Anti-Human BD-3 Antibody
518.55 EUR
In Stock
quantity
Produktdetaljer
Katalognummer: 209 - 102-P220
Produktkategori: Företag och industri > Vetenskap och laboratorium
Gentaur
Storlek: 100 µg
102-P220
Anti-Human BD-3 Antibody
Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds.
518.55 €
102-P103G
Anti-Human BD-2 Antibody
Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds.
518.55 €
102-P219
Anti-Human BD-1 Antibody
Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds.
518.55 €
101-M470
Anti-Human Dkk-3 Antibody
The dickkopf (DKK)-related protein family is comprised of four central members, DKK-1 - 4, along with the distantly-related DKK family member DKK-l1 (Soggy), which is thought to be a descendent of an ancestral DKK-3 precursor due to its unique sequence homology to DKK-3 and no other DKK family member. DKK family members, with the exception of the divergent Soggy, share two conserved cysteine-rich domains and show very little sequence similarity outside of these domains. Playing an important regulatory role in vertebrate development through localized inhibition of Wnt regulated processes, including anterior-posterior axial patterning, limb development, somitogenesis, and eye formation, DKKs have also been implicated post-developmentally in bone formation, bone disease, cancer, and neurodegenerative diseases. DKK proteins typically play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. DKK-3 has been shown to potentiate, rather than inhibit, Wnt signaling through interactions with the high-affinity, transmembrane coreceptors Kremen-1 (Krm1) and Kremen-2 (Krm2). Recombinant human DKK-3 expressed in CHO cells is a glycoprotein that has a calculated molecular weight of 36.3 kDa and contains 329 amino acid residues. Due to glycosylation, human DKK-3 migrates at an apparent molecular weight of approximately 39-49 kDa by SDS-PAGE analysis under non-reducing conditions.
748.5 €
101-M739
Anti-Human Flt-3 Antibody
The Flt3 (fms-like tyrosine kinase) receptor, also named Flk2 (fetal liver kinase) and Stk1 (stem cell tyrosine kinase) is a member of the class III subfamily of receptor tyrosine kinases that also includes KIT, the receptor for SCF and FMS, the receptor for MCSF. The extracellular region of these receptors contains five immunoglobulin-like domains and the intracellular region contains a split kinase domain. Human Flt3 cDNA encodes a 993 amino acid (aa) residue type I membrane protein with a 26 aa residue signal peptide, a 515 aa extracellular domain with 10 potential N-linked glycosylation sites, a 21 aa residue transmembrane domain and a 431 aa residue cytoplasmic domain. Mouse Flt3 has also been cloned and shown to share 85% amino acid sequence identity with human Flt3. Flt3 expression has been detected in various tissues, including placenta, gonads, and tissues of nervous and hematopoietic origin. Among hematopoietic cells, the expression of Flt3 was found to be restricted to the highly enriched stem/progenitor cell populations. The ligand for Flt3 (FL) has been identified to be a transmembrane protein with structural homology to M-CSF and SCF. Recombinant soluble Flt3/ Fc chimeric protein has been shown to bind FL with high affinity and is a potent FL antagonist.
748.5 €
101-M809
Anti-Human MMP-3 Antibody
Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP3 (stromelysin1), can degrade a broad range of substrates including collagen α chains, aggrecan, laminin, fibronectin, elastin, casein, α1 antitrypsin, myelin basic protein, IL1β, IGFBP3, pro MMP1, pro MMP7, pro MMP8, pro MMP9 and pro MMP13. MMP3 does not cleave the triple helical region of interstitial collagens, a characteristic which distinguishes the stromelysins from the collagenases. The MMP3 substrate repertoire extends beyond extracellular matrix proteins and implicates MMP3 in roles other than direct tissue remodelling, for instance, enzyme cascades and cytokine regulation. MMP3 is expressed by fibroblasts, chrondrocytes, osteoblasts, endothelial cells, smooth muscle cells and macrophages. Structurally, MMP3 may be divided into several distinct domains; a prodomain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexinlike) domain.
748.5 €
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