Description: A competitive ELISA for quantitative measurement of Canine True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Canine True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: DC-SIGN Monoclonal Antibody: Dendritic cells (DCs) that control immune responses were recently found to capture and transport HIV from the mucosal area to remote lymph nodes, where DCs hand over HIV to CD4+ T lymphocytes. DCs also amplify the amount of virus and extend the duration of viral infectivity. Multiple strains of HIV-1, HIV-2 and SIV bind to DCs via DC-SIGN. ICAM-3 is the natural ligand for DC-SIGN. A DC-SIGN homologue (termed DC-SIGNR, L-SIGN, and DC-SIGN2) was identified recently. DC-SIGN forms a novel gene family with DC-SIGNR and many alternatively spliced isoforms of DC-SIGN and DC-SIGNR are known to exisit. The expression of DC-SIGN was found in mucosal tissues including placenta, small intestine, and rectum.

Description: DC-SIGN Monoclonal Antibody: Dendritic cells (DCs) that control immune responses were recently found to capture and transport HIV from the mucosal area to remote lymph nodes, where DCs hand over HIV to CD4+ T lymphocytes. DCs also amplify the amount of virus and extend the duration of viral infectivity. Multiple strains of HIV-1, HIV-2 and SIV bind to DCs via DC-SIGN. ICAM-3 is the natural ligand for DC-SIGN. A DC-SIGN homologue (termed DC-SIGNR, L-SIGN, and DC-SIGN2) was identified recently. DC-SIGN forms a novel gene family with DC-SIGNR and many alternatively spliced isoforms of DC-SIGN and DC-SIGNR are known to exisit. The expression of DC-SIGN was found in mucosal tissues including placenta, small intestine, and rectum.

Description: XBP-1 Monoclonal Antibody: X box binding protein 1 (XBP-1) is a key protein in the mammalian unfolded protein response (UPR) that protects the cell against the stress of malfolded proteins in the endoplasmic reticulum (ER). Upon sensing unfolded proteins, an ER transmembrane endonuclease and kinase termed IRE1p is activated and excises an intron from XBP-1 mRNA. The spliced XBP-1 mRNA results in a 371 amino acid protein (XBP-1s) which is then translocated to the nucleus where it binds to the regulatory elements of downstream genes. Together with other UPR transcription factors such as ATF6, XBP-1 stimulates the production of ER stress proteins including the ER resident protein chaperones glucose regulated protein (GRP) 78 and GRP94.

Description: XBP-1 Monoclonal Antibody: X box binding protein 1 (XBP-1) is a key protein in the mammalian unfolded protein response (UPR) that protects the cell against the stress of malfolded proteins in the endoplasmic reticulum (ER). Upon sensing unfolded proteins, an ER transmembrane endonuclease and kinase termed IRE1p is activated and excises an intron from XBP-1 mRNA. The spliced XBP-1 mRNA results in a 371 amino acid protein (XBP-1s) which is then translocated to the nucleus where it binds to the regulatory elements of downstream genes. Together with other UPR transcription factors such as ATF6, XBP-1 stimulates the production of ER stress proteins including the ER resident protein chaperones glucose regulated protein (GRP) 78 and GRP94.

Description: TIGIT Antibody: The T cell immunoreceptor with Ig and ITIM domains (TIGIT) is a member of the PVR (poliovirus receptor) family of immunoglobin proteins. It is expressed on several classes of T cells including follicular B helper T cells (TFH). TIGIT has been shown to bind PVR with high affinity; this binding is thought to assist interactions between TFH and dendritic cells to regulate T cell dependent B cell responses (1). Similar to other immune checkpoint proteins such as PD-1, TIGIT is upregulated on exhausted T cells in chronic viral infections and cancer. Blockade of both TIGIT and PD-1 pathways leads to tumor rejection in mice suggesting that it may be of therapeutic use against cancer (2).

Description: TIGIT Antibody: The T cell immunoreceptor with Ig and ITIM domains (TIGIT) is a member of the PVR (poliovirus receptor) family of immunoglobin proteins. It is expressed on several classes of T cells including follicular B helper T cells (TFH). TIGIT has been shown to bind PVR with high affinity; this binding is thought to assist interactions between TFH and dendritic cells to regulate T cell dependent B cell responses (1). Similar to other immune checkpoint proteins such as PD-1, TIGIT is upregulated on exhausted T cells in chronic viral infections and cancer. Blockade of both TIGIT and PD-1 pathways leads to tumor rejection in mice suggesting that it may be of therapeutic use against cancer (2).

Description: CD137 is a member of the tumor necrosis factor (TNF) receptor family. This receptor contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.

Description: ORAI3 Monoclonal Antibody: Antigen stimulation of immune cells triggers Ca++ entry t hrough Ca++ release-activated Ca++ (CRAC) channels. ORAI3 is one of two mammalian homologs to ORAI1, a recently identified four-transmembrane spanning protein that is an essential component of CRAC. All three homologs have been shown to function as Ca++ plasma membrane channels gated through interactions with STIM1, the store-activated endoplasmic reticulum Ca++ sensor. However, ORAI3 channels failed to produce detectable Ca++ selective currents in cells co-transfected with ORAI3 and STIM1, indicating that ORAI3 channels undergo a lesser degree of depotentiation than ORAI1 or ORAI2. Na+ currents through ORAI1, 2 and 3 channels were equally inhibited by extracellular Ca++, indicating that each have similar affinities for Ca++ within the selectivity filter. This antibody is predicted to have no cross-reactivity to ORAI1 or ORAI2. Larger molecular weight bands are sometimes seen in SDS-PAGE; these may represent post-translationally modified ORAI 3.

