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Catalog Number: (BOSSBS-10320R-HRP)
Supplier: Bioss
Description: Hemagglutinin (HA) is a class I viral fusion protein from Influenza virus. It is a major glycoprotein, comprising over 80% of the envelope proteins present in the virus particle. HA binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell, and is responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. The extent of infection into host organism is determined by HA. In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoproteases secreted by the bronchial epithelial cells. The HA protein is a homotrimer of disulfide-linked HA1-HA2. It also plays a major role in the determination of host range restriction and virulence. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10320R-A488)
Supplier: Bioss
Description: Hemagglutinin (HA) is a class I viral fusion protein from Influenza virus. It is a major glycoprotein, comprising over 80% of the envelope proteins present in the virus particle. HA binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell, and is responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. The extent of infection into host organism is determined by HA. In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoproteases secreted by the bronchial epithelial cells. The HA protein is a homotrimer of disulfide-linked HA1-HA2. It also plays a major role in the determination of host range restriction and virulence. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13168R-A555)
Supplier: Bioss
Description: Fc (Ig constant fragment) receptors ensure protection of the host against foreign antigens, such as microorganisms and pathogens, by removing Ig-coated antigen complexes from circulation. Fc receptors are present on lymphoid and myeloid derivatives, where they mediate endocytosis of Ig-antigen complexes, antibody production in B cells through T cell antigen presentation, cytotoxicity and the release of cytokines and reactive oxygen species. The Fc γ-binding protein (FCGBP) interacts with the Fc portion of IgG and MUC2 to mediate the maintenance of the mucosal structure. FCGBP is a 5,405 amino acid protein that contains twelve TIL (trypsin inhibitory-like) domains and thirteen VWFD domains. It is predominantly expressed in placenta and colon epithelium as well as in thyroid and serum. Patients with various autoimmune diseases seemingly have higher levels of FCGBP protein present in their serum.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10320R-CY7)
Supplier: Bioss
Description: Hemagglutinin (HA) is a class I viral fusion protein from Influenza virus. It is a major glycoprotein, comprising over 80% of the envelope proteins present in the virus particle. HA binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell, and is responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. The extent of infection into host organism is determined by HA. In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoproteases secreted by the bronchial epithelial cells. The HA protein is a homotrimer of disulfide-linked HA1-HA2. It also plays a major role in the determination of host range restriction and virulence. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains.
UOM: 1 * 100 µl


Supplier: Biotium
Description: This MAb recognizes a protein of ~17 kDa, identified as CELA3B (Chymotrypsin like elastase family member 3B). Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, elastase 3B has little elastolytic activity. Like most of the human elastases, elastase 3B is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein; it has a digestive function in the intestine. Elastase 3B preferentially cleaves proteins after alanine residues. Elastase 3B may also function in the intestinal transport and metabolism of cholesterol. Both elastase 3A and elastase 3B have been referred to as protease E and as elastase 1, and excretion of this protein in fecal material is frequently used as a measure of pancreatic function in clinical assays.

Supplier: Biotium
Description: This MAb recognizes a protein of ~17 kDa, identified as CELA3B (Chymotrypsin like elastase family member 3B). Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, elastase 3B has little elastolytic activity. Like most of the human elastases, elastase 3B is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein; it has a digestive function in the intestine. Elastase 3B preferentially cleaves proteins after alanine residues. Elastase 3B may also function in the intestinal transport and metabolism of cholesterol. Both elastase 3A and elastase 3B have been referred to as protease E and as elastase 1, and excretion of this protein in fecal material is frequently used as a measure of pancreatic function in clinical assays.

