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Catalog Number: (470222-119)
Supplier: NIELSEN-KELLERMAN CO
Description: The drop can be easily placed in the field and begin collecting environmental data.


Catalog Number: (CAPIPA5-12621)
Supplier: Thermo Scientific
Description: The protein encoded by this gene is a member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. In vitro, this kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites.


Catalog Number: (10408-928)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Catalog Number: (CA10820-448)
Supplier: Mettler Toledo
Description: The HC103 halogen moisture analyzer combines fast halogen heating with proven weighing technology to create a compact and durable instrument ideal for laboratory and production environments. Halogen heating element.


Catalog Number: (10081-936)
Supplier: Proteintech
Description: Annexin A2 (ANXA2), also named Annexin-2 or Lipocortin II, is a Ca2+ binding protein that is up-regulated in virally transformed cell lines and human tumors. This calcium-regulated membrane-binding protein, whose affinity for calcium is greatly enhanced by anionic phospholipids, may cross-link plasma membrane phospholipids with actin and the cytoskeleton and be involved with exocytosis. Heat-stress response may also involve Annexin-2.


Catalog Number: (10084-596)
Supplier: Proteintech
Description: CIRBP, also named as A18HNRNP and CIRP, is a cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. CIRBP is also involved in cap-independent translation upon moderate cold-shock. It acts as a translational activator. CIRBP is a suppressive rather stimulatory effect on proliferation. CIRBP can translocate from nucleus to cytoplasm under stresses such as UV irradation or heat shock. Suppression of CIRBP increased the apoptotic cell population of neural stem cells at moderate low temperature. This antibody (Catalog# 10209-2-AP) is a rabbit polyclonal antibody raised against the full-length CIRBP of human origin.


Supplier: Enzo Life Sciences
Description: Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye. Phosphorylation of serine residues which occurs during development and in response to stress, is intimately linked with its function. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation.

Catalog Number: (10366-700)
Supplier: Bioss
Description: The expression of DUSP1 gene is induced in human skin fibroblasts by oxidative/heat stress and growth factors. It specifies a protein with structural features similar to members of the non-receptor-type protein-tyrosine phosphatase family, and which has significant amino-acid sequence similarity to a Tyr/Ser-protein phosphatase encoded by the late gene H1 of vaccinia virus. The bacterially expressed and purified DUSP1 protein has intrinsic phosphatase activity, and specifically inactivates mitogen-activated protein (MAP) kinase in vitro by the concomitant dephosphorylation of both its phosphothreonine and phosphotyrosine residues.


Catalog Number: (10082-922)
Supplier: Proteintech
Description: Annexin A2 (ANXA2), also named Annexin-2 or Lipocortin II, is a Ca2+ binding protein that is up-regulated in virally transformed cell lines and human tumors. This calcium-regulated membrane-binding protein, whose affinity for calcium is greatly enhanced by anionic phospholipids, may cross-link plasma membrane phospholipids with actin and the cytoskeleton and be involved with exocytosis. Heat-stress response may also involve Annexin-2.


Catalog Number: (10408-646)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Catalog Number: (10408-648)
Supplier: Bioss
Description: Proteolytic degradation is critical to the maintenance of appropriate levels of short-lived and regulatory proteins as important and diverse as those involved in cellular metabolism, heat shock and stress response, antigen presentation, modulation of cell surface receptors and ion channels, cell cycle regulation, transcription, and signalling factors. The ubiquitin-proteasome pathway deconstructs most proteins in the eukaryotic cell cytosol and nucleus. Others are degraded via the vacuolar pathway which includes endosomes, lysosomes and the endoplasmic reticulum.


Catalog Number: (10070-936)
Supplier: Prosci
Description: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. In T-cells, JNK1 and JNK2 are required for polarized differentiation of T-helper cells into Th1 cells By similarity. Phosphorylates heat shock factor protein 4 (HSF4). /Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as c-Jun and ATF2 and thus regulates AP-1 transcriptional activity. In T-cells, JNK1 and JNK2 are required for polarized differentiation of T-helper cells into Th1 cells. JNK2 isoforms display different binding patterns: alpha-1 and alpha-2 preferentially bind to c-Jun, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. JUNB is not a substrate for JNK2 alpha-2, and JUND binds only weakly to it./Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating a number of transcription factors, primarily components of AP-1 such as c-Jun and ATF2 and thus regulates AP-1 transcriptional activity. Required for stress-induced neuronal apoptosis and the pathogenesis of glutamate excitotoxicity


Catalog Number: (97021-958)
Supplier: Ohaus
Description: Model MB23 basic moisture analyzers combine high quality durable construction with easy one-button setup, ideal for operators of all skill levels


Catalog Number: (10366-708)
Supplier: Bioss
Description: The expression of DUSP1 gene is induced in human skin fibroblasts by oxidative/heat stress and growth factors. It specifies a protein with structural features similar to members of the non-receptor-type protein-tyrosine phosphatase family, and which has significant amino-acid sequence similarity to a Tyr/Ser-protein phosphatase encoded by the late gene H1 of vaccinia virus. The bacterially expressed and purified DUSP1 protein has intrinsic phosphatase activity, and specifically inactivates mitogen-activated protein (MAP) kinase in vitro by the concomitant dephosphorylation of both its phosphothreonine and phosphotyrosine residues.


Catalog Number: (10104-338)
Supplier: Prosci
Description: HSPA2 belongs to the heat shock protein 70 family.In cooperation with other chaperones, HSPA2 stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage.


Catalog Number: (10088-506)
Supplier: Proteintech
Description: HSPA1A , collectively known as HSP70 (also referred to HSP72), is a stress-inducible member of heat-shock protein 70 (HSP70) proteins which are highly conserved chaperons implicated in protein folding, protein refolding, protein transport, and protein targeting. Encoded by two closely linked, intronless and stress-inducible genes, HSPA1A and HSPA1B differ by only two amino acids and are believed to be fully interchangeable proteins. HSPA1A is a cytosol/nuclear protein able to translocate between cytoplasm and nucleus. Generally, HSPA1A is thought to be expressed in unstressed normal cells at low or undetectable levels. Expression of HSPA1A protein can be highly activated by various stressful stimuli. Significant up-regulation of HSPA1A has been found in various tumors. Recently it has been reported that HSPA1A can be constitutively expressed in selected cell types. This antibody well recognized the endogenous HSPA1A protein in multiple cell lines. (21373891)


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