lymphoid

Expression system: E. coli
Length: 29-151, Full Length of Mature Protein
Activity: Not Tested

Iduronate 2-Sulfatase, also known as IDS, is a member of the highly conserved sulfatase family of enzymes that catalyze the hydrolysis of O- and N-sulfate esters from a variety of substrates. The human Iduronate 2-Sulfatase IDS consists of a signal peptide, a propeptide, and a mature chain that may be further processed into two chains. Among the identified 18 human sulfatases, Iduronate 2-Sulfatase IDS is required for the lysosomal degradation of the glycosaminoglycans (GAG), heparan sulfate, and dermatan sulfate. Multiple mutations in this X-chromosome localized gene result in Iduronate 2-Sulfatase IDS enzymatic deficiency and lead to the sex-linked Mucopolysaccharidosis Type II (MPS II ), also known as Hunter Syndrome characterized by the lysosomal accumulation of the GAG and their excretion in urine. MPS II has a wide spectrum of clinical manifestations ranging from mild to severe due to the level of Iduronate 2-Sulfatase IDS enzyme. Retroviral-mediated Iduronate 2-Sulfatase IDS gene transfer into lymphoid cells would be a promising gene therapeutic strategy.

Hematopoietic lineage cell-specific protein (HCLS1) is a protein that in humans is encoded by the HCLS1 gene. It is expressed only in tissues and cells of hematopoietic origin. It is substrate of the antigen receptor-coupled tyrosine kinase and plays a role in antigen receptor signaling for both clonal expansion and deletion in lymphoid cells. It may also be involved in the regulation of gene expression.

Expression system: Baculovirus Insect Cells
Length: 38-479, Partial
Activity: Not Tested

Expression system: E. coli
Length: 38-479, Partial
Activity: Not Tested

Expression system: E. coli
Length: 35-205, Full Length of Mature Protein
Activity: Cell Activity

RELA (v-rel reticuloendotheliosis viral oncogene homolog A), also known as Nuclear factor NF-kappa-B p65 subunit, or Transcription factor p65, is a transcription factor expressed in growth plate chondrocytes where it facilitates chondrogenesis. The v-rel avian reticuloendotheliosis viral oncogene homolog A (RELA) gene encodes the major component of the NF-?B complex. NF-kappaB is a generic name for an evolutionarily conserved transcription-factor system that contributes to the mounting of an effective immune response but is also involved in the regulation of cell proliferation, development, and apoptosis. The implication of NF-kappaB in central biological processes and its extraordinary connectivity to other signaling pathways raise a need for highly controlled regulation of NF-kappaB activity at several levels. The mammalian Rel NF-kappaB family of transcription factors, including RelA, c-Rel, RelB, NF-kappaB1 (p50 and its precursor p105), and NF-kappaB2 (p52 and its precursor p100), plays a central role in the immune system by regulating several processes ranging from the development and survival of lymphocytes and lymphoid organs to the control of immune responses and malignant transformation.

T-cell leukemia lymphoma protein 1A (abbreviated for TCL1A) is a member of the TCL1 family. TCL1 protooncogene is expressed in CD3-CD4-CD8-precursor T cells and is extinguished at the CD4+CD8+stage of thymocyte development. In B cells, TCL1 is first expressed in pro-B cells and remains high in naive mantle zone B cells of peripheral lymphoid tissues. The TCL1 protooncogene is overexpressed in many mature B cell lymphomas, especially from AIDS patients. It has been demonstrated that TCL1 is a powerful oncogene that, when overexpressed in both B and T cells, predominantly yields mature B cell lymphomas. All TCL1 isoforms bind to the Akt pleckstrin homology domain. Both in vitro and in vivo TCL1 increases Akt kinase activity and as a consequence enhances substrate phosphorylation. In vivo, TCL1 stabilizes the mitochondrial transmembrane potential and enhances cell proliferation and survival. It has been shown that TCL1 is a novel Akt kinase coactivator, which promotes Akt-induced cell survival and proliferation.

RGS1 (regulator of G-protein signaling 1) has been associated with multiple autoimmune disorders including type I diabetes. RGS1 desensitizes the chemokine receptors CCR7 and CXCR4 that are critical to the localization of T and B cells in lymphoid organs. RGS1 expression may be a prognostic marker for risk stratification and a promising target for the development of a new Multiple myeloma (MM) therapy. The markers in the RGS1 gene might be in linkage disequilibrium with a protective allele that reduces the risk of anxiety and depressive disorders.