Catalog Number: (BOSSBS-0423R-CY5.5)
Supplier: Bioss
Description: Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28kD proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18kD active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.
UOM: 1 * 100 µl


Catalog Number: (BNUM1218-50)
Supplier: Biotium
Description: This MAb recognizes a protein of ~17 kDa, identified as CELA3B (Chymotrypsin like elastase family member 3B). Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, elastase 3B has little elastolytic activity. Like most of the human elastases, elastase 3B is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein; it has a digestive function in the intestine. Elastase 3B preferentially cleaves proteins after alanine residues. Elastase 3B may also function in the intestinal transport and metabolism of cholesterol. Both elastase 3A and elastase 3B have been referred to as protease E and as elastase 1, and excretion of this protein in fecal material is frequently used as a measure of pancreatic function in clinical assays.
UOM: 1 * 50 µl


Supplier: Biotium
Description: This MAb recognizes a protein of ~17 kDa, identified as CELA3B (Chymotrypsin like elastase family member 3B). Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, elastase 3B has little elastolytic activity. Like most of the human elastases, elastase 3B is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein; it has a digestive function in the intestine. Elastase 3B preferentially cleaves proteins after alanine residues. Elastase 3B may also function in the intestinal transport and metabolism of cholesterol. Both elastase 3A and elastase 3B have been referred to as protease E and as elastase 1, and excretion of this protein in fecal material is frequently used as a measure of pancreatic function in clinical assays.

Catalog Number: (BOSSBS-13168R)
Supplier: Bioss
Description: Fc (Ig constant fragment) receptors ensure protection of the host against foreign antigens, such as microorganisms and pathogens, by removing Ig-coated antigen complexes from circulation. Fc receptors are present on lymphoid and myeloid derivatives, where they mediate endocytosis of Ig-antigen complexes, antibody production in B cells through T cell antigen presentation, cytotoxicity and the release of cytokines and reactive oxygen species. The Fc γ-binding protein (FCGBP) interacts with the Fc portion of IgG and MUC2 to mediate the maintenance of the mucosal structure. FCGBP is a 5,405 amino acid protein that contains twelve TIL (trypsin inhibitory-like) domains and thirteen VWFD domains. It is predominantly expressed in placenta and colon epithelium as well as in thyroid and serum. Patients with various autoimmune diseases seemingly have higher levels of FCGBP protein present in their serum.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13168R-A488)
Supplier: Bioss
Description: Fc (Ig constant fragment) receptors ensure protection of the host against foreign antigens, such as microorganisms and pathogens, by removing Ig-coated antigen complexes from circulation. Fc receptors are present on lymphoid and myeloid derivatives, where they mediate endocytosis of Ig-antigen complexes, antibody production in B cells through T cell antigen presentation, cytotoxicity and the release of cytokines and reactive oxygen species. The Fc γ-binding protein (FCGBP) interacts with the Fc portion of IgG and MUC2 to mediate the maintenance of the mucosal structure. FCGBP is a 5,405 amino acid protein that contains twelve TIL (trypsin inhibitory-like) domains and thirteen VWFD domains. It is predominantly expressed in placenta and colon epithelium as well as in thyroid and serum. Patients with various autoimmune diseases seemingly have higher levels of FCGBP protein present in their serum.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-0423R-CY3)
Supplier: Bioss
Description: Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28kD proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18kD active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-0423R-CY7)
Supplier: Bioss
Description: Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28kD proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18kD active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-0423R-CY5)
Supplier: Bioss
Description: Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28kD proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18kD active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-0423R-A488)
Supplier: Bioss
Description: Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28kD proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18kD active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-10320R-CY5)
Supplier: Bioss
Description: Hemagglutinin (HA) is a class I viral fusion protein from Influenza virus. It is a major glycoprotein, comprising over 80% of the envelope proteins present in the virus particle. HA binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell, and is responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. The extent of infection into host organism is determined by HA. In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoproteases secreted by the bronchial epithelial cells. The HA protein is a homotrimer of disulfide-linked HA1-HA2. It also plays a major role in the determination of host range restriction and virulence. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
-Additional Documentation May be needed to purchase this item. A VWR representative will contact you if needed.
This product has been blocked by your organisation. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
Product(s) marked with this symbol are discontinued - sold till end of stock. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service on +353 1 8822222.
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