You Searched For: Resazurin+sodium+salt

Catalog Number: (BOSSBS-9006R-A350)

Supplier: Bioss

Description: Adenosine deaminase is an enzyme that is present in most tissues and exists predominantly as a monomer, although in some tissues it is associated with adenosine deaminase-binding protein. Adenosine deaminase degrades extracellular adenosine, which is toxic for lymphocytes. A novel family of growth factors that share sequence similarity to adenosine deaminase has been identified. The cat eye syndrome critical region protein (CECR) family includes CECR1, CECR2, CECR3, CECR4, CECR5, CECR6, CECR7, CECR8 and CECR9. The genes encoding CECR proteins are candidates for Cat Eye Syndrome (CES), a developmental disorder associated with the duplication of a 2 Mb region of 22q11.2. CES is characterized by the combination of coloboma of the iris and anal atresia with fistula, downslanting palpebral fissures, preauricular tags and/or pits, frequent occurrence of heart and renal malformations, and normal or near-normal mental development. CECR family members are widely expressed. Specifically, CECR1 has the highest expression in adult heart, lung, lymphoblasts and placenta. CECR2 is also involved in neurulation and chromatin remodeling. Mutations in the CECR2 gene result in neural tube defects.

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Catalog Number: (BOSSBS-9006R-A647)

Supplier: Bioss

Description: Adenosine deaminase is an enzyme that is present in most tissues and exists predominantly as a monomer, although in some tissues it is associated with adenosine deaminase-binding protein. Adenosine deaminase degrades extracellular adenosine, which is toxic for lymphocytes. A novel family of growth factors that share sequence similarity to adenosine deaminase has been identified. The cat eye syndrome critical region protein (CECR) family includes CECR1, CECR2, CECR3, CECR4, CECR5, CECR6, CECR7, CECR8 and CECR9. The genes encoding CECR proteins are candidates for Cat Eye Syndrome (CES), a developmental disorder associated with the duplication of a 2 Mb region of 22q11.2. CES is characterized by the combination of coloboma of the iris and anal atresia with fistula, downslanting palpebral fissures, preauricular tags and/or pits, frequent occurrence of heart and renal malformations, and normal or near-normal mental development. CECR family members are widely expressed. Specifically, CECR1 has the highest expression in adult heart, lung, lymphoblasts and placenta. CECR2 is also involved in neurulation and chromatin remodeling. Mutations in the CECR2 gene result in neural tube defects.

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Catalog Number: (BOSSBS-10493R-CY5)

Supplier: Bioss

Description: Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi. Multiple alternatively spliced transcript variants that encode the same proteins have been identified.[provided by RefSeq, Sep 2008].

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Catalog Number: (BOSSBS-11871R-A647)

Supplier: Bioss

Description: LIMK 1 and 2 likely regulate aspects of the cytoskeleton, through control of the organization of actin filaments. They can phosphorylate an actin-binding protein, cofilin which binds to actin monomers and polymers and promotes the disassembly of actin filament.The phosphorylation of cofilin via LIMK inactivates this potential. LIMK1 is highly active in the brain and spinal chord, where it is believed to be involved in the development of nerve cells whilst LIMK2 is ubiquitously expressed in many adult tissues. LIMK1 may play an important role in areas of the brain that are responsible for processing visual-spatial information (visuospatial constructive cognition). These parts of the brain are important for visualizing an object as a set of parts and performing tasks such as writing, drawing, constructing models, and assembling puzzles. LIMK1 is specifically stimulated by Rac, one of the Rho family proteins, while LIMK2 activity is activated under the control of other Rho family members, Rho and Cdc42, suggesting that two distinct pathways exist in the Rho family driven actin cytoskeleton dynamics.

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Catalog Number: (BOSSBS-6216R-A647)

Supplier: Bioss

Description: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity (By similarity)

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Supplier: ENZO LIFE SCIENCES

Description: Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.

