"Test Lead"

Supplier: Rockland Immunochemical

Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR6 was first identified as a close homolog of TLR1, sharing 69% sequence identify. Like TLR1, TLR6 can form heterodimers with TLR2, and these TLR6:TLR2 dimers coordinate macrophage activation by Gram-positive bacteria and the yeast cell wall particle zymosan. Activation of these complexes not only initiates pro-inflammatory cascades, but also can lead to apoptotic responses.

Supplier: Rockland Immunochemical

Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR6 was first identified as a close homolog of TLR1, sharing 69% sequence identify. Like TLR1, TLR6 can form heterodimers with TLR2, and these TLR6:TLR2 dimers coordinate macrophage activation by Gram-positive bacteria and the yeast cell wall particle zymosan. Activation of these complexes not only initiates pro-inflammatory cascades, but also can lead to apoptotic responses.

Supplier: Rockland Immunochemical

The human uracil-DNA glycosylase (UNG) gene encodes both mitochondrial (UNG1) and nuclear (UNG2) forms through differentially regulated promotes and alternative splicing. While UNG2 is the major enzyme in the base excision repair pathway that removes uracil residues from nuclear DNA that arise through either misincorporation during replication or cytosine deamination, inhibition of UNG1 by uracil glycosylase inhibitor did not lead to increased levels of spontaneous or induced mitochondrial DNA mutations. However, decreased levels of UNG activity and increased oxidative damage to mitochondrial DNA were seen in older mice, suggesting that mitochondrial DNA repair mechanisms may be involved in various neurodegenerative disorders in an age-dependent manner. This UNG1 antibody will not cross-react with UNG2.

Supplier: Thermo Fisher Scientific

This general purpose, semi-micro tipped combination electrode with top-performance glass body can be used for precise pH determinations in micro volume samples.

Supplier: Wards

Large, lightweight meters, ideal for classroom demonstrations.

Supplier: DRG International

An enzyme immunoassay for the quantitative measurement of total 5α-dihydrotestosterone (DHT) in serum or plasma.

Supplier: Prosci

The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR). The NMDAR plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death. Overexpression of the NR2B subunit of the receptor has been associated with increases in learning and memory while aged, memory impaired animals have deficiencies in NR2B expression. Tyr1472 on NR2B is phosphorylated and this may lead to the increased expression of the NMDAR at the synapse that plays a role in synaptic plasticity.

Supplier: Rockland Immunochemical

Glycoprotein VI (GP6) is a 58kD platelet membrane glycoprotein that plays a crucial role in the collagen-induced activation and aggregation of platelets. It is uniquely expressed by cells of the megakaryocytic/platelet lineage, and is a member of the immunoglobulin gene superfamily, closely related to Fc receptor gamma chain (FcRgamma) and natural killer receptors. Glycoprotein VI plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcRgamma, the Src kinases (likely Fyn/Lyn), the adapter protein LAT and leads to the activation of phospholipase C gamma2. GPVI deficiency can result in bleeding disorders. Further study should reveal the extent of GPVI involvement in thrombotic disease and allow the development of alternative anti-thrombotic compounds.

Supplier: Rockland Immunochemical

TANK was initially identified as a novel TRAF-interacting protein that regulated TRAF-mediated signal transduction. Specifically, ligand binding by surface receptors in the tumor necrosis factor (TNF) receptor and Toll/interleukin-1 (IL-1) receptor families lead to the formation of a TRAF/TANK complex that mediates the activation of the transcription factor NF-kB. This activation of NF-kB occurs through an association with the kinases IKKe and TBK1. More recently, it was shown that these proteins can then form a complex with NEMO, a protein that regulates the activity of the IkB complex. This suggests that in addition to the possibility that TBK1 and IKKe activate the IKKs, the association with the IKK complex may help these kinases modulate other functions, such as the transactivation potential of NF-kB proteins. At least two isoforms of TANK are known to exist.

Supplier: Rockland Immunochemical

Rho GTPases, which are activated by specific guanine-nucleotide exchange factors (GEFs), play pivotal roles in several cellular functions. TEM4, encoding a protein containing 1510 amino acids, contains a RhoGEF-specific Dbl homology (DH) domain but lacks their typical pleckstrin homology domain. TEM4 is a Rho-specific GEF with novel structural and regulatory properties and predominant expression in the heart. It couples tyrosine kinase signals with the activation of the rho/rac GTPases, thus leading to cell differentiation and/or proliferation. Elevated levels of TEM4, TEM5, TEM6, TEM7 and TEM7R were also raised in breast cancer tissues. TEM4 could also prove to be useful targets therapeutically.

