Anti-Human LEC Antibody

101-M73

Anti-Human LEC Antibody

LEC is a CC chemokine that can signal through the CCR8 and CCR1 receptors. It is expressed in the liver, spleen, and thymus. LEC is chemotactic towards monocytes and lymphocytes but not neutrophils. Recombinant human LEC is an 11.2 kDa protein containing 97 amino acid residues, including the four conserved cysteine residues present in CC chemokines.

520.12 €

GWB-BIG63D

Anti-Human LEC

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MBS550695-01mg

Anti-Human LEC (CCL16)

516.5 €

101-M616

Anti-Human EGF Antibody

Epidermal growth factor (EGF) is the founding member of the EGF family that also includes TGFα, amphiregulin (AR), betacellulin (BTC), epiregulin (EPR), heparin-binding EGF-like growth factor (HBEGF), epigen, and the neuregulins (NRG)1 through 6. Members of the EGF family share a structural motif, the EGFlike domain, which is characterized by three intramolecular disulfide bonds that are formed by six similarly spaced conserved cysteine residues. All EGF family members are synthesized as type I transmembrane precursor proteins that may contain several EGF domains in the extracellular region. The mature proteins are released from the cell surface by regulated proteolysis. The 1207 amino acid (aa) human EGF precursor contains nine EGF domains and nine LDLR class B repeats. The mature protein consists of 53 aa and is generated by proteolytic excision of the EGF domain proximal to the transmembrane region. Mature human EGF shares 70% aa sequence identity with mature mouse and rat EGF. EGF is present in various body fluids, including blood, milk, urine, saliva, seminal fluid, pancreatic juice, cerebrospinal fluid, and amniotic fluid. Four ErbB (HER) family receptor tyrosine kinases including EGFR/ErbB1, ErbB2, ErbB3 and ErbB4, mediate responses to EGF family members.

748.5 €

101-M619

Anti-Human Ret Antibody

The GDNF family of neurotrophic factors forms a subfamily within the TGFβ superfamily. These proteins are potent survival factors for various central and peripheral neurons during development and the adult animal. The GDNF family members (GDNF, neurturin, artemin and persephin) signal through multicomponent receptors that consist of the Ret receptor tyrosine kinase and one of four glycosylphosphatidylinositol (GPI)linked ligandbinding subunits (GFRα14). GFRα1 2, 3 and 4 are the preferred ligandbinding subunits for GDNF, neurturin, artemin and persephin, respectively. The Ret tyrosinekinase receptor is encoded by the c-ret protooncogene. Mutations of the ret gene have been associated with various human diseases affecting tissues derived from the neural crest, including Hirschsprung’s disease, multiple endocrine neoplasia MEN2A and MEN2B, and familial medullary thyroid carcinoma. Human and mouse Ret share 83% amino acid sequence homology (77% homology in the extracellular domain and 93% homology in the cytoplasmic domain). Although Ret does not bind GDNF ligands directly, the extracellular domain of Ret binds the GDNFGFRα complex with high affinity and is a potent GDNF antagonist in the presence of soluble GFRα.

748.5 €

101-M621

Anti-Human SCF Antibody

Stem cell factor (SCF), also known as c-kit ligand (KL), mast cell growth factor (MGF), and steel factor (SLF), is a widely expressed 28 - 40 kDa type I transmembrane glycoprotein. It promotes the survival, differentiation, and mobilization of multiple cell types including myeloid, erythroid, megakaryocytic, lymphoid, germ cell, and melanocyte progenitors. SCF is a primary growth and activation factor for mast cells and eosinophils. Mature human SCF consists of a 189 amino acid (aa) extracellular domain (ECD), a 23 aa transmembrane segment, and a 36 aa cytoplasmic tail. The ECD shows both N-linked and O-linked glycosylation. Proteolytic cleavage at two alternate sites in the extracellular juxtamembrane region releases a 25 kDa soluble molecule which is comparable to the only form produced by Steel-dickie mutant mice. An alternately spliced isoform of human SCF lacks 28 aa that encompasses the primary proteolytic recognition site. Within the ECD of the short isoform (corresponding to this recombinant protein), human SCF shares 75 - 83% aa sequence identity with canine, feline, mouse, and rat SCF. Rat SCF is active on mouse and human cells, but human SCF is only weakly active on mouse cells. Noncovalent dimers of transmembrane or soluble SCF interact with the receptor tyrosine kinase SCF-R/c-kit to trigger receptor dimerization and signaling. SCF assists in the recovery of cardiac function following myocardial infarction by increasing the number of cardiomyocytes and vascular channels.

748.5 €