumin proteins are each expressed in neural tissues. In addition, S-100 alpha and beta are present in a variety of other tissues and calbindin is present in intestine and kidney.

Supplier: Biotium

This MAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, PML and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Biotium

This MAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, PML and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Biotium

This MAb reacts with both SUMO-2 and SUMO-3. The small ubiquitin-related modifier (SUMO) proteins, which include SUMO-1, 2 and 3, belong to the ubiquitin-like protein family. Like ubiquitin, the SUMO proteins are synthesized as precursor proteins that undergo processing before conjugation to target proteins. Also, both utilize the E1, E2 and E3 cascade enzymes for conjugation. However, SUMO and ubiquitin differ with respect to targeting. Ubiquitination predominantly targets proteins for degradation, whereas sumoylation targets proteins to a variety of cellular processing, including nuclear transport, transcriptional regulation, apoptosis and protein stability. The unconjugated SUMO-1, 2 and 3 proteins localize to the nuclear membrane, nuclear bodies and cytoplasm, respectively. SUMO-1 utilizes Ubc9 for conjugation to several target proteins, which include MDM2, p53, PML and RanGap1. SUMO-2 and 3 contribute to a greater percentage of protein modification than does SUMO-1 and unlike SUMO-1, they can form polymeric chains. In addition, SUMO-3 regulates beta-Amyloid generation and may be critical in the onset or progression of Alzheimer’s disease.

Supplier: Biotium

This MAb is specific to Complement 4d (C4d) and it reacts with the secreted as well as cell-bound C4d.C4d is a degradation product of the activated complement factor C4b. Complement 4b is typically activated by binding of Abs to specific target molecules. Following activation and degradation of the C4 molecule, thio-ester groups are exposed, which allow transient, covalent binding of the degradation product Complement 4d to endothelial cell surfaces and extracellular matrix components of vascular basement membranes near the sites of C4 activation. The presence of C4d in peritubular capillaries is a key indicator for acute humoral (i.e. antibody-mediated) rejection of kidney, heart, pancreas and lung allografts. As an established marker of antibody-mediated acute renal allograft rejection and its proclivity for endothelium, this component can be detected in peritubular capillaries in chronic renal allograft rejection as well as hyperacute rejection, acute vascular rejection, acute cellular rejection, and borderline rejection. It has been shown to be a significant predictor of transplant kidney graft survival. Anti-C4d, combined with anti-C3d, can be utilized as a tool for diagnosis of allograft rejection that may warrant a prompt and aggressive anti-rejection treatment.

Supplier: Biotium

This MAb is specific to Complement 4d (C4d) and it reacts with the secreted as well as cell-bound C4d.C4d is a degradation product of the activated complement factor C4b. Complement 4b is typically activated by binding of Abs to specific target molecules. Following activation and degradation of the C4 molecule, thio-ester groups are exposed, which allow transient, covalent binding of the degradation product Complement 4d to endothelial cell surfaces and extracellular matrix components of vascular basement membranes near the sites of C4 activation. The presence of C4d in peritubular capillaries is a key indicator for acute humoral (i.e. antibody-mediated) rejection of kidney, heart, pancreas and lung allografts. As an established marker of antibody-mediated acute renal allograft rejection and its proclivity for endothelium, this component can be detected in peritubular capillaries in chronic renal allograft rejection as well as hyperacute rejection, acute vascular rejection, acute cellular rejection, and borderline rejection. It has been shown to be a significant predictor of transplant kidney graft survival. Anti-C4d, combined with anti-C3d, can be utilized as a tool for diagnosis of allograft rejection that may warrant a prompt and aggressive anti-rejection treatment.

