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Catalog Number: (BOSSBS-11871R-CY3)
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


Catalog Number: (BOSSBS-11871R)
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


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.

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-13276R-FITC)
Supplier: Bioss
Description: Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into alpha, beta, and gamma families, and the beta and gamma-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. gamma-crystallins are structural proteins in the lens, and they exists as monomers which typically lack connecting peptides and terminal extensions. The gamma-crystallins include seven closely related gamma A, gamma B, gamma C, gamma D, gamma E, gamma F, and gamma G-crystallin, as well as the gamma N and gamma S-crystallin genes. The gamma-crystallins are differentially regulated after early development, and are involved in cataract formation as a result of either age-related protein degradation or genetic mutation.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11676R-A680)
Supplier: Bioss
Description: UCH-L1 is a member of a gene family whose products hydrolyse small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumours. UCH-L1 is expressed in brain neurons. Examination of specific brain regions reveals expression in all areas tested, particularly in the substantia nigra. UCH-L1 represents 1 to 2% of total soluble brain protein. Its occurrence in Lewy bodies and its function in the proteasome pathway make it a compelling candidate gene in Parkinson disease. The gene which encodes UCH-L1 maps to human chromosome 4p14. The 230 amino acid human UCH-L3 protein is 54% identical to that of UCH-L1. UCH-L3 is the predominant thiol protease and has high-affinity binding sites for ubiquitin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11676R-A555)
Supplier: Bioss
Description: UCH-L1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. UCH-L1 is expressed in brain neurons. Examination of specific brain regions reveals expression in all areas tested, particularly in the substantia nigra. UCH-L1 represents 1 to 2% of total soluble brain protein. Its occurrence in Lewy bodies and its function in the proteasome pathway make it a compelling candidate gene in Parkinson disease. The gene which encodes UCH-L1 maps to human chromosome 4p14. The 230 amino acid human UCH-L3 protein is 54% identical to that of UCH-L1. UCH-L3 is the predominant thiol protease and has high-affinity binding sites for ubiquitin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11676R-A647)
Supplier: Bioss
Description: UCH-L1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. UCH-L1 is expressed in brain neurons. Examination of specific brain regions reveals expression in all areas tested, particularly in the substantia nigra. UCH-L1 represents 1 to 2% of total soluble brain protein. Its occurrence in Lewy bodies and its function in the proteasome pathway make it a compelling candidate gene in Parkinson disease. The gene which encodes UCH-L1 maps to human chromosome 4p14. The 230 amino acid human UCH-L3 protein is 54% identical to that of UCH-L1. UCH-L3 is the predominant thiol protease and has high-affinity binding sites for ubiquitin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3023R-HRP)
Supplier: Bioss
Description: AML1/Runx1 binds DNA as a monomer and through the Runt domain. DNA binding is increased by heterodimerization with CBFB. Isoform AML1L can neither bind DNA nor heterodimerize and interferes with the transactivation activity of AML1/Runx1. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T cell receptor enhancers, LCK, IL3 and GMCSF promoters. The alpha subunit binds DNA and appears to have a role in the development of normal hematopoiesis. AML1/Runx1 is expressed in a wide variety of tissues and is expressed at the highest levels in thymus, bone marrow and peripheral blood. Defects in AML1/Runx1 are the cause of familial platelet disorder with associated myeloid malignancy, an autosomal dominant disease characterized by qualitative and quantitative platelet defects, and propensity to develop acute myelogenous leukemia.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-3023R-CY7)
Supplier: Bioss
Description: AML1/Runx1 binds DNA as a monomer and through the Runt domain. DNA binding is increased by heterodimerization with CBFB. Isoform AML1L can neither bind DNA nor heterodimerize and interferes with the transactivation activity of AML1/Runx1. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T cell receptor enhancers, LCK, IL3 and GMCSF promoters. The alpha subunit binds DNA and appears to have a role in the development of normal hematopoiesis. AML1/Runx1 is expressed in a wide variety of tissues and is expressed at the highest levels in thymus, bone marrow and peripheral blood. Defects in AML1/Runx1 are the cause of familial platelet disorder with associated myeloid malignancy, an autosomal dominant disease characterized by qualitative and quantitative platelet defects, and propensity to develop acute myelogenous leukemia.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13086R)
Supplier: Bioss
Description: Epithelial protein lost in neoplasm (EPLIN) is a cytoskeleton-associated protein characterized by the presence of a single centrally located lin-11, isl-1 and mec-3 (LIM) domain. It also contains at least two Actin-binding domains, in which the C-terminal domain binds more effectively than the N-terminal domain. By binding Actin monomers and filaments, EPLIN is involved in regulation of the Actin cytoskeleton by increasing the number and size of Actin stress fibers, delaying filament nucleation, reducing formation of branched filaments and bundling of Actin filaments. It also inhibits membrane ruffling and Actin filament depolymerization. EPLIN is strongly expressed in placenta, kidney, pancreas, prostate, ovary, spleen and heart, and to a lesser degree in lung, liver, brain, skeletal muscle, thymus, testis and intestine. It is expressed as two isoforms, EPLIN-α and EPLIN-β. Downregulation of EPLIN-α expression may contribute to the motility of invasive tumor cells.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-15573R-A488)
Supplier: Bioss
Description: Ig delta chain C region is an allelic product of the human IGHD gene. The two known IGHD alleles, IGHD*01 and IGHD*02, respectively produce isoforms 1, a secreted protein, and 2, a single-pass type I membrane protein. A member of the adaptive immune system, IgD are monomers expressed by activated B cells. Containing 3 Ig-like (immunoglobulin-like) domains, IgD chain C is located on chromosome 14 within the human heavy chain locus, lying on the 3? side of the IgM chain C region from the V-D-J cassette. Polyadenylation at certain sites along the heavy chain locus likely effects the mechanism that determines the alternative splicing event which results in the expression of either IgD chain C or IgM chain C. Some studies have suggested that antigenic coactivation of IgD+ B cells can have a negative influence on bone resorption during infectious events.
UOM: 1 * 100 µl


Catalog Number: (BTIUBNUM0724-50)
Supplier: Biotium
Description: 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.
UOM: 1 * 50 µl


Catalog Number: (ORIGTA183039)
Supplier: OriGene
Description: Anti-DsRed-Monomer IgG1 Monoclonal Antibody (Magnetic beads) [clone: OTI4C7 (formerly 4C7)]
UOM: 1 * 1 mL


Catalog Number: (BOSSBS-0474R-A750)
Supplier: Bioss
Description: Human IgA (immunoglobulin A) is a glycosylated protein of 160 kDa and is produced as a monomer or as a J chain linked dimer. Monomeric IgA constitutes 5-15 % of the serum immunoglobulins whereas dimeric IgA is localised to mucosa surfaces such as saliva, gastrointestinal secretion, bronchial fluids and milk. Mucosal IgA plays a major role in host defence by neutralising infectious agents at mucosal surfaces. The production is usually local and antigen specific IgA producing B cells can be found in regions under the lamina propria where they mature into dimeric IgA producing plasma cells. IgA deficiency is the most common immunodeficiency that may affect both serum and mucosal produced IgA.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9585R-A750)
Supplier: Bioss
Description: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated and Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. S-crystallin (Gamma-crystallin S), also known as Beta-crystallin S, is a 178 amino acid protein that exists as a monomer which does not aggregate. S-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. S-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.
UOM: 1 * 100 µl


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