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1-Bromo-2-isopropoxy-3-methoxybenzene
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1-Bromo-2-isopropoxy-3-methoxybenzene
Catalog Number:
(89359-700)
Supplier:
Genetex
Description:
Calnexin, also referred to as IP90, p88 and p90, is an ~90 kDa integral membrane protein of the endoplasmic reticulum (ER). Many resident ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into multisubunit proteins. Studies indicate that calnexin associates with the major histocompatability complex (MHC) class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin, but not with completed receptor complexes. It has been shown that calnexin is a chaperone that retains incompletely or improperly folded proteins in the ER. The sequence Lys-Asp-Glu-Leu (KDEL) or a closely related sequence, is present at the carboxy-terminus of soluble ER resident proteins such as GRP 78 and GRP 94 and protein disulfide isomerase. Integral membrane ER resident proteins, like calnexin, often lack this KDEL sequence but contain positively charged cytosolic residues that ensure ER retention. Calnexin contains a large ER luminal domain (461 amino acids), a transmembrane segment (22 amino acids), and a cytoplasmic tail (89 amino acids).
Catalog Number:
(103010-276)
Supplier:
Anaspec Inc
Description:
Matrix metalloproteinases (MMP’s) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-1 (collagenase-1) is involved in tumor development and metastasis and rheumatoid arthritis. It is proposed as a therapeutic target for these diseases. Native pro-MMP-1 is prepared from culture medium of human rheumatoid synovial fibroblasts. MMP-1 is secreted as pro-enzyme, which consists of a propeptide of 80 amino acids, a catalytic domain of 162 amino acids, a 16-residue linker region, and a hemopexin domain of 189 amino acids. The native pro-MMP-1 has a major Mr 52-kDa unglycosylated and a minor Mr 57-kDa glycosylated form. The proteolytic activation of the 57/52-kDa species will form 47/42-kDa active collagenase, and a 22-kDa C-terminal fragment
The apparent Mr on SDS-PAGE is approximately 56kDa/52 kDa. The pro-MMP-1 can be fully activated by incubating with 1 mM APMA at 37°C for 3 hr. Its activity can be measured by FRET peptides. 10-20 ng of enzyme is sufficient for FRET-based assay
Catalog Number:
(103705-716)
Supplier:
Novus Biologicals
Description:
IL‑28A (Interferon-lambda 2; IFN-lambda 2), IL-28B/IFN-lambda 3, and IL-29/IFN-lambda 1 are type III interferons which are distantly related to IL-10 family and type I IFN family cytokines. Mature human IL-28A is an approximately 22 to 25 kDa protein that shares 66% amino acid sequence identity with mouse and rat IL-28A and shows cross-species activity. It shares 96% and 70% aa sequence identity with human IL-28B and IL-29, respectively.
Catalog Number:
(102970-892)
Supplier:
Lifeline Cell Technology
Description:
Alizarin Red Stains are for calcium deposits, which are indicative of functional osteocytes.
Catalog Number:
(10434-062)
Supplier:
Bioss
Description:
EMP-2 is a 167 amino acid multi-pass membrane protein that contains four-transmembrane domains and belongs to the GAS3/PMP22 (growth arrest-specific-3/peripheral myelin protein-22) family. Localized to lipid raft domains in the plasma membrane, EMP-2 regulates the expression of several target proteins and is necessary for blastocyst implantation in the uterine endometrium. Specifically, EMP-2 mediates blastocyst implantation by controlling the cell membrane expression of MHC and glycosylphosphatidylinositol-anchored proteins, as well as Integrins and caveolin-1. In adult tissues, EMP-2 is expressed in heart, lung, ovary and intestine, while fetal expression is highest in kidney, brain and liver. Overexpression of EMP-2 is associated with endometrial adenocarcinoma, suggesting a possible role for EMP-2 in tumorigenesis.