Catalog Number: (BOSSBS-5808R-CY3)

Supplier: Bioss

Description: CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. 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.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

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Catalog Number: (BOSSBS-5808R-A647)

Supplier: Bioss

Description: CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. 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.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.

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Supplier: Biotium

Description: MAb 2H11 reacts with a partially defined epitope of human thyroglobulin. This epitope is different form the epitope recognized by MAb 6E1. Thyroglobulin is a 660 kDa dimeric pre-protein with mutiple glycosylation sites. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for anti-thyroglobulin even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently anti-thyroglobulin negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Anti-thyroglobulin, combined with anti-calcitonin, can identify medullary carcinomas of the thyroid. Furthermore, anti-thyroglobulin, combined with anti-TTF1, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.

Supplier: Biotium

Description: MAb 2H11 reacts with a partially defined epitope of human thyroglobulin. This epitope is different form the epitope recognized by MAb 6E1. Thyroglobulin is a 660 kDa dimeric pre-protein with mutiple glycosylation sites. It is produced by and processed within the thyroid gland to produce the hormone thyroxine and triiodothyronine. Prior to forming dimers, thyroglobulin monomers undergo conformational maturation in the endoplasmic reticulation. The vast majority of follicular carcinomas of the thyroid will give positive immunoreactivity for anti-thyroglobulin even though sometimes only focally. Poorly differentiated carcinomas of the thyroid are frequently anti-thyroglobulin negative. Adenocarcinomas of other-than-thyroid origin do not react with this antibody. This antibody is useful in identification of thyroid carcinoma of the papillary and follicular types. Presence of thyroglobulin in metastatic lesions establishes the thyroid origin of tumor. Anti-thyroglobulin, combined with anti-calcitonin, can identify medullary carcinomas of the thyroid. Furthermore, anti-thyroglobulin, combined with anti-TTF1, can be a reliable marker to differentiate between primary thyroid and lung neoplasms.

Catalog Number: (BOSSBS-11871R-FITC)

Supplier: Bioss

Description: LIMK 1 and 2 likely regulate aspects of the cytoskeleton, through control of the organization of actin filaments. They can phosphorylate an actin-binding protein, cofilin which binds to actin monomers and polymers and promotes the disassembly of actin filament.The phosphorylation of cofilin via LIMK inactivates this potential. LIMK1 is highly active in the brain and spinal chord, where it is believed to be involved in the development of nerve cells whilst LIMK2 is ubiquitously expressed in many adult tissues. LIMK1 may play an important role in areas of the brain that are responsible for processing visual-spatial information (visuospatial constructive cognition). These parts of the brain are important for visualizing an object as a set of parts and performing tasks such as writing, drawing, constructing models, and assembling puzzles. LIMK1 is specifically stimulated by Rac, one of the Rho family proteins, while LIMK2 activity is activated under the control of other Rho family members, Rho and Cdc42, suggesting that two distinct pathways exist in the Rho family driven actin cytoskeleton dynamics.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11871R-A488)

Supplier: Bioss

Description: LIMK 1 and 2 likely regulate aspects of the cytoskeleton, through control of the organization of actin filaments. They can phosphorylate an actin-binding protein, cofilin which binds to actin monomers and polymers and promotes the disassembly of actin filament.The phosphorylation of cofilin via LIMK inactivates this potential. LIMK1 is highly active in the brain and spinal chord, where it is believed to be involved in the development of nerve cells whilst LIMK2 is ubiquitously expressed in many adult tissues. LIMK1 may play an important role in areas of the brain that are responsible for processing visual-spatial information (visuospatial constructive cognition). These parts of the brain are important for visualizing an object as a set of parts and performing tasks such as writing, drawing, constructing models, and assembling puzzles. LIMK1 is specifically stimulated by Rac, one of the Rho family proteins, while LIMK2 activity is activated under the control of other Rho family members, Rho and Cdc42, suggesting that two distinct pathways exist in the Rho family driven actin cytoskeleton dynamics.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11871R-HRP)

