1521 Résultats pour : "single-use assemblies"

Supplier: ProSci Inc.

DIRC2 is a membrane-bound protein from the major facilitator superfamily of transporters. Disruption of DIRC2 by translocation has been associated with haplo-insufficiency and renal cell carcinomas. Alternatively spliced transcript variants have been described, but their biological validity has not yet been determined.This gene encodes a membrane-bound protein from the major facilitator superfamily of transporters. Disruption of this gene by translocation has been associated with haplo-insufficiency and renal cell carcinomas. Alternatively spliced transcript variants have been described, but their biological validity has not yet been determined. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence and transcripts to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Biotium

Human immunodeficiency virus (HIV) is a retrovirus that causes acquired immune deficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. HIV mainly infects vital cells in the human immune system such as helper T cells (specifically CD4 T cells), macrophages and dendritic cells. Two species of HIV infect humans: HIV-1 and HIV-2, with HIV-1 being the more virulent strain. The gag gene of human immunodeficiency virus 1 (HIV-1) encodes a precursor protein known as Pr55Gag. The viral protease PR cleaves this precursor to generate p17, p24, p7, and p6 proteins, which are required for virus particle assembly. HIV-1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV-1. p6 and p7 are the components of the nucleocapsid, and p17 provides a protective matrix. HIV-1 Gag p24 is indispensable to the reproduction of AIDS virus and constitutes an essential element for the AIDS virus particle construction. As this protein is detectable from the early stage of AIDS virus infection, its measurement is commonly used as an indicator of HIV-1 infection and viral load.

Supplier: Biotium

Human immunodeficiency virus (HIV) is a retrovirus that causes acquired immune deficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. HIV mainly infects vital cells in the human immune system such as helper T cells (specifically CD4 T cells), macrophages and dendritic cells. Two species of HIV infect humans: HIV-1 and HIV-2, with HIV-1 being the more virulent strain. The gag gene of human immunodeficiency virus 1 (HIV-1) encodes a precursor protein known as Pr55Gag. The viral protease PR cleaves this precursor to generate p17, p24, p7, and p6 proteins, which are required for virus particle assembly. HIV-1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV-1. p6 and p7 are the components of the nucleocapsid, and p17 provides a protective matrix. HIV-1 Gag p24 is indispensable to the reproduction of AIDS virus and constitutes an essential element for the AIDS virus particle construction. As this protein is detectable from the early stage of AIDS virus infection, its measurement is commonly used as an indicator of HIV-1 infection and viral load.

Supplier: STEMCELL Technologies

Stimulating T cells with HIV-1 (B Gag) peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. HIV-1 (B Gag) Peptide Pool is a lyophilised mixture of 123 peptides from the gag polyprotein of human immunodeficiency virus 1 (HIV-1). The pool consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 500 on gag polyprotein. The HIV-1 gag polyprotein is a key mediator of viral particle assembly (Campbell and Rein; Dong et al.), and together with the endosomal sorting complexes required for transport (ESCRT), results in budding during virion release (Carlson et al.). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Biotium

Human immunodeficiency virus (HIV) is a retrovirus that causes acquired immune deficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. HIV mainly infects vital cells in the human immune system such as helper T cells (specifically CD4 T cells), macrophages and dendritic cells. Two species of HIV infect humans: HIV-1 and HIV-2, with HIV-1 being the more virulent strain. The gag gene of human immunodeficiency virus 1 (HIV-1) encodes a precursor protein known as Pr55Gag. The viral protease PR cleaves this precursor to generate p17, p24, p7, and p6 proteins, which are required for virus particle assembly. HIV-1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV-1. p6 and p7 are the components of the nucleocapsid, and p17 provides a protective matrix. HIV-1 Gag p24 is indispensable to the reproduction of AIDS virus and constitutes an essential element for the AIDS virus particle construction. As this protein is detectable from the early stage of AIDS virus infection, its measurement is commonly used as an indicator of HIV-1 infection and viral load.