Supplier:
BeanTown Chemical
Description:
CAS: 25102-12-9; EC No: 217-895-0; MDL No: MFCD00150036
Crystalline/Powder; Molecular Formula: C10H14K2N2O8·2H2O; MW: 404.46
Melting Point: 255-280° (decomposes)
Catalog Number:
(AA42773-AE)
Supplier:
Thermo Scientific Chemicals
Description:
sodium salt, 0.1% w/v Aqueous Solution,UN1170,Liquid,DANGER: FLAMMABLE, causes CNS effects, irritates skin & eyes,100ml.FLAMMABLE LIQUID,
Catalog Number:
(89351-936)
Supplier:
Genetex
Description:
Adenovirus capsid proteins are synthesized in the cytoplasm and transported to the nucleus for assembly into the virus particles. The three major capsid proteins (hexon, penton base, and fiber) are synthesized late in infection. Fiber plays a crucial role in adenovirus infection by attaching the virus to a specific receptor on the cell surface. Ad2 and Ad5 fibers are proposed to consist of three domains: an N-terminal tail that interacts with penton base, a shaft composed of 22 repeats of a 15 amino acid segment that forms beta sheet and beta bends, and a knob at the C terminus that contains the type specific antigen and is responsible for binding to the cell surface receptor. It is shown that the fiber of Ad2 is most likely a trimer when found on the virion.
Catalog Number:
(10668-468)
Supplier:
Bioss
Description:
Tripartite motif-containing protein 3 (TRIM3), also known as RING finger protein 22 (RNF22), RING finger protein 97 (RNF97) or brain-expressed RING finger protein (BERP), is a 744 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Localized to cytoplasmic filaments, TRIM3 has been shown to interact with å-actinin-4 and myosin V, two proteins associated with the actin cytoskeleton. Specifically, å-actinin-4 interacts with the RBCC domain of TRIM3, and the C-terminal tail of Myosin V interacts with with the unique C-terminal ∫-propeller domain of TRIM3. These associations suggest that TRIM3 may play a role in cell motility and cargo transport. Three named isoforms of TRIM3 exist as a result of alternative splicing events.
Catalog Number:
(10672-078)
Supplier:
Bioss
Description:
Tripartite motif-containing protein 3 (TRIM3), also known as RING finger protein 22 (RNF22), RING finger protein 97 (RNF97) or brain-expressed RING finger protein (BERP), is a 744 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Localized to cytoplasmic filaments, TRIM3 has been shown to interact with å-actinin-4 and myosin V, two proteins associated with the actin cytoskeleton. Specifically, å-actinin-4 interacts with the RBCC domain of TRIM3, and the C-terminal tail of Myosin V interacts with with the unique C-terminal ∫-propeller domain of TRIM3. These associations suggest that TRIM3 may play a role in cell motility and cargo transport. Three named isoforms of TRIM3 exist as a result of alternative splicing events.
Catalog Number:
(10434-068)
Supplier:
Bioss
Description:
EMP-2 is a 167 amino acid multi-pass membrane protein that contains four-transmembrane domains and belongs to the GAS3/PMP22 (growth arrest-specific-3/peripheral myelin protein-22) family. Localized to lipid raft domains in the plasma membrane, EMP-2 regulates the expression of several target proteins and is necessary for blastocyst implantation in the uterine endometrium. Specifically, EMP-2 mediates blastocyst implantation by controlling the cell membrane expression of MHC and glycosylphosphatidylinositol-anchored proteins, as well as Integrins and caveolin-1. In adult tissues, EMP-2 is expressed in heart, lung, ovary and intestine, while fetal expression is highest in kidney, brain and liver. Overexpression of EMP-2 is associated with endometrial adenocarcinoma, suggesting a possible role for EMP-2 in tumorigenesis.