Description: ORAI3 Monoclonal Antibody: Antigen stimulation of immune cells triggers Ca++ entry t hrough Ca++ release-activated Ca++ (CRAC) channels. ORAI3 is one of two mammalian homologs to ORAI1, a recently identified four-transmembrane spanning protein that is an essential component of CRAC. All three homologs have been shown to function as Ca++ plasma membrane channels gated through interactions with STIM1, the store-activated endoplasmic reticulum Ca++ sensor. However, ORAI3 channels failed to produce detectable Ca++ selective currents in cells co-transfected with ORAI3 and STIM1, indicating that ORAI3 channels undergo a lesser degree of depotentiation than ORAI1 or ORAI2. Na+ currents through ORAI1, 2 and 3 channels were equally inhibited by extracellular Ca++, indicating that each have similar affinities for Ca++ within the selectivity filter. This antibody is predicted to have no cross-reactivity to ORAI1 or ORAI2. Larger molecular weight bands are sometimes seen in SDS-PAGE; these may represent post-translationally modified ORAI 3.

Description: LIGHT Antibody: LIGHT, also known as Tumor Necrosis Factor Superfamily member 14 (TNFSF14), is a co-stimulatory molecule that can regulate T-cell activation (1) and has recently been identified as an immune checkpoint protein. LIGHT binds to two different receptors, Herpes Virus Entry Mediator (HVEM) and Lymphotoxin beta Receptor (LTβR). While LIGHT binding to HVEM delivers a co-stimulatory signal to T cells (1), LIGHT binding to LTβR is critical for the formation of lymphoid structures which can stimulate T cell infiltration and activation of a tumor microenvironment, leading to rapid T cell-mediated tissue destruction (2). It has been shown that targeted delivery of LIGHT to tumors, thereby causing the T cell infiltration of the tumor, can enhance the response of the PD-1/PD-L1 checkpoint blockade anti-cancer therapy (3), suggesting that LIGHT may become a potent tool in anti-cancer treatment.

Description: LIGHT Antibody: LIGHT, also known as Tumor Necrosis Factor Superfamily member 14 (TNFSF14), is a co-stimulatory molecule that can regulate T-cell activation (1) and has recently been identified as an immune checkpoint protein. LIGHT binds to two different receptors, Herpes Virus Entry Mediator (HVEM) and Lymphotoxin beta Receptor (LTβR). While LIGHT binding to HVEM delivers a co-stimulatory signal to T cells (1), LIGHT binding to LTβR is critical for the formation of lymphoid structures which can stimulate T cell infiltration and activation of a tumor microenvironment, leading to rapid T cell-mediated tissue destruction (2). It has been shown that targeted delivery of LIGHT to tumors, thereby causing the T cell infiltration of the tumor, can enhance the response of the PD-1/PD-L1 checkpoint blockade anti-cancer therapy (3), suggesting that LIGHT may become a potent tool in anti-cancer treatment.

Description: LIGHT Antibody: LIGHT, also known as Tumor Necrosis Factor Superfamily member 14 (TNFSF14), is a co-stimulatory molecule that can regulate T-cell activation (1) and has recently been identified as an immune checkpoint protein. LIGHT binds to two different receptors, Herpes Virus Entry Mediator (HVEM) and Lymphotoxin beta Receptor (LTβR). While LIGHT binding to HVEM delivers a co-stimulatory signal to T cells (1), LIGHT binding to LTβR is critical for the formation of lymphoid structures which can stimulate T cell infiltration and activation of a tumor microenvironment, leading to rapid T cell-mediated tissue destruction (2). It has been shown that targeted delivery of LIGHT to tumors, thereby causing the T cell infiltration of the tumor, can enhance the response of the PD-1/PD-L1 checkpoint blockade anti-cancer therapy (3), suggesting that LIGHT may become a potent tool in anti-cancer treatment.

Description: LIGHT Antibody: LIGHT, also known as Tumor Necrosis Factor Superfamily member 14 (TNFSF14), is a co-stimulatory molecule that can regulate T-cell activation (1) and has recently been identified as an immune checkpoint protein. LIGHT binds to two different receptors, Herpes Virus Entry Mediator (HVEM) and Lymphotoxin beta Receptor (LTβR). While LIGHT binding to HVEM delivers a co-stimulatory signal to T cells (1), LIGHT binding to LTβR is critical for the formation of lymphoid structures which can stimulate T cell infiltration and activation of a tumor microenvironment, leading to rapid T cell-mediated tissue destruction (2). It has been shown that targeted delivery of LIGHT to tumors, thereby causing the T cell infiltration of the tumor, can enhance the response of the PD-1/PD-L1 checkpoint blockade anti-cancer therapy (3), suggesting that LIGHT may become a potent tool in anti-cancer treatment.

Description: LIGHT Antibody: LIGHT, also known as Tumor Necrosis Factor Superfamily member 14 (TNFSF14), is a co-stimulatory molecule that can regulate T-cell activation (1) and has recently been identified as an immune checkpoint protein. LIGHT binds to two different receptors, Herpes Virus Entry Mediator (HVEM) and Lymphotoxin beta Receptor (LTβR). While LIGHT binding to HVEM delivers a co-stimulatory signal to T cells (1), LIGHT binding to LTβR is critical for the formation of lymphoid structures which can stimulate T cell infiltration and activation of a tumor microenvironment, leading to rapid T cell-mediated tissue destruction (2). It has been shown that targeted delivery of LIGHT to tumors, thereby causing the T cell infiltration of the tumor, can enhance the response of the PD-1/PD-L1 checkpoint blockade anti-cancer therapy (3), suggesting that LIGHT may become a potent tool in anti-cancer treatment.