Supplier: Rockland Immunochemical

Tumor necrosis factor receptor (TNFR) superfamily members are defined by cysteine-rich domains in their extracellular regions that bind TNF-related ligands that share a common structural homology in their extracellular domain. TNFRSF14 was initially identified as the Herpesvirus entry mediator and upon binding to the herpes simplex virus (HSV) envelope glycoprotein D or either of its natural ligands LIGHT and lymphotoxin alpha (LT), activates the transcription factors NF-kB and AP-1. Activation of this signal transduction pathway in T cells stimulates T cell proliferation and cytokine production, leading to inflammation and enhanced CTL-mediated tumor immunity, suggesting that these proteins may be useful as potential targets for controlling cellular immune responses.

Supplier: Rockland Immunochemical

The human uracil-DNA glycosylase (UNG) gene encodes both mitochondrial (UNG1) and nuclear (UNG2) forms through differentially regulated promotes and alternative splicing. While UNG2 is the major enzyme in the base excision repair pathway that removes uracil residues from nuclear DNA that arise through either misincorporation during replication or cytosine deamination, inhibition of UNG1 by uracil glycosylase inhibitor did not lead to increased levels of spontaneous or induced mitochondrial DNA mutations. However, decreased levels of UNG activity and increased oxidative damage to mitochondrial DNA were seen in older mice, suggesting that mitochondrial DNA repair mechanisms may be involved in various neurodegenerative disorders in an age-dependent manner. This UNG1 antibody will not cross-react with UNG2.

Supplier: Tonbo Biosciences

The Hit8a antibody is specific for the 32-34 kDa alpha chain of human CD8, known as CD8a or CD8 alpha. CD8a can form a homodimer (CD8 alpha-alpha), but is more commonly expressed as a heterodimer with a second chain known as CD8b or CD8 beta. CD8 acts as a co-receptor for antigen recognition and subsequent T cell activation that is initiated upon binding of the T cell receptor (TCR) to antigen-bearing MHC Class I molecules. The cytoplasmic domains of CD8 provide binding sites for the tyrosine kinase lck, facilitating intracellular signaling events that lead to T cell activation, development, and cytotoxic effector functions. CD8+ cytotoxic T cells (CTLs) play an important role in inducing cell death of tumor cells, as well as cells infected by virus, bacteria or parasites.

Supplier: Rockland Immunochemical

The PIAS proteins (protein inhibitor of activated STAT) play a crucial role as transcriptional coregulators in various cellular pathways, including the STAT, p53 and the steroid hormone signaling pathway. The PIAS protein family includes at least five evolutionarily conserved genes, including PIAS1. The major function of the PIAS proteins is the control of gene transcription and can also act as small ubiquitin-like-modifier (SUMO) E3 ligases. PIAS1 binds specifically to STAT1, inhibiting STAT1-mediated gene activation and also binds to the Gu/RNA helicase II enzyme, leading to the proteolytic cleavage of Gu/RH-II. PIAS1 is a potent co-activator for CP2c-mediated alpha-globin expression in erythroid cells.

Supplier: Tonbo Biosciences

The SK1 antibody is specific for the 32-34 kDa alpha chain of human CD8, known as CD8a or CD8 alpha. CD8a can form a homodimer (CD8 alpha-alpha), but is more commonly expressed as a heterodimer with a second chain known as CD8b or CD8 beta. CD8 acts as a co-receptor for antigen recognition and subsequent T cell activation that is initiated upon binding of the T cell receptor (TCR) to antigen-bearing MHC Class I molecules. The cytoplasmic domains of CD8 provide binding sites for the tyrosine kinase lck, facilitating intracellular signaling events that lead to T cell activation, development, and cytotoxic effector functions. CD8+ cytotoxic T cells (CTLs) play an important role in inducing cell death of tumor cells, as well as cells infected by virus, bacteria or parasites.

Supplier: Rockland Immunochemical

The receptor activator of NF-kB ligand (RANK-L) is a recently discovered member of the TNF-ligand family involved in the regulation of the T cell-dependent immune response, lymph node organogenesis and bone formation. RANK-L exists as both a normal, transmembrane form and a truncated, soluble form (sRANK-L), both of which can stimulate the receptor. Activation of T cells, such as by treatment with interleukin-7, induces RANK-L production and leads to an increase of osteoclast formation and bone loss. Finally, sRANK-L can activate the antiapoptotic kinase Akt through a signaling complex involving Src kinase and TRAF6, suggesting sRANK-L may also play a role in regulating apoptosis. This antibody will recognize both the soluble form and the uncleaved transmembrane form of RANK-L.