Supplier: Biotium

Human immunodeficiency virus (HIV) is a retrovirus that causes acquired immune deficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. HIV mainly infects vital cells in the human immune system such as helper T cells (specifically CD4 T cells), macrophages and dendritic cells. Two species of HIV infect humans: HIV-1 and HIV-2, with HIV-1 being the more virulent strain. The gag gene of human immunodeficiency virus 1 (HIV-1) encodes a precursor protein known as Pr55Gag. The viral protease PR cleaves this precursor to generate p17, p24, p7, and p6 proteins, which are required for virus particle assembly. HIV-1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV-1. p6 and p7 are the components of the nucleocapsid, and p17 provides a protective matrix. HIV-1 Gag p24 is indispensable to the reproduction of AIDS virus and constitutes an essential element for the AIDS virus particle construction. As this protein is detectable from the early stage of AIDS virus infection, its measurement is commonly used as an indicator of HIV-1 infection and viral load.

Supplier: Biotium

Human immunodeficiency virus (HIV) is a retrovirus that causes acquired immune deficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. HIV mainly infects vital cells in the human immune system such as helper T cells (specifically CD4 T cells), macrophages and dendritic cells. Two species of HIV infect humans: HIV-1 and HIV-2, with HIV-1 being the more virulent strain. The gag gene of human immunodeficiency virus 1 (HIV-1) encodes a precursor protein known as Pr55Gag. The viral protease PR cleaves this precursor to generate p17, p24, p7, and p6 proteins, which are required for virus particle assembly. HIV-1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV-1. p6 and p7 are the components of the nucleocapsid, and p17 provides a protective matrix. HIV-1 Gag p24 is indispensable to the reproduction of AIDS virus and constitutes an essential element for the AIDS virus particle construction. As this protein is detectable from the early stage of AIDS virus infection, its measurement is commonly used as an indicator of HIV-1 infection and viral load.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Tonbo Biosciences

The SK7 antibody is specific for human CD3e, also known as CD3 epsilon, a 20 kDa subunit of the T cell receptor complex, along with CD3 gamma and CD3 delta. These integral membrane protein chains assemble with additional chains of the T cell receptor (TCR), as well as CD3 zeta chain, to form the T cell receptor - CD3 complex. Together with co-receptors CD4 or CD8, the complex serves to recognize antigens bound to MHC molecules on antigen-presenting cells. These interactions promote T cell receptor signaling (T cell activation), inducing cell proliferation, differentiation, production of cytokines or activation-induced cell death. CD3 is differentially expressed during thymocyte-to-T cell development and on all mature T cells. The SK7 antibody is a widely used phenotypic marker for human T cells. This antibody may induce T cell activation in the presence of monocytes. The antibody has also been demonstrated to be cross-reactive with Chimpanzee CD3. Binding of clone SK7 can be blocked by an alternative Anti-Human CD3 clone, OKT3. Please choose the appropriate format for each application.

Supplier: Biotium

Human immunodeficiency virus (HIV) is a retrovirus that causes acquired immune deficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. HIV mainly infects vital cells in the human immune system such as helper T cells (specifically CD4 T cells), macrophages and dendritic cells. Two species of HIV infect humans: HIV-1 and HIV-2, with HIV-1 being the more virulent strain. The gag gene of human immunodeficiency virus 1 (HIV-1) encodes a precursor protein known as Pr55Gag. The viral protease PR cleaves this precursor to generate p17, p24, p7, and p6 proteins, which are required for virus particle assembly. HIV-1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV-1. p6 and p7 are the components of the nucleocapsid, and p17 provides a protective matrix. HIV-1 Gag p24 is indispensable to the reproduction of AIDS virus and constitutes an essential element for the AIDS virus particle construction. As this protein is detectable from the early stage of AIDS virus infection, its measurement is commonly used as an indicator of HIV-1 infection and viral load.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Biotium

