New Antibodies from Ximbio

This fungal endo-glycosidase (ENGase) from Trichoderma viride will release “Man5GlcNAc to Man9GlcNAc oligosaccharides from RNase B, ManGlcNAc, Man3GlcNAc, Man5GlcNAc, Man6GlcNAc and Man8GlcNAc from ovalbumin, and high-mannose and oligomannose structures from yeast invertase.”1 However, this enzyme will “not act on fucosylated, hybrid, complex-type or bisecting N-acetyl-glucosamine-containing N-linked oligosaccharide structures from ovalbumin, IgG and fetuin.”1 The exclusive preference of this enzyme “for high mannose type oligosaccharides without substitutions is in contrast to the bacterial ENGases, Endo H and Endo F1, which additionally cleave hybrid structures, and also tolerate fucosylation in the case of Endo H.”1 This enzyme has an ~Mr of 35 kDa as determined by SDS-PAGE. 

PMID: 11342414 , 9763568.

CD11A encodes the integrin alpha L chain. Integrins are heterodimeric integral membrane proteins composed of alpha and beta chains. This L-domain containing alpha integrin combines with the beta 2 chain to form the integrin lymphocyte function-associated antigen-1 expressed on all leukocytes and this plays a central role in leukocyte intercellular adhesion through interactions with its ligands.

Reactivity: E.coli

E.coli BirA is a well-characterized multifunctional protein that either catalyses the transfer of biotin to biotin carboxyl carrier protein (BCCP), a acetyl-CoA carboxylase subunit or, alternatively, binds to the biotin operator resulting in transcriptional repression of the biotin operon. A mutant BirA (R118G) shows loss of DNA binding ability and promiscuity of substrate biotinylation. These properties of BirA R118G were used to develop an in vivo proximity labelling technique that identifies potential interacting proteins (BioID). In the BioID method, a protein of interest is tagged with BirA R118G and expressed in live cells. Addition of the biotin to the culture medium results in biotinylation of proteins in vicinity of the bait. The biotinylated proteins can then be affinity purified with biotin binding proteins such as strepavidin or avidin even under harsh denaturing conditions and subsequently identified by mass spectrometry or immunoblot analysis.

Reactivity: Human
A notable feature of metazoan cells is their morphological plasticity associated with acquisition of a range of complex activities. Implementation of numerous specialized functions during differentiation is dependent upon the rearrangement and transformation of organelles, including the cell nucleus. Crucial to many cell specific changes in nuclear localization and organization is establishment of connections between the nucleus and cytoskeleton. Such connections are formed in part by KASH-domain proteins of the outer nuclear membrane (ONM). In mammals six KASH proteins are known (Nesprins 1, 2, 3, 4, LRMP and KASH5). Appropriate localization of KASH proteins is dependent upon tethering in the ONM by SUN-domain proteins of the inner nuclear membrane. Together, SUN-KASH pairs form LINC complexes (LInker of the Nucleoskeleton and Cytoskeleton) that span both nuclear membranes and which couple nuclear structures to the cytoskeleton. In recent years it has become apparent that LINC complex defects may contribute to a number of human genetic diseases, including muscular dystrophy, cerebellar ataxia, hearing loss and infertility.

A notable feature of metazoan cells is their morphological plasticity associated with acquisition of a range of complex activities. Implementation of numerous specialized functions during differentiation is dependent upon the rearrangement and transformation of organelles, including the cell nucleus. Crucial to many cell specific changes in nuclear localization and organization is establishment of connections between the nucleus and cytoskeleton. Such connections are formed in part by KASH-domain proteins of the outer nuclear membrane (ONM). In mammals six KASH proteins are known (Nesprins 1, 2, 3, 4, LRMP and KASH5). Appropriate localization of KASH proteins is dependent upon tethering in the ONM by SUN-domain proteins of the inner nuclear membrane. Together, SUN-KASH pairs form LINC complexes (LInker of the Nucleoskeleton and Cytoskeleton) that span both nuclear membranes and which couple nuclear structures to the cytoskeleton. In recent years it has become apparent that LINC complex defects may contribute to a number of human genetic diseases, including muscular dystrophy, cerebellar ataxia, hearing loss and infertility.

Carcinoembryonic antigen related cell adhesion molecules (CEACAM) (CD66a) belong to the immunoglobulin superfamily. They are highly glycosylated proteins with the typical N-terminal variable Ig-like domain followed by 0-6 constant Ig-like domains. A hydrophobic transmembrane domain with a cytoplasmic tail anchors CEACAM1 to the cell membrane. CEACAM1 is known as an epithelial tumour suppressor and an angiogenic growth factor.

Carcinoembryonic antigen related cell adhesion molecules (CEACAM) (CD66a) belong to the immunoglobulin superfamily. They are highly glycosylated proteins with the typical N-terminal variable Ig-like domain followed by 0-6 constant Ig-like domains. A hydrophobic transmembrane domain with a cytoplasmic tail anchors CEACAM1 to the cell membrane. CEACAM1 is known as an epithelial tumour suppressor and an angiogenic growth factor.

LH24 targets the basement membrane zone of keratinocytes, specifically Type VII Collagen non-collagenous domain 2. Type VII collagen and anchoring fibril deficiencies in skin biopsy samples were confirmed by immunofluorescence microscopy and immunoelectron microscopy using the LH24 antibody.

CEACAM8 is a glycosylphosphatidylinositol (GPI)-linked protein also known as CD67, CGM6, and NCA-95. CEACAM8 is a member of the immunoglobulin superfamily, carcinoembryonic antigen (CEA)-like subfamily. CEACAM8, expressed on granulocytes, has been reported to induce activation in neutrophils and to be involved in heterophilic adhesion with CEACAM6.