Kit ligand, also known as Hematopoietic growth factor KL, Mast cell growth factor, Steel factor, Stem cell factor, c-Kit ligand, Kitlg and KITL, is a single-pass type I membrane protein that belongs to the SCF family. KITL kit ligand also belongs to the family of dimeric transmembrane growth factors. The soluble form of KIT ligand is a secreted protein. Mast cells are thought to participate in a variety of immune responses, such as parasite resistance and the allergic reaction. Mast cell development depends on stem cell factor (Kit ligand) and its receptor, c-Kit. KITL kit ligand stimulates the proliferation of mast cells. KITL kit ligand is able to augment the proliferation of both myeloid and lymphoid hematopoietic progenitors in bone marrow culture. Efficient cell surface presentation of KITL kit ligand is essential for the migration, proliferation, and survival of melanocytes, germ cells, hemopoietic stem cells, and mastocytes. KITL kit ligand acts synergistically with other cytokines, probably interleukins. KITL kit ligand plays a crucial role in the development and maintenance of the melanocyte lineage in adult skin. It exerts permanent survival, proliferation and migration functions in Kit receptor-expressing melanocytes. KITL kit ligand misexpression in some hyperpigmented lesions may open the avenue for Kitl-dependent treatment of pathological skin conditions.

Expression system: E. coli
Length: 78-235, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 32-215, Partial
Activity: BLI

Expression system: HEK293 Cells
Length: 22-225, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 26-281, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 26-177, Full Length of Mature Protein
Activity: BLI、Cells

Expression system: HEK293 Cells
Length: 39-207, Partial
Activity: Not Tested

Expression system: E. coli
Length: 151-450, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-270, Full Length
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 1-323, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 20-381, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1-244, Partial
Activity: Not Tested

Receptors for the Fc region of IgG (FcγR) are members of the Ig superfamily that function in the activation or inhibition of immune responses. Human FcγRs are divided into three classes designated FcγRI (CD64), FcγRII (CD32), and FcγRIII (CD16), which generate multiple isoforms, are recognized. The activating­ type receptor either has or associates non­covalently with an accessory subunit that has an immunoreceptor tyrosine­based activation motif (ITAM) in its cytoplasmic domain. FcγRI binds IgG with high affinity and functions during early immune responses, whereas FcγRII and RIII are low affinity receptors that recognize IgG as aggregates surrounding multivalent antigens during late immune responses. Three genes for human FcγRII (A, B, and C) and one for mouse (FcγRIIB), encoding type I transmembrane proteins with ITAM motifs (FcγRII A and C) or ITIM motifs (FcγRIIB) in their cytoplasmic domains, have been identified. Human CD32, also known as Low affinity immunoglobulin γ Fc region receptor II-a (IgG Fc receptor II-a), FcγRII A or FCGR2A Protein, is expressed on cells of both myeloid and lymphoid lineages as well as on cells of non-hematopoietic origin. Associated with an ITAM-bearing adapter subunit, FcRγ, CD32a (FcγRII A) delivers an activating signal upon ligand binding, and results in the initiation of inflammatory responses including cytolysis, phagocytosis, degranulation, and cytokine production. The responses can be modulated by signals from the co-expressed inhibitory receptors such as Fcγ RII B, and the strength of the signal is dependent on the ratio of expression of the activating and inhibitory receptors.

IL15RA is a high-affinity receptor for interleukin-15. Il15ra associates as a heterotrimer with the IL-2 receptor beta and gamma subunits to initiate signal transduction. It can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Il15ra is expressed in special cells including a wide variety of Tand B cells and non-lymphoid cells.IL-15 is a cytokine that regulates T cell and natural killer cell activation and proliferation. IL-15 binds to the alpha subunit of the IL-15RA with high affinity. IL-15 also binds to the beta and gamma chains of the IL-2 receptor, but not the alpha subunit of the IL2 receptor. IL-15 is structurally and functionally related to IL-2. Both cytokines share some subunits of receptors, allowing them to compete for and negatively regulate each other's activity. The number of CD8+ memory T cells is controlled by a balance between IL-15 and IL-2. Despite their many overlapping functional properties, IL-2 and IL-15 are, in fact, quite distinct players in the immune system. IL-15 is constitutively expressed by a wide variety of cell types and tissues, including monocytes, macrophages and DCs.

Macrophage receptor MARCO, also known as Macrophage receptor with collagenous structure and Marco, is a single-pass type II membrane protein. MARCO is a member of the class A scavenger receptor family and is part of the innate antimicrobial immune system. It is expressed in subpopulations of macrophages in the spleen and the medullary cord of lymph nodes. Although it is expressed on subsets of macrophages, it can be upregulated on other macrophages after bacterial infection. The strategic position of MARCO-expressing cells in lymphoid organs suggests an important role for this bacteria-binding molecule in the removal of pathogens. MARCO has a short N-terminal cytoplasmic domain, a transmembrane domain, and a large extracellular part composed of a 75-residue long spacer domain, a 27-residue collagenous domain, and a 99-residue long scavenger receptor cysteine-rich (SRCR) domain. It is possible that cooperation between the SRCR domain and the collagenous domain is needed for high-affinity bacterial binding, or that the SRCR domain has to be in a trimeric form to effectively bind to bacteria