2-Fluorothioanisole
Catalog Number:
(10247-482)
Supplier:
Bioss
Description:
HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilization. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.
Catalog Number:
(10247-484)
Supplier:
Bioss
Description:
HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilization. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.
Catalog Number:
(10298-400)
Supplier:
Bioss
Description:
GMEB-1 is a 573 amino acid protein that contains one SAND domain and is a member of the KDWK family of combinatorial transcription modulators. Localized to both the cytoplasm and the nucleus, GMEB-1 forms a heterodimer with GMEB-2 (Glucocorticoid modulatory element-binding protein 2) and, once associated with GMEB-2, plays a key role in parvovirus DNA replication. In addition, GMEB-1 functions alone as a trans-acting factor that, by binding to glucocorticoid modulatory elements (GMEs) in TAT (tyrosine aminotransferase) promoters, increases intracellular sensitivity to glucocorticoid concentrations. GMEB-1 also interacts with initiator procaspases and, via this interaction, can inhibit caspase-induced apoptosis. Due to alternative splicing events, GMEB-1 is expressed as two isoforms.
Catalog Number:
(10250-808)
Supplier:
Bioss
Description:
Extracellular proteases mediate the digestion of neighboring extracellular matrix components in initial tumor growth, allow desquamation of tumor cells into the surrounding environment, provide the basis for invasion of basement membranes in targeted metastatic organs and are required for release and activation of many growth and angiogenic factors. TMPRSS5 (transmembrane protease, serine 5), also known as spinesin, is a 457 amino acid single-pass type II membrane protein that is expressed specifically in brain and is thought to play a role in hearing. A member of the peptidase S1 family, TMPRSS5 contains one peptidase S1 domain and an SRCR domain, and is encoded by a gene that maps to human chromosome 11q23.2. Defects in the gene encoding TMPRSS5 are associated with deafness.
Catalog Number:
(10263-462)
Supplier:
Bioss
Description:
PIRT is a 137 amino acid multi-pass membrane protein. Highly conserved among vertebrates, PIRT consists of two transmembrane domains and one putative C-terminal phosphoinositide-binding domain. Although PIRT is expressed in peripheral nervous system, with highest levels in dorsal root ganglion and trigeminal neurons, and lowest levels in sympathetic and enteric neurons, it is not expressed in spinal cord. PIRT is a required component of the VR1 complex, which positively regulates VR1, a sensor of both noxious heat and capsaicin. Correspondingly, PIRT knockout results in impaired responses to noxious heat and capsaicin exposure, while VR1 remains unaltered. The gene that encodes PIRT maps to human chromosome 17p13.1.
Catalog Number:
(10668-488)
Supplier:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF10 (ring finger protein 10), also known as RIE2, is an 811 amino acid protein that localizes to the cytoplasm and contains one RING-type zinc finger. Existing as multiple alternatively spliced isoforms, RNF10 interacts with MOX-2 and is thought to regulate its transcription in schwann cells, possibly playing a role in myelin formation. The gene encoding RNF10 maps to human chromosome 12, which encodes over 1,100 genes and comprises approximately 4.5% of the human genome. Chromosome 12 is associated with a variety of diseases and afflictions, including hypochondrogenesis, achondrogenesis, Kniest dysplasia, Noonan syndrome and Trisomy 12p, which causes facial developmental defects and seizure disorders.
Catalog Number:
(102998-454)
Supplier:
Anaspec Inc
Description:
A 32-amino acid long peptide with a disulfide bridge between Cys1 and Cys7 and C-terminal amidated Proline, Calcitonin (CT) is involved plasma calcium level. Compared to human or rat calcitonin, Salmon Calcitonin (sCT) is more potent in its biological actions such as inhibition of osteoclasts resorption of bones, renal ion excretion modulation, and others. The reason for its potency has been attributed to the fact that sCT forms an amphipathic helix in its amino acids 9-19 region.
Sequence: CSNLSTCVLGKLSQELHKLQTYPRTNTGSGTP-NH2 (Disulfide bridge: 1-7) MW: 3431.9 Da % Peak area by HPLC: 95 Storage condition: -20° C
Catalog Number:
(10275-976)
Supplier:
Bioss
Description:
DPPA5 is a 116 amino acid protein that localizes to the cytoplasm and contains one KH domain. Expressed in embryonic germ (EG), primordial germ (PG) and embryonic stem (ES) cells, DPPA5 plays an important role in the maintenance of ES cell pluripotency and may be necessary for proper embryogenesis. The gene encoding DPPA5 maps to human chromosome 6, which contains 170 million base pairs and comprises nearly 6% of the human genome. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer, suggesting the presence of a cancer susceptibility locus. Additionally, Porphyria cutanea tarda, Parkinson's disease, Stickler syndrome and a susceptibility to bipolar disorder are all associated with genes that map to chromosome 6.
Catalog Number:
(10291-260)
Supplier:
Bioss
Description:
Fibronectins are multi-domain glycoproteins that bind to a variety of substances including collagen, actin, heparin, DNA, fibrin and fibronectin receptors. They are involved in a diverse array of important functions such as blood coagulation, wound healing, cell adhesion, cell differentiation and migration. FNDC4 (Fibronectin type III domain-containing protein 4), also known as FRCP1 (Fibronectin type III repeat-containing protein 1), is a 234 amino acid membrane protein that contains one fibronectin type-III domain, which serves as a binding site for DNA, heparin or the cell surface. The gene encoding FNDC4 is localized to human chromosome two, which houses over 1,400 genes and comprises nearly 8% of the human genome.
