Other Proteins

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.

Recombinant Human VAP-1 (Legacy Tebubio ref. 167150-16). VAP-1 is a type II membrane cell adhesion protein belonging to the copper/topaquinone oxidase family. It is primarily expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. VAP-1 can catalyze the oxidative deamination of low molecular weight amines, and plays an important role in the migration of lymphocytes to inflamed tissue. Inhibition of VAP-1 can protect against inflammation-related damage to certain injured tissues. Additionally, VAP-1 can function as a significant prognostic marker for certain cancers and cardiovascular diseases. Recombinant Human VAP-1 is a mixture of monomeric and disulfide-linked homodimeric forms of a 737 amino acid polypeptide, corresponding to amino acids 27 to 763 of the VAP-1 precursor. The calculated molecular weight of Recombinant Human VAP-1 is 81.8 kDa.

Recombinant Human VAP-1 (Legacy Tebubio ref. 167150-16). VAP-1 is a type II membrane cell adhesion protein belonging to the copper/topaquinone oxidase family. It is primarily expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. VAP-1 can catalyze the oxidative deamination of low molecular weight amines, and plays an important role in the migration of lymphocytes to inflamed tissue. Inhibition of VAP-1 can protect against inflammation-related damage to certain injured tissues. Additionally, VAP-1 can function as a significant prognostic marker for certain cancers and cardiovascular diseases. Recombinant Human VAP-1 is a mixture of monomeric and disulfide-linked homodimeric forms of a 737 amino acid polypeptide, corresponding to amino acids 27 to 763 of the VAP-1 precursor. The calculated molecular weight of Recombinant Human VAP-1 is 81.8 kDa.

Recombinant Human Semaphorin 3A Fc (Legacy Tebubio ref. 167150-17H). Semaphorins are a large group of structurally-related, secreted, GPI-anchored, transmembrane, cell-signaling molecules. There are 8 major classifications of Semaphorins (the first seven ordered by number, 1-7, and the eighth designated V for virus), which are characterized by the existence of a conserved 500 amino acid SEMA domain at the amino terminus. Classes 3, 4, 6, and 7 are found in vertebrates only, whilst class 5 is found in both vertebrates and invertebrates. Each class is then divided into additional subgroups based on shared structural characteristics. Semaphorins primarily function as axon growth cone guidance factors during neuronal development. Semaphorin 3A acts as a chemo-repellent to axons, and an inhibitor of the growth of axons by signaling through receptors, Neuropilin-1 and Plexin-A. PeproTech's CHO cell-derived Recombinant Human Semaphorin 3A Fc is a glycosylated, disulfide-linked homodimer of

Recombinant Human Semaphorin 3A Fc (Legacy Tebubio ref. 167150-17H). Semaphorins are a large group of structurally-related, secreted, GPI-anchored, transmembrane, cell-signaling molecules. There are 8 major classifications of Semaphorins (the first seven ordered by number, 1-7, and the eighth designated V for virus), which are characterized by the existence of a conserved 500 amino acid SEMA domain at the amino terminus. Classes 3, 4, 6, and 7 are found in vertebrates only, whilst class 5 is found in both vertebrates and invertebrates. Each class is then divided into additional subgroups based on shared structural characteristics. Semaphorins primarily function as axon growth cone guidance factors during neuronal development. Semaphorin 3A acts as a chemo-repellent to axons, and an inhibitor of the growth of axons by signaling through receptors, Neuropilin-1 and Plexin-A. PeproTech's CHO cell-derived Recombinant Human Semaphorin 3A Fc is a glycosylated, disulfide-linked homodimer of

Recombinant Human Uteroglobin (Legacy Tebubio ref. 167150-18). Uteroglobin, which is a member of the Secretoglobin superfamily and is also known as Clara cell phospholipid-binding protein, is a multifunctional protein that can exert anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. The small, non-glycosylated protein named for its high levels of expression in pre-implantation embryos, where it exhibits growth stimulatory effects, is produced and secreted by the non-ciliated, non-mucous Clara cells predominant in the epithelial surfaces of pulmonary airways, as well as other non-ciliated epithelia. Members of the Secretoglobin superfamily demonstrate a high level of structural conservation and are characterized as small, secretory homo- or heterodimers. In addition to sequestering pro-inflammatory mediators and carcinogens, Uteroglobin has been implicated in the inhibition of cell migration and invasion, plate

Recombinant Human Uteroglobin (Legacy Tebubio ref. 167150-18). Uteroglobin, which is a member of the Secretoglobin superfamily and is also known as Clara cell phospholipid-binding protein, is a multifunctional protein that can exert anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. The small, non-glycosylated protein named for its high levels of expression in pre-implantation embryos, where it exhibits growth stimulatory effects, is produced and secreted by the non-ciliated, non-mucous Clara cells predominant in the epithelial surfaces of pulmonary airways, as well as other non-ciliated epithelia. Members of the Secretoglobin superfamily demonstrate a high level of structural conservation and are characterized as small, secretory homo- or heterodimers. In addition to sequestering pro-inflammatory mediators and carcinogens, Uteroglobin has been implicated in the inhibition of cell migration and invasion, plate

Recombinant Human TIM-3 Fc (Legacy Tebubio ref. 167150-20). T‐cell immunoglobulin mucin receptor 3 (TIM‐3), or HAVcr‐2, is a type I transmembrane receptor of the immunoglobulin superfamily involved in modulating innate and adaptive immune responses. TIM‐3 is expressed in T cells, including Th1, Th17, CD4+, CD8+, NK, and Tregs, as well as myeloid cells, including macrophages, monocytes and dendritic cells. TIM‐3 displays predominantly inhibitory functions, however recent studies have demonstrated stimulatory effects in select cell types. TIM‐3 is a relevant marker of T cell exhaustion and its expression directly correlates with chronic viral disease progression and tumor progression in a wide range of cancers. TIM‐3 expression is downregulated in autoimmune disorders such as MS, RA and psoriasis. Interaction of TIM‐3 and its ligands suppresses T cell responses and induces immune tolerance. Four ligands, Gal‐9, PtdSer, HMGB1, and Ceacam‐1, have been identified, each inducing distinct res

Recombinant Human TIM-3 Fc (Legacy Tebubio ref. 167150-20). T‐cell immunoglobulin mucin receptor 3 (TIM‐3), or HAVcr‐2, is a type I transmembrane receptor of the immunoglobulin superfamily involved in modulating innate and adaptive immune responses. TIM‐3 is expressed in T cells, including Th1, Th17, CD4+, CD8+, NK, and Tregs, as well as myeloid cells, including macrophages, monocytes and dendritic cells. TIM‐3 displays predominantly inhibitory functions, however recent studies have demonstrated stimulatory effects in select cell types. TIM‐3 is a relevant marker of T cell exhaustion and its expression directly correlates with chronic viral disease progression and tumor progression in a wide range of cancers. TIM‐3 expression is downregulated in autoimmune disorders such as MS, RA and psoriasis. Interaction of TIM‐3 and its ligands suppresses T cell responses and induces immune tolerance. Four ligands, Gal‐9, PtdSer, HMGB1, and Ceacam‐1, have been identified, each inducing distinct res