Supplier: Bioss

Description: LIMK 1 and 2 likely regulate aspects of the cytoskeleton, through control of the organization of actin filaments. They can phosphorylate an actin-binding protein, cofilin which binds to actin monomers and polymers and promotes the disassembly of actin filament.The phosphorylation of cofilin via LIMK inactivates this potential. LIMK1 is highly active in the brain and spinal chord, where it is believed to be involved in the development of nerve cells whilst LIMK2 is ubiquitously expressed in many adult tissues. LIMK1 may play an important role in areas of the brain that are responsible for processing visual-spatial information (visuospatial constructive cognition). These parts of the brain are important for visualizing an object as a set of parts and performing tasks such as writing, drawing, constructing models, and assembling puzzles. LIMK1 is specifically stimulated by Rac, one of the Rho family proteins, while LIMK2 activity is activated under the control of other Rho family members, Rho and Cdc42, suggesting that two distinct pathways exist in the Rho family driven actin cytoskeleton dynamics.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11871R-A750)

Supplier: Bioss

Description: LIMK 1 and 2 likely regulate aspects of the cytoskeleton, through control of the organization of actin filaments. They can phosphorylate an actin-binding protein, cofilin which binds to actin monomers and polymers and promotes the disassembly of actin filament. The phosphorylation of cofilin via LIMK inactivates this potential. LIMK1 is highly active in the brain and spinal chord, where it is believed to be involved in the development of nerve cells whilst LIMK2 is ubiquitously expressed in many adult tissues. LIMK1 may play an important role in areas of the brain that are responsible for processing visual-spatial information (visuospatial constructive cognition). These parts of the brain are important for visualizing an object as a set of parts and performing tasks such as writing, drawing, constructing models, and assembling puzzles. LIMK1 is specifically stimulated by Rac, one of the Rho family proteins, while LIMK2 activity is activated under the control of other Rho family members, Rho and Cdc42, suggesting that two distinct pathways exist in the Rho family driven actin cytoskeleton dynamics.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11871R-A350)

Supplier: Bioss

Description: LIMK 1 and 2 likely regulate aspects of the cytoskeleton, through control of the organization of actin filaments. They can phosphorylate an actin-binding protein, cofilin which binds to actin monomers and polymers and promotes the disassembly of actin filament.The phosphorylation of cofilin via LIMK inactivates this potential. LIMK1 is highly active in the brain and spinal chord, where it is believed to be involved in the development of nerve cells whilst LIMK2 is ubiquitously expressed in many adult tissues. LIMK1 may play an important role in areas of the brain that are responsible for processing visual-spatial information (visuospatial constructive cognition). These parts of the brain are important for visualizing an object as a set of parts and performing tasks such as writing, drawing, constructing models, and assembling puzzles. LIMK1 is specifically stimulated by Rac, one of the Rho family proteins, while LIMK2 activity is activated under the control of other Rho family members, Rho and Cdc42, suggesting that two distinct pathways exist in the Rho family driven actin cytoskeleton dynamics.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3800R-CY5)

Supplier: Bioss

Description: Immunoglobulins belong to a group of related glyco proteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately 110 amino acids with high sequence variability. The amino acid sequence of the heavy chain determines the class of an immunoglobulin. The five types of immunoglobulin heavy chains are known as: IgG, IgA, IgM, IgD, and IgE. IgG is divided into four subclasses, and IgA is divided into two subclasses. In serum IgA and IgG are monomers with a single 4 polypeptide unit; while, IgM is a pen tamer. IgA may also form polymers. Kappa light chain antibody can be used for the identification of leukemias, plasmacytomas and certain non Hodgkin's lymphomas. Kappa light chain contains one immunoglobulin like domain. The EU sequence has the INV allotypic marker, Ala 45 and Val 83. The ROY sequence has the INV allotypic marker, Ala 45 and Leu 83.

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