Catalog Number:
(10263-880)
Supplier:
Bioss
Description:
Biotin, also known as vitamin B7, is an essential water-soluble vitamin that is a cofactor in glucogenesis and in the metabolism of fatty acids and leucine. Biotinidase is a 523 amino acid enzyme that catalyzes the hydrolysis of biocytin to biotin and lysine. Secreted into extracellular space, biotinidase is expressed in liver, heart, placenta, brain, skeletal muscle, pancreas and kidney. Biotinidase contains one carbon-nitrogen hydrolase domain, which is involved in the reduction of organic nitrogen compounds and ammonia production. Defects in the gene encoding biotinidase are the cause of biotinidase deficiency, which is characterized by skin rash, ataxia, seizures, hearing loss, hypotonia and optic atrophy. These symptoms are due to the individual’s inability to reutilize biotin and can, therefore, typically be treated with the addition of free biotin.
Catalog Number:
(10263-878)
Supplier:
Bioss
Description:
Biotin, also known as vitamin B7, is an essential water-soluble vitamin that is a cofactor in glucogenesis and in the metabolism of fatty acids and leucine. Biotinidase is a 523 amino acid enzyme that catalyzes the hydrolysis of biocytin to biotin and lysine. Secreted into extracellular space, biotinidase is expressed in liver, heart, placenta, brain, skeletal muscle, pancreas and kidney. Biotinidase contains one carbon-nitrogen hydrolase domain, which is involved in the reduction of organic nitrogen compounds and ammonia production. Defects in the gene encoding biotinidase are the cause of biotinidase deficiency, which is characterized by skin rash, ataxia, seizures, hearing loss, hypotonia and optic atrophy. These symptoms are due to the individual’s inability to reutilize biotin and can, therefore, typically be treated with the addition of free biotin.
Catalog Number:
(10249-798)
Supplier:
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 (PCDH) gene clusters, designated alpha, beta and gamma, all of which contain multiple tandemly arranged genes. PCDHGA9 (Protocadherin gamma-A9) is a 932 amino acid that is one of 22 proteins encoded by the protocadherin gamma cluster. The protocadherein gamma cluster consists of three subfamilies (A, B and C) and PCDHGA9 is a member of the gamma subfamily A. PCDHGA9 is a type I transmembrane receptor containing six cadherin motifs and is expressed in the central nervous system where it localizes to synapses. Members of the gamma cluster of protocadherins are essential for neuronal survival. There are two isoforms of PCDHGA9 that are produced as a result of alternative splicing events.
Catalog Number:
(10283-290)
Supplier:
Bioss
Description:
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Zinc finger protein 568 (ZNF568) is a 644 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZNF568 contains fifteen C2H2-type zinc fingers and one KRAB domain through which it is thought to be involved in DNA-binding and transcriptional regulation. Two isoforms of ZNF568 exist as a result of alternative splicing events.
Catalog Number:
(10304-634)
Supplier:
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 a, b and g, all of which contain multiple tandemly-arranged genes. PCDHB10 (protocadherin b10), also known as PCHB10 or PCDH-b10, is an 800 amino acid protein that is one of 16 proteins in the protocadherin b cluster. Unlike the a and g gene clusters, whose genes are spliced to downstream constant-region exons during transcription, members of the b cluster (such as PCDHB10) do not use constant-region exons to produce mRNAs. As a result, each protocadherin b gene encodes the transmembrane, extracellular and short cytoplasmic domains of the protein. Localized to the cell membrane, PCDHB10 is a single-pass type I membrane protein that contains six cadherin domains.
Catalog Number:
(10332-632)
Supplier:
Bioss
Description:
Matrix Metalloproteinase 8 (MMP8) is also known as neutrophil collagenase and collagenase 2. MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. All collagenases cleave fibrillar collagens at one specific site resulting in generation of N terminal three quarter and C terminal one quarter fragments, which then denature to gelatin at body temperature. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. MMP13, in turn degrades type II collagen 6 fold more efficiently than type I and type II collagens and displays almost 50 fold stronger gelatinolytic activity than MMP1 and MMP8. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. Most cell types do not produce MMP8. Until recently, it was thought that MMP8 was produced exclusively by neutrophils, but it has also been detected in other cell types including arthritic chondrocytes and gingival fibroblasts. The human MMP8 gene has the chromosomal location of 11q22.2-22.3. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd. The zymogen is quickly activated to the 64 Kd form, and this breaks down to a cascade of active forms.
Catalog Number:
(76110-018)
Supplier:
Bioss
Description:
Members of the suppressor of cytokine signaling (SOCS) family of proteins contain C-terminal regions of homology called the SOCS box, which serves to couple SOCS proteins and their binding partners with the Elongin B/C complex. Several other families of proteins also contain SOCS boxes, but differ from the SOCS proteins in the type of domain they contain upstream of the SOCS box. The largest family of SOCS box-containing proteins is the ankyrin repeat and SOCS box-containing (ASB) protein family. ASB-7 (ankyrin repeat and SOCS box-containing 7) is a 318 amino acid protein that contains one SOCS box domain and seven ANK repeats and belongs to the ASB family. Existing as multiple alternatively spliced isoforms, ASB-7 functions as a substrate-recognition component of an E3 ubiquitin-protein ligase complex and, working in conjunction with other proteins, plays a role in the ubiquitination and subsequent proteasomal degradation of target proteins.
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