Supplier: Biotium

This MAb is specific to Complement 4d (C4d) and it reacts with the secreted as well as cell-bound C4d.C4d is a degradation product of the activated complement factor C4b. Complement 4b is typically activated by binding of Abs to specific target molecules. Following activation and degradation of the C4 molecule, thio-ester groups are exposed, which allow transient, covalent binding of the degradation product Complement 4d to endothelial cell surfaces and extracellular matrix components of vascular basement membranes near the sites of C4 activation. The presence of C4d in peritubular capillaries is a key indicator for acute humoral (i.e. antibody-mediated) rejection of kidney, heart, pancreas and lung allografts. As an established marker of antibody-mediated acute renal allograft rejection and its proclivity for endothelium, this component can be detected in peritubular capillaries in chronic renal allograft rejection as well as hyperacute rejection, acute vascular rejection, acute cellular rejection, and borderline rejection. It has been shown to be a significant predictor of transplant kidney graft survival. Anti-C4d, combined with anti-C3d, can be utilized as a tool for diagnosis of allograft rejection that may warrant a prompt and aggressive anti-rejection treatment.

Supplier: Biotium

This MAb is specific to Complement 4d (C4d) and it reacts with the secreted as well as cell-bound C4d.C4d is a degradation product of the activated complement factor C4b. Complement 4b is typically activated by binding of Abs to specific target molecules. Following activation and degradation of the C4 molecule, thio-ester groups are exposed, which allow transient, covalent binding of the degradation product Complement 4d to endothelial cell surfaces and extracellular matrix components of vascular basement membranes near the sites of C4 activation. The presence of C4d in peritubular capillaries is a key indicator for acute humoral (i.e. antibody-mediated) rejection of kidney, heart, pancreas and lung allografts. As an established marker of antibody-mediated acute renal allograft rejection and its proclivity for endothelium, this component can be detected in peritubular capillaries in chronic renal allograft rejection as well as hyperacute rejection, acute vascular rejection, acute cellular rejection, and borderline rejection. It has been shown to be a significant predictor of transplant kidney graft survival. Anti-C4d, combined with anti-C3d, can be utilized as a tool for diagnosis of allograft rejection that may warrant a prompt and aggressive anti-rejection treatment.

Supplier: Biotium

Recognizes a protein of ~55 kDa, identified as SOX10. This MAb is highly specific and does not cross-react with other members of the SOX-family. SOX genes comprise a family of genes that are related to the mammalian sex-determining gene SRY. These genes similarly contain sequences that encode for the HMG-box domain, which is responsible for the sequence-specific DNA-binding activity. SOX-10 is a sensitive marker of melanoma, including conventional, spindled, and desmoplastic subtypes. It is expressed by metastatic melanomas and nodal capsular nevus in sentinel lymph nodes, but not by other lymph node components such as dendritic cells, which usually express S100 protein. Commonly used melanoma markers, such as anti-HMB-45 and anti-Melan-A, are poorly expressed in desmoplastic melanomas while SOX-10 is moderately to strongly expressed in desmoplastic melanomas. SOX-10 is considered as a very reliable marker for recognizing residual desmoplastic melanomas. In normal tissues, it is expressed in Schwann cells, melanocytes, and myoepithelial cells of salivary, bronchial and mammary glands. SOX-10 expression is also observed in mast cells.

Supplier: Biotium

Recognizes a protein of 57 kDa, identified as p57Kip2. It shows no cross-reaction with p27Kip1. p57Kip2 is a potent tight-binding inhibitor of several G1 cyclin complexes, and is a negative regulator of cell proliferation. Anti-p57 has been used as an aide in identification of complete hydatidiform mole (CHM) (no nuclear labeling of cytotrophoblasts and stromal cells) from partial hydatidiform mole (PHM) in which both cytotrophoblasts and stromal cells stain. The histological differentiation of complete mole, partial mole, and hydropic spontaneous abortion is problematic. Most complete hydatidiform moles are diploid, whereas most partial moles are triploid. Ploidy studies will identify partial moles, but will not differentiate complete moles from non-molar gestations. Complete moles carry a high risk of persistent disease and choriocarcinoma, while partial moles have a very low risk. In normal placenta, many cytotrophoblast nuclei and stromal cells are labeled with this antibody. Similar findings apply to PHM and hydropic abortus tissues. Intervillous trophoblastic islands (IVTIs) demonstrate nuclear labeling in all three entities and serve as an internal control.