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Ethyl+2-(6-aminopyridin-3-yl)acetate
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Ethyl+2-(6-aminopyridin-3-yl)acetate
Catalog Number:
(75844-000)
Supplier:
BIOGEMS INTERNATIONAL INC.
Description:
The RPA-T4 monoclonal antibody specifically binds to the CD4 receptor for the human immunodeficiency virus (HIV). CD4 is a 59 kDa single-chain transmembrane glycoprotein that expressed on the surface of most of the thymocytes, T-helper cells, and in low levels on monocytes and macrophages. CD4 is a co-receptor in the antigen-induced T cell activation, together with the MHC class II. The RPA-T4 antibody is capable of blocking HIV binding and inhibiting syncytium formation, by binding to the D1 domain of the CD4 antigen. The OKT4 and the RPA-T4 monoclonal antibodies recognize different epitopes of CD4 and they do not exhibit cross-block binding.
Catalog Number:
(10446-992)
Supplier:
Bioss
Description:
Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.
Catalog Number:
(10398-612)
Supplier:
Bioss
Description:
Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.
Catalog Number:
(10446-980)
Supplier:
Bioss
Description:
Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.
Catalog Number:
(10446-998)
Supplier:
Bioss
Description:
Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.
Catalog Number:
(10425-860)
Supplier:
Bioss
Description:
Myosin is a protein which is known to interact with actin in muscle and non-muscle cells. It contains two identical heavy chains and four light chains. Myosin molecules consist of two major regions: tails (rods) and heads. They aggregate into filaments through the tail region and interact with actin and with ATP through the head region. Multiple forms of myosin heavy chains exist for each muscle type-skeletal, cardiac, smooth and non-muscle isomyosin forms exist in different types of skeletal muscle, depending on the physiological function of the muscle. They are designated at type I (slow twitch) and type II (fast twitch).
Catalog Number:
(75790-496)
Supplier:
Prosci
Description:
Bone Morphogenetic Protein Receptor Type-1A (BMPR1A) belongs to the TKL Ser/Thr protein kinase family and TGFB receptor subfamily, including the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. BMPR1A is a single-pass type I membrane protein and highly expressed in skeletal muscle. BMPR1A contains one GS domain and one protein protein kinase domain. BMPR1A is necessary for the extracellular matrix depostition by osteoblasts. BMPR1A can activate SMAD transcriptional regulators, binding with ligands. Defects in BMPR1A are a cause of juvenile polyposis syndrome, Cowden disease and hereditary mixed polyposis syndrome 2 (HMPS2).
Catalog Number:
(77436-736)
Supplier:
Bioss
Description:
May contribute to arginine-vasopressin (AVP)-mediated regulation of renal salt-water balance, glucose and lipid metabolism, apoptosis, and/or cell cycle. Binds arginine-vasopressin but not angiotensin II and acts as an arginine-vasopressin V2 receptor. Plays a role in modulating inflammatory responses in the colon to allow recovery from intestinal epithelial damage and limit tumorigenic potential. Protects against the development of colitis by controlling the composition of the gut microbiota by preventing colonization of the colon by harmful, inflammation-inducing bacteria such as Prevotella species. May mediate activation of CASP1 via ASC, promote activation of NF-kappa-B and stimulate cAMP accumulation (By similarity).
Catalog Number:
(10360-820)
Supplier:
Bioss
Description:
Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling.
Catalog Number:
(10106-202)
Supplier:
Prosci
Description:
Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TBPL1 encodes a protein that serves the same function as TBP and substitutes for TBP at some promoters that are not recognized by TFIID. It is essential for spermiogenesis and believed to be important in expression of developmentally regulated genes.
Catalog Number:
(76079-100)
Supplier:
Bioss
Description:
Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in -pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.
Catalog Number:
(10398-602)
Supplier:
Bioss
Description:
Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine.
Catalog Number:
(10801-630)
Supplier:
Rockland Immunochemical
Description:
The 50 kDa type III intermediate filament protein glial fibrillary acidic protein (GFAP) is a major structural component of astrocytes. GFAP associates with the calcium binding protein annexin II-p2 and S-100. Association with these proteins together with phosphorylation regulates GFAP polymerization. Astroycytes respond to brain injury by proliferatin (astrogliosis), and one of the first events to occur during astrocyte proiliferation is increased GFAP expression. Interestingly, antibodies to GFAP have been detected in individuals with dementia. Anti-GFAP is ideal for investigators involved in Neuroscience Research, including Alexander Disease, Oligodendroglioma, Cytoskleton Remolding Neurofilaments and PIP3/AKT Signaling.
Catalog Number:
(10801-594)
Supplier:
Rockland Immunochemical
Description:
The 50 kDa type III intermediate filament protein glial fibrillary acidic protein (GFAP) is a major structural component of astrocytes. GFAP associates with the calcium binding protein annexin II-p2 and S-100. Association with these proteins together with phosphorylation regulates GFAP polymerization. Astroycytes respond to brain injury by proliferatin (astrogliosis), and one of the first events to occur during astrocyte proiliferation is increased GFAP expression. Interestingly, antibodies to GFAP have been detected in individuals with dementia. Anti-GFAP is ideal for investigators involved in Neuroscience Research, including Alexander Disease, Oligodendroglioma, Cytoskleton Remolding Neurofilaments and PIP3/AKT Signaling.
Catalog Number:
(10296-042)
Supplier:
Bioss
Description:
2010013H22Rik; 2210021I22Rik; 2210401J11Rik; 3-galactosyl-O-glycosyl-glycoprotein beta-1; 6-N-acetylglucosaminyltransferase 3; 6-N-acetylglucosaminyltransferase; Beta 1 3 galactosyl O glycosyl glycoprotein beta 1 6 N acetylglucosaminyltransferase 3; Beta-1; Beta1 6 N acetylglucosaminyltransferase 3; beta1 6 N acetylglucosaminyltransferase; C2/4GnT; C24GNT; C2GnT M; C2GnT mucin type; C2GnT-M; C2GnT-mucin type; C2GnT2; C2GNTM; Core 2 beta 1 6 N acetylglucosaminyltransferase II; Core 2/core 4 beta 1 6 N acetylglucosaminyltransferase; Core 2/core 4 beta-1; dI/C2/C4GnT; EC 2.4.1.102; EC 2.4.1.150; GCNT3; GCNT3_HUMAN; Glucosaminyl (N acetyl) transferase 3; Glucosaminyl (N acetyl) transferase 3 mucin type; GnT M; GNTM; hC2GnT M; hC2GnT-M; Mucus-type core 2 beta-1,6-N-acetylglucosaminyltransferase. OTTHUMP00000163601.
Catalog Number:
(10264-164)
Supplier:
Bioss
Description:
CSAD is a 493 amino acid protein that exists as a homodimer and belongs to the group II decarboxylase family. CSAD catalyzes the conversion of 3-sulfino-L-alanine to hypotaurine and carbon dioxide, binds pyridoxal phosphate as a cofactor and undergoes alternative splicing to produce three isoforms. The gene encoding CSAD 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.
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 is still displayed and you need assistance, please call us at 1-800-932-5000.
Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
is still displayed and you need assistance, please call us at 1-800-932-5000.
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