Other Proteins

Recombinant Human VCAM-1 (Legacy Tebubio ref. 167150-04). VCAM is a 110 kDa, cell surface integral membrane glycoprotein that belongs to the Ig-related superfamily of adhesion molecules. The primary function of VCAM-1 is the mediation of leukocyte-endothelial cell adhesion and signal transduction. VCAM-1 may play a vital role in the development of several diseases, including atherosclerosis and rheumatoid arthritis. The human VCAM-1 gene codes for a 715 amino acid transmembrane glycoprotein containing a 19 amino acid cytoplasmic domain, a 22 amino acid transmembrane domain, and a 674 amino acid extracellular domain. Recombinant Human VCAM-1 is a 74.1 kDa glycoprotein comprising the extracellular domain (674 amino acid residues) of VCAM-1. Monomeric glycosylated VCAM-1 migrates at an apparent molecular weight of approximately 90.0 kDa by SDS-PAGE analysis under reducing conditions.

Recombinant Human VCAM-1 (Legacy Tebubio ref. 167150-04). VCAM is a 110 kDa, cell surface integral membrane glycoprotein that belongs to the Ig-related superfamily of adhesion molecules. The primary function of VCAM-1 is the mediation of leukocyte-endothelial cell adhesion and signal transduction. VCAM-1 may play a vital role in the development of several diseases, including atherosclerosis and rheumatoid arthritis. The human VCAM-1 gene codes for a 715 amino acid transmembrane glycoprotein containing a 19 amino acid cytoplasmic domain, a 22 amino acid transmembrane domain, and a 674 amino acid extracellular domain. Recombinant Human VCAM-1 is a 74.1 kDa glycoprotein comprising the extracellular domain (674 amino acid residues) of VCAM-1. Monomeric glycosylated VCAM-1 migrates at an apparent molecular weight of approximately 90.0 kDa by SDS-PAGE analysis under reducing conditions.

Recombinant Human ICAM-1 (Legacy Tebubio ref. 167150-05). ICAMs are members of the Ig superfamily of calcium-independent transmembrane glycoproteins. ICAM-1 is a ligand for the lymphocyte function-associated antigen (LFA) and Mac-1 integrins, as well as the major human rhinovirus receptor. The primary function of ICAM-1 is to provide adhesion between endothelial cells and leukocytes after stress or injury. The human ICAM-1 gene codes for a 505 amino acid transmembrane glycoprotein containing a 29 amino acid cytoplasmic domain, a 23 amino acid transmembrane domain, and a 453 amino acid extracellular domain. Recombinant Human ICAM-1 is a 49.5 kDa glycoprotein comprising the extracellular domain (453 amino acid residues) of ICAM-1. Monomeric glycosylated ICAM-1 migrates at an apparent molecular weight of approximately 72.0-80.0 kDa by SDS-PAGE analysis under reducing conditions.

Recombinant Human ICAM-1 (Legacy Tebubio ref. 167150-05). ICAMs are members of the Ig superfamily of calcium-independent transmembrane glycoproteins. ICAM-1 is a ligand for the lymphocyte function-associated antigen (LFA) and Mac-1 integrins, as well as the major human rhinovirus receptor. The primary function of ICAM-1 is to provide adhesion between endothelial cells and leukocytes after stress or injury. The human ICAM-1 gene codes for a 505 amino acid transmembrane glycoprotein containing a 29 amino acid cytoplasmic domain, a 23 amino acid transmembrane domain, and a 453 amino acid extracellular domain. Recombinant Human ICAM-1 is a 49.5 kDa glycoprotein comprising the extracellular domain (453 amino acid residues) of ICAM-1. Monomeric glycosylated ICAM-1 migrates at an apparent molecular weight of approximately 72.0-80.0 kDa by SDS-PAGE analysis under reducing conditions.