Human immunodeficiency virus (HIV) is a retrovirus that causes acquired immune deficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. HIV mainly infects vital cells in the human immune system such as helper T cells (specifically CD4 T cells), macrophages and dendritic cells. Two species of HIV infect humans: HIV-1 and HIV-2, with HIV-1 being the more virulent strain. The gag gene of human immunodeficiency virus 1 (HIV-1) encodes a precursor protein known as Pr55Gag. The viral protease PR cleaves this precursor to generate p17, p24, p7, and p6 proteins, which are required for virus particle assembly. HIV-1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV-1. p6 and p7 are the components of the nucleocapsid, and p17 provides a protective matrix. HIV-1 Gag p24 is indispensable to the reproduction of AIDS virus and constitutes an essential element for the AIDS virus particle construction. As this protein is detectable from the early stage of AIDS virus infection, its measurement is commonly used as an indicator of HIV-1 infection and viral load.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal ?crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: ProSci Inc.

Cell adhesion molecule 1(CADM1) is a single-pass type I membrane protein and belongs to the nectin family. It contains 2 Ig-like C2-type (immunoglobulin-like) domains and 1 Ig-like V-type (immunoglobulin-like) domain. CADM1 acts as a tumor suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction with CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM3 in vivo. CADM1 may contribute to the less invasive phenotypes of lepidic growth tumor cells. In mast cells, it may mediate attachment to and promote communication with nerves. CADM1, together with MITF, is essential for development and survival of mast cells in vivo. The protein acts as a synaptic cell adhesion molecule and plays a role in the formation of dendritic spines and in synapse assembly. It may be involved in neuronal migration, axon growth, pathfinding, and fasciculation on the axons of differentiating neurons. CADM1 may play diverse roles in the spermatogenesis including in the adhesion of spermatocytes and spermatids to Sertoli cells and for their normal differentiation into mature spermatozoa.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Biotium

Human immunodeficiency virus (HIV) is a retrovirus that causes acquired immune deficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. HIV mainly infects vital cells in the human immune system such as helper T cells (specifically CD4 T cells), macrophages and dendritic cells. Two species of HIV infect humans: HIV-1 and HIV-2, with HIV-1 being the more virulent strain. The gag gene of human immunodeficiency virus 1 (HIV-1) encodes a precursor protein known as Pr55Gag. The viral protease PR cleaves this precursor to generate p17, p24, p7, and p6 proteins, which are required for virus particle assembly. HIV-1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV-1. p6 and p7 are the components of the nucleocapsid, and p17 provides a protective matrix. HIV-1 Gag p24 is indispensable to the reproduction of AIDS virus and constitutes an essential element for the AIDS virus particle construction. As this protein is detectable from the early stage of AIDS virus infection, its measurement is commonly used as an indicator of HIV-1 infection and viral load.

Supplier: Bioss

The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the small HSPs, the immunophilins and the HSP 110 family. HSPB7 (heat shock 27kDa protein family, member 7), also known as cvHSP (cardiovascular heat shock protein) or Heat shock protein beta-7, is a member of the small HSP (sHSP) family expressed in heart and skeletal muscle. Members of the sHSP family contain a conserved C-terminal crystallin domain and typically function in homo- or heteromeric complexes. The sHSPs bind to denatured proteins and are responsible for preventing the aggregation of these proteins. In response to muscle fiber transformation and in muscular dystrophy, the expression levels of HSPB7 are drastically increased, suggesting that HSPB7 may be a useful target in therapeutic strategies for preventing age-related muscle wasting.

Supplier: Biotium

Human immunodeficiency virus (HIV) is a retrovirus that causes acquired immune deficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. HIV mainly infects vital cells in the human immune system such as helper T cells (specifically CD4 T cells), macrophages and dendritic cells. Two species of HIV infect humans: HIV-1 and HIV-2, with HIV-1 being the more virulent strain. The gag gene of human immunodeficiency virus 1 (HIV-1) encodes a precursor protein known as Pr55Gag. The viral protease PR cleaves this precursor to generate p17, p24, p7, and p6 proteins, which are required for virus particle assembly. HIV-1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV-1. p6 and p7 are the components of the nucleocapsid, and p17 provides a protective matrix. HIV-1 Gag p24 is indispensable to the reproduction of AIDS virus and constitutes an essential element for the AIDS virus particle construction. As this protein is detectable from the early stage of AIDS virus infection, its measurement is commonly used as an indicator of HIV-1 infection and viral load.