Catalog Number:
(76120-460)
Supplier:
Bioss
Description:
Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes lead to severe genetic diseases such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKRD20A (ankyrin repeat domain-containing protein 20A) is an 823 amino acid protein that contains five ANK repeats. The gene encoding ANKRD20A maps to chromosome 9, which consists of about 145 million bases and encodes nearly 900 genes. Considered to play a role in gender determination, deletion of the distal portion of 9p can lead to development of male to female sex reversal, the phenotype of a female with a male X,Y genotype. Hereditary hemorrhagic telangiectasia, which is characterized by harmful vascular defects, and familial dysautonomia are associated with chromosome 9. Also, chromosome 9 is partnered with chromosome 22 in the translocation leading to the aberrant production of BCR-ABL fusion protein often found in leukemias.
Catalog Number:
(10434-046)
Supplier:
Bioss
Description:
EMP-2 is a 167 amino acid multi-pass membrane protein that contains four-transmembrane domains and belongs to the GAS3/PMP22 (growth arrest-specific-3/peripheral myelin protein-22) family. Localized to lipid raft domains in the plasma membrane, EMP-2 regulates the expression of several target proteins and is necessary for blastocyst implantation in the uterine endometrium. Specifically, EMP-2 mediates blastocyst implantation by controlling the cell membrane expression of MHC and glycosylphosphatidylinositol-anchored proteins, as well as Integrins and caveolin-1. In adult tissues, EMP-2 is expressed in heart, lung, ovary and intestine, while fetal expression is highest in kidney, brain and liver. Overexpression of EMP-2 is associated with endometrial adenocarcinoma, suggesting a possible role for EMP-2 in tumorigenesis.
Catalog Number:
(10668-462)
Supplier:
Bioss
Description:
Tripartite motif-containing protein 3 (TRIM3), also known as RING finger protein 22 (RNF22), RING finger protein 97 (RNF97) or brain-expressed RING finger protein (BERP), is a 744 amino acid member of the TRIM family, also known as the RING-B-box coiled-coil (RBCC) family. Members of the RBCC family have an N-terminal RING finger, followed by one or two zinc-binding domains (B-box domains), a leucine coiled-coil region and a variable C-terminal domain. Localized to cytoplasmic filaments, TRIM3 has been shown to interact with å-actinin-4 and myosin V, two proteins associated with the actin cytoskeleton. Specifically, å-actinin-4 interacts with the RBCC domain of TRIM3, and the C-terminal tail of Myosin V interacts with with the unique C-terminal ∫-propeller domain of TRIM3. These associations suggest that TRIM3 may play a role in cell motility and cargo transport. Three named isoforms of TRIM3 exist as a result of alternative splicing events.
Supplier:
BeanTown Chemical
Description:
CAS: 5437-45-6; EC No: 226-611-4; MDL No: MFCD00000190; RTECS: AF5957215
Liquid; Linear Formula: C6H5CH2CO2CH2Br ; Molecular Formula: C9H9BrO2; MW: 229.07
Boiling Point: 166-170°/22 mmHg; Flash point: <gt/>110°C (<gt/>230°F)
Density (g/mL): 1.446; Refractive Index: 1.544
Catalog Number:
(10434-060)
Supplier:
Bioss
Description:
EMP-2 is a 167 amino acid multi-pass membrane protein that contains four-transmembrane domains and belongs to the GAS3/PMP22 (growth arrest-specific-3/peripheral myelin protein-22) family. Localized to lipid raft domains in the plasma membrane, EMP-2 regulates the expression of several target proteins and is necessary for blastocyst implantation in the uterine endometrium. Specifically, EMP-2 mediates blastocyst implantation by controlling the cell membrane expression of MHC and glycosylphosphatidylinositol-anchored proteins, as well as Integrins and caveolin-1. In adult tissues, EMP-2 is expressed in heart, lung, ovary and intestine, while fetal expression is highest in kidney, brain and liver. Overexpression of EMP-2 is associated with endometrial adenocarcinoma, suggesting a possible role for EMP-2 in tumorigenesis.
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