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Fournisseur:
Biotium
Description:
Recognizes a protein of 18-35 kDa, identified as CD90 (also known as Thy1). CD90 is a member of the immunoglobulin superfamily. It may contribute to inhibition of proliferation/differentiation of hematopoietic stem cells and neuron memory formation in the CNS. It consists of a single Ig domain (112 amino acids; 25-35 kDa) inserted into the cell membrane via a GPI anchor. Expressed by hematopoietic stem cells and neurons in all species studied. Its highly expressed in connective tissue and various fibroblast and stromal cell lines, expressed on all thymocytes and peripheral T cells in mice, but in humans expressed only on small % fetal thymocytes, 10-40% of CD34 cells in bone marrow, and <1% of CD3 CD4 lymphocytes in peripheral circulation. It is also expressed by human lymph node HEV endothelium but not other endothelia. Lastly, it is expressed by a limited number of lymphoblastoid and leukemic cell lines.
Numéro de catalogue:
(BOSSBS-15573R)
Fournisseur:
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
Numéro de catalogue:
(BOSSBS-15429R-A488)
Fournisseur:
Bioss
Description:
HCP5 is a region present on chromosome 6p21.3 that is characterised by multiple duplicated gene families. HCP5 (HLA class I histocompatibility antigen protein P5), also known as P5-1, is a 132 amino acid protein that is encoded by a gene mapping to human chromosome 6p21.33. Localising within the MHC class I region, HCP5 is not structurally related to other MHC class I genes, but does have high sequence similarity with HERV-L and HERV-16. HCP5 also has high sequence homology to retroviral Pol genes, making it a possible candidate for interaction with HIV-1 through an antisense mechanism that prevents retrovirus transcription. Single-nucleotide polymorphisms (SNPs) to the region of the HCP5 gene that corresponds with HLA-B has been linked to a lower HIV-1 viral set point. HCP5 is highly expressed in lymphoid tissues, spleen and activated lymphocytes, as well as B-cell and natural killer (NK) cell lines.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6049R-CY5.5)
Fournisseur:
Bioss
Description:
FGFRL1 is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11955R-A647)
Fournisseur:
Bioss
Description:
SLITRK family proteins are integral membrane proteins that have a C-terminal domain that is partially similar to TRK neurotrophin receptor proteins and two leucine-rich repeat (LRR) domains that are similar to those of SLIT proteins. SLITRK2 (SLIT and NTRK-like protein 2) is a 845 amino acid single-pass type I membrane protein that contains 14 LRR (leucine-rich) repeats and is expressed in neural tissues, with highest levels found in adult cerebral cortex. Overexpression of SLITRK2 leads to inhibition of unipolar neurites in cultured cells, suggesting that it suppresses neurite outgrowth. Inhibitory activity of SLITRK2 is localized to its C-terminal intracellular domain and without this region the protein induces neurite outgrowth. Variants in the gene encoding SLITRK2 may contribute to the development of bipolar disorder, autism spectrum disorder and schizophrenia. There are two isoforms of SLITRK2 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11955R-FITC)
Fournisseur:
Bioss
Description:
SLITRK family proteins are integral membrane proteins that have a C-terminal domain that is partially similar to TRK neurotrophin receptor proteins and two leucine-rich repeat (LRR) domains that are similar to those of SLIT proteins. SLITRK2 (SLIT and NTRK-like protein 2) is a 845 amino acid single-pass type I membrane protein that contains 14 LRR (leucine-rich) repeats and is expressed in neural tissues, with highest levels found in adult cerebral cortex. Overexpression of SLITRK2 leads to inhibition of unipolar neurites in cultured cells, suggesting that it suppresses neurite outgrowth. Inhibitory activity of SLITRK2 is localized to its C-terminal intracellular domain and without this region the protein induces neurite outgrowth. Variants in the gene encoding SLITRK2 may contribute to the development of bipolar disorder, autism spectrum disorder and schizophrenia. There are two isoforms of SLITRK2 that are produced as a result of alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8381R-A555)
Fournisseur:
Bioss
Description:
Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8381R-FITC)
Fournisseur:
Bioss
Description:
Ubiquitination is an important molecular mechanism by which abnormal or short-lived proteins are targeted for degradation by the concerted efforts of at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2J2 (Ubiquitin-conjugating enzyme E2 J2), also known as NCUBE2 (Non-canonical ubiquitin-conjugating enzyme 2), is a 259 amino acid single pass type IV membrane protein that that belongs to the E2 ubiquitin-conjugating enzyme family and is involved in protein degradation. Localized to the membrane of the endoplasmic reticulum (ER), UBE2J2 catalyzes the attachment of ubiquitin to misfolded membrane proteins, thereby targeting them for proteasomal destruction. This ATP-dependent reaction yields AMP, a diphosphate and a ubiquitin-tagged protein and may be a method of quality control within the ER. Two isoforms of UBE2J2 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11227R-A750)
Fournisseur:
Bioss
Description:
Microcephalin modulates brain size and has been proliferating under strong positive selection for several thousand years, although the nature of the positive selection is poorly understood. Human Microcephalin contains three BRCA1 C-terminal (BRCT) domains and shares 57% identity with its mouse ortholog, the most conserved regions being BRCT domains where there is 80% identity. Predominant expression of human Microcephalin is observed in fetal brain, liver and kidney tissues and is expressed during neurogenesis in mice. Microcephalin displays significantly higher rates of protein evolution in primates than in rodents; this trend is most noticeable for the subset of genes associated with nervous system development. Microcephalin has a very young, single nucleotide, polymorphism haplotype associated with modern humans; this gene is presumably still evolving in Homo sapiens. It functions in DNA damage response and regulation of cell cycle checkpoints.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12496R-HRP)
Fournisseur:
Bioss
Description:
Apolipoproteins are protein components of plasma lipoproteins. The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins. The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages. The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues. The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase. The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6587R-A647)
Fournisseur:
Bioss
Description:
Function as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb recognizes a 27 kDa protein, identified as the p27Kip1, a cell cycle regulatory mitotic inhibitor. It is highly specific and shows no cross-reaction with other related mitotic inhibitors. In Western blotting of cell lysates from 7 human breast cancer cell lines (ZR75-1, ZR75-30, MCF-7, MDAMB453, T47D, CAL51, 734B), the antibody labels a single band corresponding to p27Kip1. It functions as a negative regulator of G1 progression and has been proposed to function as a possible mediator of TGF- induced G1 arrest. p27Kip1 is a candidate tumor suppressor gene. Reportedly, low p27 expression has been associated with unfavorable prognosis in renal cell carcinoma, colon carcinoma, breast carcinomas, non-small-cell lung carcinoma, hepatocellular carcinoma, multiple myeloma, and lymph node metastases in papillary carcinoma of the thyroid, as well as a more aggressive phenotype in carcinoma of the cervix.