Supplier: Biotium

Human immunodeficiency virus (HIV) is a retrovirus that causes acquired immune deficiency syndrome (AIDS), a condition in humans in which the immune system begins to fail, leading to life-threatening opportunistic infections. HIV mainly infects vital cells in the human immune system such as helper T cells (specifically CD4 T cells), macrophages and dendritic cells. Two species of HIV infect humans: HIV-1 and HIV-2, with HIV-1 being the more virulent strain. The gag gene of human immunodeficiency virus 1 (HIV-1) encodes a precursor protein known as Pr55Gag. The viral protease PR cleaves this precursor to generate p17, p24, p7, and p6 proteins, which are required for virus particle assembly. HIV-1 Gag p24 is a capsid protein that constitutes the core of AIDS virus HIV-1. p6 and p7 are the components of the nucleocapsid, and p17 provides a protective matrix. HIV-1 Gag p24 is indispensable to the reproduction of AIDS virus and constitutes an essential element for the AIDS virus particle construction. As this protein is detectable from the early stage of AIDS virus infection, its measurement is commonly used as an indicator of HIV-1 infection and viral load.

Supplier: Tonbo Biosciences

The 3.9 antibody reacts with human CD11c, also known as integrin alpha X. This 150 kDa cell surface glycoprotein is part of a family of integrin receptors that mediate adhesion between cells (cell-cell) and components of the extracellular matrix, e.g. fibrinogen (cell-matrix). In addition, integrins are active signaling receptors which recruit leukocytes to inflammatory sites and promote cell activation. Complete, functional integrin receptors consist of distinct combinations of integrin chains which are differentially expressed. Integrin alpha X (CD11c) assembles with Integrin beta-2 (CD18) into a receptor known as CR4 which can bind and induce signaling through ICAMs and VCAM-1 on endothelial cells and can also facilitate removal of iC3b bearing foreign cells. The 3.9 antibody is widely used as a marker for CD11c expression on dendritic cells (DC), often in parallel with markers for CD11b, for identification of developmental stages and mature subsets of this cell type. CD11c is prominently expressed on tissue macrophages, and is also detected on activated neutrophils, granulocytes, some types of activated T cells and intestinal intraepithelial lymphocytes (IEL). The antibody is reported to be cross-reactive with Baboon, Chimpanzee, Cynomolgus and Rhesus CD11c.

Supplier: STEMCELL Technologies

Stimulating T cells with HPV18 (L2) peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. A lyophilised mixture of 113 peptides from minor capsid protein L2 of human papillomavirus type 18 (HPV18), HPV18 (L2) peptide pool consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 462 on L2. With two nuclear localization signals, L2 may enter the nuclei of host cells via several import pathways mediated by Kap α2β1 heterodimers, Kap β2, and Kap β (Klucevsek et al.). L2 can also assemble into virus-like particles, and may have a role in encapsidation (Stauffer et al.). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

Supplier: ProSci Inc.

GGTL3 is an enzymes involved in both the metabolism of glutathione and in the transpeptidation of amino acids. Changes in the activity of gamma-glutamyltransferase may signal preneoplastic or toxic conditions in the liver or kidney. GGTL3 consists of a heavy and a light chain, and it can interact with CT120, a plasma membrane-associated protein that is possibly involved in lung carcinogenesis.This gene is a member of a gene family that encodes enzymes involved in both the metabolism of glutathione and in the transpeptidation of amino acids. Changes in the activity of gamma-glutamyltransferase may signal preneoplastic or toxic conditions in the liver or kidney. The protein encoded by this gene consists of a heavy and a light chain, and it can interact with CT120, a plasma membrane-associated protein that is possibly involved in lung carcinogenesis. Sequence Note: This RefSeq record was created from transcript and genomic sequence data to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on transcript alignments.