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4-Amino-1-phenylpyrrolidin-2-one+hydrochloride
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4-Amino-1-phenylpyrrolidin-2-one+hydrochloride
Catalog Number:
(103006-660)
Supplier:
Anaspec Inc
Description:
This peptide is amino acids 323 to 339 amidated fragment of ovalbumin (OVA), the H-2b-restricted OVA class II epitope. This peptide is recognized by many T cells because it contains multiple T cell epitopes. This OVA fragment contains a nested set of CD4+ T cell epitopes. OVA 323 to 339 can be presented by I-Ad in at least three binding registers. The residues 327 to 333 are critical for peptide binding to I-Ad.
Sequence: ISQAVHAAHAEINEAGR-NH2 MW: 1773 Da % Peak Area by HPLC: ≥ 95% Storage condition: -20°C
Catalog Number:
(10751-362)
Supplier:
Prosci
Description:
TMEM88 Antibody: Transmembrane protein 88 (TMEM88) is a two-transmembrane-type protein whose C-terminal tail has been shown to bind the PDZ domain of Dishevelled (Dvl), one of the key components in Wnt signaling pathways. TMEM88 attentuated the Wnt/beta-catenin signaling induced by Wnt-1 ligand in a dose-dependent manner and knockdown of TMEM88 by RNAi increased Wnt activity, suggesting that TMEM88 plays a role in regulating Wnt signaling in a context-dependent manner.
Catalog Number:
(10749-690)
Supplier:
Prosci
Description:
SARS Matrix Antibody: A novel coronavirus has recently been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. The M protein (Membrane protein, Matrix protein) is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with S (Spike) protein and the nucleocapsid protein.
Catalog Number:
(10332-636)
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:
(10332-646)
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:
(10750-062)
Supplier:
Prosci
Description:
Cathelicidin Antibody: One component of host defense at mucosal surfaces is epithelial-derived antimicrobial peptides. Cathelicidins are one family of antimicrobial peptides characterized by conserved pro-peptide sequences that have been identified in epithelial tissues and some myeloid cells of humans and animals. LL-37/hCAP-18 is the only Cathelicidin found in humans and is expressed in inflammatory and epithelial cells. The presence of these molecules is essential for defense against invasive bacterial infection in skin. Besides their direct antimicrobial function, Cathelicidins have multiple roles in mediating innate and adaptive immunity, such as endotoxin neutralizing, angiogenesis, wound healing and promoting neutrophil chemotaxis and mast cell recruitment. Finally, Cathelicidin antimicrobial peptides qualify as prototypes of innovative drugs that may be used to treat infection and/or modulate the immune response.
Catalog Number:
(76108-722)
Supplier:
Bioss
Description:
F box proteins are an expanding family of eukaryotic proteins characterized by an approximately 40 amino acid motif, the F box. Some F box proteins have been shown to be critical for the ubiquitin mediated degradation of cellular regulatory proteins. In fact, F box proteins are one of the four subunits of ubiquitin protein ligases, called SCFs. SCF ligases bring ubiquitin conjugating enzymes to substrates that are specifically recruited by the different F box proteins. A large family of mammalian F box proteins has recently been identified and classified into three groups based on the presence of either the WD 40 repeats, the leucine rich repeats, or the presence or absence of other protein protein interacting domains. The FBXW2 gene product, the second identified member of the F box gene family, contains multiple WD 40 repeats.
Catalog Number:
(10669-620)
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. SH3RF2 (SH3 domain containing ring finger 2), also known as RNF158, is a 729 amino acid protein with one RING-type zinc finger domain and three SH3 domains. Via its RING-type zinc finger domain, SH3RF2 binds an E2 ubiquitin-conjugating enzyme. This suggests that SH3RF2 functions as an E3 ubiquitin-protein ligase that accepts a ubiquitin residue from an E2 ubiquitin-conjugating enzyme and immediately transfers that residue to a protein that is targeted for degradation. Due to alternative splicing events, SH3RF2 is expressed as two different isoforms.
Catalog Number:
(10413-318)
Supplier:
Bioss
Description:
Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.
Catalog Number:
(10413-344)
Supplier:
Bioss
Description:
Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.
Catalog Number:
(10413-226)
Supplier:
Bioss
Description:
Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.
Catalog Number:
(10750-320)
Supplier:
Prosci
Description:
Dact2 Antibody: The Wnt signaling cascade is a conserved process in multicellular animals that plays important roles during development and can contribute to cancer and other diseases. Many members of this pathway are also expressed in the postnatal tissues such as brain. One such protein is Dact2, a member of the Dact protein family that was initially identified through binding to Disheveled (Dvl), a cytoplasmic protein essential to Wnt signaling. Dact2 is most prominent during the development of the thymus kidneys, and salivary gland. Dact2 is thought to play a role distinct from that of Dact1 with Dact2 having a greater impact on a beta-catenin-independent process termed planar cell polarity/convergent-extension signaling. Furthermore, Dact2 but not Dact1 can inhibit Nodal signaling by promoting the endocytic degradation of TGF-beta receptors. At least two isoforms of Dact2 are known to exist.
Catalog Number:
(10749-858)
Supplier:
Prosci
Description:
VISA Antibody: Two distinct signaling pathways activate the host innate immunity against viral infection. One pathway is reliant on members of the Toll-like receptor (TLR) family while the other uses the RNA helicase RIG-I as a receptor for intracellular viral double-stranded RNA as a trigger for the immune response. VISA is a mitochondrial membrane protein that was identified as a critical component in the IFN-b signaling pathways that recruits IRF-3 to RIG-I, leading to its activation and that of NF-kappa B. VISA is also thought to interact with other components of the innate immune pathway such as the TLR adapter protein TRIF, TRAF2 and TRAF6. VISA also interacts with the IKKalpha , IKKbeta ; and IKKepsilon kinases through its C-terminal region. Cleavage of this region by the Hepatitis C virus (HCV) protease allows HCV to escape the host immune system. At least three isoforms of VISA are known to exist.
Catalog Number:
(10332-644)
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:
(10748-774)
Supplier:
Prosci
Description:
Dact3 Antibody: The Wnt signaling cascade is a conserved process in multicellular animals that plays important roles during development and can contribute to cancer and other diseases. Many members of this pathway are also expressed in the postnatal tissues such as brain. One such protein is Dact3, a member of the Dact protein family that was initially identified through binding to Disheveled (Dvl), a cytoplasmic protein essential to Wnt signaling. Dact3 is expressed in the ventral region of maturing somites, limb bud and branchial arch mesenchyme, embryonic CNS, and the adult brain. Recent evidence shows that Dact3 acts as a negative regulator Wnt/beta-catenin signaling that is repressed at the transcriptional level in colorectal cancer and this repression is associated with bivalent histone modifications. This repression can be reversed by pharmacological agents that targets both histone methylation and deacetylation, suggesting that Dact3 may be a potential target for therapeutic treatment of this cancer. At least three isoforms of Dact3 are known to exist.
Catalog Number:
(10670-054)
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. RNF130 (ring finger protein 130), also known as GP, G1RZFP (G1-related zinc finger protein) or GOLIATH, is a 419 amino acid single-pass type I membrane protein that shares similarity with a Drosophila zinc-finger protein found in mesoderm known as g1. RNF130 contains one PA (protease associated) domain and a single RING-type zinc finger. Implicated in the regulation of growth factor withdrawal-induced apoptosis of myeloid precursor cells, RNF130 is encoded by a gene located on human chromosome 5q35.3 and mouse chromosome 11 B1.3.
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is still displayed and you need assistance, please call us at 1-800-932-5000.
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