Numéro de catalogue:
(BOSSBS-12497R-A555)
Fournisseur:
Bioss
Description:
Apolipoproteins are protein components of plasma lipoproteins (1). The apolipoprotein C gene family encodes four homologous proteins designated apoC-I to -IV, which specifically modulate the metabolism of triglyceride-rich lipoproteins (2). The human apoC-I gene maps to chromosome 19q13.2 and is expressed primarily in the liver where it is activated when monocytes differentiate into macrophages (3,4). The human apoC-II gene maps to chromosome 19q13.2 and encodes a 79 amino acid single chain protein that is a necessary cofactor for the activation of lipoprotein lipase, the enzyme that hydrolyzes triglycerides in plasma and transfers the fatty acids to tissues (5–7). The human apoC-III gene maps to chromosome 11q23 and encodes a protein that may delay catabolism of triglyceride-rich particles by inhibiting lipoprotein lipase and hepatic lipase (8). The human apoC-IV gene maps to chromosome 19q13.2 and encodes a 127 amino acid protein that is primarily expressed in the liver (9,10).
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb recognizes a 27 kDa protein, identified as the p27Kip1, a cell cycle regulatory mitotic inhibitor. It is highly specific and shows no cross-reaction with other related mitotic inhibitors. In Western blotting of cell lysates from 7 human breast cancer cell lines (ZR75-1, ZR75-30, MCF-7, MDAMB453, T47D, CAL51, 734B), the antibody labels a single band corresponding to p27Kip1. It functions as a negative regulator of G1 progression and has been proposed to function as a possible mediator of TGF- induced G1 arrest. p27Kip1 is a candidate tumor suppressor gene. Reportedly, low p27 expression has been associated with unfavorable prognosis in renal cell carcinoma, colon carcinoma, breast carcinomas, non-small-cell lung carcinoma, hepatocellular carcinoma, multiple myeloma, and lymph node metastases in papillary carcinoma of the thyroid, as well as a more aggressive phenotype in carcinoma of the cervix.
Numéro de catalogue:
(BOSSBS-13628R-A350)
Fournisseur:
Bioss
Description:
The C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily consists of a variety of proteins that share a common protein fold and have diverse functions, including cell-cell signaling, cell adhesion, glycoprotein turnover and immune responses. CLEC-12A (C-type lectin domain family 12, member A), also known as CLL1, MICL, CLL-1 or DCAL-2, is a 275 amino acid single-pass type II membrane protein that contains one C-type lectin domain and belongs to the CTL/CTLD superfamily. Existing as multiple alternatively spliced isoforms that are expressed in neutrophils, eosinophils, monocytes and dendritic cells, CLEC-12A functions as a cell surface receptor that acts as a negative regulator of granulocyte and monocyte function and, via this activity, modulates signaling cascades. CLEC-12A is highly subject to post-translational glycosylation at its N-terminus and may also exist as a homodimer.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11468R-A680)
Fournisseur:
Bioss
Description:
Nogo is an oligodendrocyte-specific member of the Reticulon family and is a component of CNS white matter that inhibits axon outgrowth, induces collapse of growth cones of chick dorsal root ganglion cells, and inhibits the spreading of 3T3 fibroblasts. Nogo is expressed by oligodendrocytes but not by Schwann cells and associates primarily with the endoplasmic reticulum. Nogo exists in three different splice forms, Nogo A, B and C. NgBR (Nogo-B receptor), also known as nuclear undecaprenyl pyrophosphate synthase 1 homolog, is a 293 amino acid single-pass type I membrane protein that acts as a specific receptor for the amino-terminus of Nogo-B. Through this interaction, NgBR is involved in the regulation of vascular remodeling and angiogenesis. NgBR also enhances Niemann-Pick type C2 protein (NPC2) stabilisation. Knockdown of NgBR mRNA leads to decreased NPC2 levels, which results in the hallmarks of NPC2 mutation: increased intracellular cholesterol accumulation and a loss of sterol sensing.
UOM:
1 * 100 µl
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