Recombinant Human PECAM-1 (Legacy Tebubio ref. 167150-06). PECAM is transmembrane glycoprotein that belongs to the Ig-related superfamily of adhesion molecules. It is highly expressed at endothelial cell junctions, and is also expressed in platelets and most leukocyte sub-types. The primary function of PECAM-1 is the mediation of leukocyte-endothelial cell adhesion and signal transduction. PECAM-1 has been implicated in the pathogenesis of various inflammation-related disorders, including thrombosis, multiple sclerosis (MS), and rheumatoid arthritis. The human PECAM-1 gene codes for a 738 amino acid transmembrane glycoprotein that contains a 118 amino acid cytoplasmic domain, a 19 amino acid transmembrane domain, and a 574 amino acid extracellular domain. Recombinant Human PECAM-1 is a 572 amino acid glycoprotein comprising the extracellular domain of PECAM-1. Monomeric glycosylated PECAM-1 migrates at an apparent molecular weight of approximately 80.0-95.0 kDa by SDS-PAGE analysis und

Recombinant Human PECAM-1 (Legacy Tebubio ref. 167150-06). PECAM is transmembrane glycoprotein that belongs to the Ig-related superfamily of adhesion molecules. It is highly expressed at endothelial cell junctions, and is also expressed in platelets and most leukocyte sub-types. The primary function of PECAM-1 is the mediation of leukocyte-endothelial cell adhesion and signal transduction. PECAM-1 has been implicated in the pathogenesis of various inflammation-related disorders, including thrombosis, multiple sclerosis (MS), and rheumatoid arthritis. The human PECAM-1 gene codes for a 738 amino acid transmembrane glycoprotein that contains a 118 amino acid cytoplasmic domain, a 19 amino acid transmembrane domain, and a 574 amino acid extracellular domain. Recombinant Human PECAM-1 is a 572 amino acid glycoprotein comprising the extracellular domain of PECAM-1. Monomeric glycosylated PECAM-1 migrates at an apparent molecular weight of approximately 80.0-95.0 kDa by SDS-PAGE analysis und

Recombinant Human Slit2-N (Legacy Tebubio ref. 167150-11). Slit2 is a member of the Slit family that signals through the Roundabout (Robo) receptor as a repellent for axon guidance and neuronal migration, and also acts as a chemoattractant to vascular endothelial cells and a chemotaxis inhibitor for leukocytes. Slit2 is expressed primarily in the fetal lung, kidney, and adult spinal cord, and to a lesser extent in the adult adrenal gland, thyroid and trachea. Slit2 is initially synthesized as a 1499 amino acid precursor, which is subsequently cleaved into N-terminal and C-terminal fragments, designated as Slit2-N and Slit2-C respectively. The neurodevelopment-related activities, as measured by the ability to repel olfactory bulb axons and to induce branching in dorsal root ganglia axons, are contained only in the N-terminal fragment. Recombinant Human Slit2-N is a 1093 amino acid glycoprotein corresponding to the N-terminal portion of the full length Slit2 precursor, and has a calculat

Recombinant Human Slit2-N (Legacy Tebubio ref. 167150-11). Slit2 is a member of the Slit family that signals through the Roundabout (Robo) receptor as a repellent for axon guidance and neuronal migration, and also acts as a chemoattractant to vascular endothelial cells and a chemotaxis inhibitor for leukocytes. Slit2 is expressed primarily in the fetal lung, kidney, and adult spinal cord, and to a lesser extent in the adult adrenal gland, thyroid and trachea. Slit2 is initially synthesized as a 1499 amino acid precursor, which is subsequently cleaved into N-terminal and C-terminal fragments, designated as Slit2-N and Slit2-C respectively. The neurodevelopment-related activities, as measured by the ability to repel olfactory bulb axons and to induce branching in dorsal root ganglia axons, are contained only in the N-terminal fragment. Recombinant Human Slit2-N is a 1093 amino acid glycoprotein corresponding to the N-terminal portion of the full length Slit2 precursor, and has a calculat

Recombinant Human E-Selectin (Legacy Tebubio ref. 167150-15). Selectins are a family of calcium-dependent type 1 transmembrane proteins. Endothelial (E)-selectin is a heavily glycosylated transmembrane protein expressed by activated endothelial cells in microvascular linings. E-selectin, along with P-selectin and L-selectin, initiate recruitment of circulating leukocytes from blood to sites of inflammation in the vascular lining through interaction with specific cell surface-associated carbohydrate determinants. E-selectin consists of an N-terminal type 1 lectin domain, an EGF-like domain, 6 sushi (CCP/SCR) domains, a transmembrane sequence, and a short cytoplasmic domain. Recombinant Human E-selectin is a 58.6 kDa protein containing 535 amino acid residues, corresponding to the extracellular portion of the full length protein. Due to glycosylation, E-selectin migrates at an apparent molecular weight of approximately 65-85 kDa by SDS-PAGE analysis under reducing conditions.