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Bioss
Numéro de catalogue:
(BOSSBS-11114R-FITC)
Fournisseur:
Bioss
Description:
Protocadherins are a large family of cadherin-like cell adhesion proteins that are involved in the establishment and maintenance of neuronal connections in the brain. There are three protocadherin gene clusters, designated alpha, beta and gamma, all of which contain multiple tandemly arranged genes. PCDH8 (protocadherin-8), also known as Arcadlin or PAPC, is a 1,070 amino acid single-pass type I membrane protein that contains six cadherin domains and belongs to the protocadherin family. Localized to the cell membrane and expressed specifically in fetal and adult brain, PCDH8 is thought to play a role in cell adhesion events in the central nervous system (CNS). PCDH8 is inactivated or silenced in breast cancer, suggesting a possible role in tumor suppression. Two isoforms of PCDH8 that differ in their cytoplasmic tails are expressed due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6980R-FITC)
Fournisseur:
Bioss
Description:
The type II cAMP-protein kinase (PKA) is a multifunctional kinase with a broad range of substrates (1). Specificity of PKA signaling is thought to be mediated by the compartmentalization of the kinase to specific sites within the cell. To maintain this specific localization, the R subunit (RII) of PKA interacts with specific RII-anchoring proteins. This family of proteins has been designated A-kinase anchoring proteins (AKAP) (1-3). Members of this family, including MAP2 (microtubule-associated protein 2), neuronally expressed AKAP 79 and AKAP 150, and the DNA binding AKAP 95, display differential tissue specificity and localization (4-6). Evidence suggests that AKAP 79 and AKAP 150 are both capable of anchoring PKA to postsynaptic densities (PSD), which are a network of proteins located on the internal surfaces of excitatory synapses.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12463R-A555)
Fournisseur:
Bioss
Description:
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12463R-CY3)
Fournisseur:
Bioss
Description:
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1578R-A488)
Fournisseur:
Bioss
Description:
Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11113R-CY5)
Fournisseur:
Bioss
Description:
As a subfamily of the cadherin superfamily, protocadherins are cadherin-like cell adhesion proteins that contain up to seven extracellular domains and are predominantly expressed in the nervous system. Importantly, the adhesion mechanism of protocadherins is distinct from classic cadherins. Through inactivation or overexpression, several protocadherins have been implicated in a variety of cancers. Protocadherin-20 (PCDH20), also known as protocadherin-13, is a 924 amino acid protein containing 6 cadherin domains and potentially functioning as a calcium-dependent cell-adhesion protein. In non-small cell lung cancer cell lines, a homozygous loss of PCDH20 was identified through either deletion of one allele and methylation of the other or methylation of both alleles. Hypermethylation of PCDH20 is associated with worse prognosis and clinical outcome, suggesting that PCDH20 may function as a tumor suppressor.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7545R-A680)
Fournisseur:
Bioss
Description:
High density lipoproteins (HDLs) play a critical role in cholesterol metabolism and their plasma concentrations are inversely correlated with risk for atherosclerosis. SR-BI and SR-BII (previously known as SR-BI.2) are the alternatively spliced products of a single gene. SR-BII and SR-BI are identical except for the encoded c-terminal cytoplasmic domain. Both SR-BI and SR-BII bind HDL and mediates selective uptake of HDL cholesteryl ester, but with SR-BII having an approximately 4-fold lower efficiency than SR-BI. SR-BI and SR-BII are expressed primarily in liver and non-placental steroidgenic tissues. Although the role of these scavenger receptors is not completely clear, SR-BII mRNA results from the alternative splicing of SR-BI precursor transcripts with both isoforms mediating selective transfer of lipid between HDL and cells. Therefore, the relative expression and functional activities of these two isoforms create a potential means of regulating selective lipid transfer between HDL and cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7772R-A680)
Fournisseur:
Bioss
Description:
Septin 14, also known as SEPT14, is a 432 amino acid protein that belongs to the septin family. The highly conserved septin family of GTP-binding cytoskeletal proteins is implicated in membrane transport, apoptosis, cell polarity, cell cycle regulation, cytokinesis and other cellular functions. Septins polymerise into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. Septin 14 has a GTPase domain followed by a C-terminal coiled-coil domain characteristic of group II septins. Septin 14 interacted with all septins except those that are members of its phylogenetic cluster, including itself. Septin 14 shares highest identity (67%) with Septin 10. Expressed in testis and more weakly in fetal liver, tonsil and thymus, the Septin 14 protein is not detected in testicular cancer or other normal or cancer cell lines. The Septin 14 gene is conserved in chimpanzee, dog, cow, mouse and rat, and maps to human chromosome 7p11.2.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3879R-CY5)
Fournisseur:
Bioss
Description:
Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7110R-HRP)
Fournisseur:
Bioss
Description:
Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1.Tissue specificity: Highly expressed in placenta, lung, kidney, pancreas and ovary. Expressed at intermediate level in thymus, testes and colon.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3250R-FITC)
Fournisseur:
Bioss
Description:
This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3250R-HRP)
Fournisseur:
Bioss
Description:
This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3250R-CY5.5)
Fournisseur:
Bioss
Description:
This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3250R-CY3)
Fournisseur:
Bioss
Description:
This gene, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3191R-FITC)
Fournisseur:
Bioss
Description:
The protein encoded by this gene belongs to the NF-kappa-B inhibitor family, which inhibit NF-kappa-B by complexing with, and trapping it in the cytoplasm. Phosphorylation of serine residues on these proteins by kinases marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF-kappa-B, which translocates to the nucleus to function as a transcription factor. Alternatively spliced transcript variants have been found for this gene.[provided by RefSeq, Jul 2011].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5859R-A750)
Fournisseur:
Bioss
Description:
ADAMTS proteases are secreted enzymes containing a prometalloprotease domain of the reprolysin type. The ADAMTS proteases function in processing of procollagens and von Willebrand factor as well as catabolism of aggrecan, versican and brevican. They have been demonstrated to have important roles in connective tissue organisation, coagulation, inflammation, arthritis, angiogenesis and cell migration.A member of the metalloproteinase family containing disintegrin like domains (ADAMs), the function of ADAMTS8 is still poorly understood. ADAMTS8 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active on a range of substrates. ADAMTS8 is inhibited by the endogenous MMP inhibitors, TIMP1, 2, 3 and 4, but most efficiently by TIMP3. In addition to the metalloprotease domain, ADAMTS8 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine rich domain and thrombospondin 1 like domains.
UOM:
1 * 100 µl
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