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Bioss
Numéro de catalogue:
(BOSSBS-3347R-CY5.5)
Fournisseur:
Bioss
Description:
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. EG-VEGF possesses an HIF-1 binding site; its expression is induced by hypoxia and restricted to the steroidogenic glands (ovary, testis, adrenal and placenta). Expression of EG-VEGF is often complementary to the expression of VEGF, suggesting that these molecules function in a coordinated manner. EG-VEGF is an example of a class of highly specific mitogens that act to regulate proliferation and differentiation of the vascular endothelium in a tissue-specific manner. It is expressed primarily in one type of tissue and acts selectively on one type of endothelium. EG-VEGF, possibly through binding to a G protein-coupled receptor, results in the activation of MAPK p44/42 and phosphatidylinositol 3-kinase signaling pathways, leading to proliferation, migration and survival of responsive endothelial cells .
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12161R-FITC)
Fournisseur:
Bioss
Description:
CAPS1 is a 189 amino acid cytoplasmic protein that contains four EF-hand domains, which serve as calcium-binding sites, and was first identified in canine thyroid. Interestingly, CAPS1 is much less abundant in humans than in canines. Synthesis and phosphorylation of CAPS1 is upregulated by cAMP-agonists in thyrocytes. CAPS1 likely functions in the regulation of ionic transport and may be involved in cross-signaling between cAMP and Ca(+2)-phophatidylinositol cascades. In addition to thyriod, CAPS1 is expressed in brain, salivary glands and lung. Expression of CAPS1 is increased in endometrial cancer and prognosis seems to be dependent on the level of CAPS1 expression, indicating that CAPS1 may be an appropriate prognostic marker for patient survival.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12161R-A680)
Fournisseur:
Bioss
Description:
CAPS1 is a 189 amino acid cytoplasmic protein that contains four EF-hand domains, which serve as calcium-binding sites, and was first identified in canine thyroid. Interestingly, CAPS1 is much less abundant in humans than in canines. Synthesis and phosphorylation of CAPS1 is upregulated by cAMP-agonists in thyrocytes. CAPS1 likely functions in the regulation of ionic transport and may be involved in cross-Signalling between cAMP and Ca²⁺-phophatidylinositol cascades. In addition to thyriod, CAPS1 is expressed in brain, salivary glands and lung. Expression of CAPS1 is increased in endometrial cancer and prognosis seems to be dependent on the level of CAPS1 expression, indicating that CAPS1 may be an appropriate prognostic marker for patient survival.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5174R-A750)
Fournisseur:
Bioss
Description:
This gene encodes a subunit of the anaphase-promoting complex. This complex is an E3 ubiquitin ligase that regulates progression through the metaphase to anaphase portion of the cell cycle by ubiquitinating proteins which targets them for degradation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9033R-CY5)
Fournisseur:
Bioss
Description:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12161R-CY5)
Fournisseur:
Bioss
Description:
CAPS1 is a 189 amino acid cytoplasmic protein that contains four EF-hand domains, which serve as calcium-binding sites, and was first identified in canine thyroid. Interestingly, CAPS1 is much less abundant in humans than in canines. Synthesis and phosphorylation of CAPS1 is upregulated by cAMP-agonists in thyrocytes. CAPS1 likely functions in the regulation of ionic transport and may be involved in cross-signaling between cAMP and Ca(+2)-phophatidylinositol cascades. In addition to thyriod, CAPS1 is expressed in brain, salivary glands and lung. Expression of CAPS1 is increased in endometrial cancer and prognosis seems to be dependent on the level of CAPS1 expression, indicating that CAPS1 may be an appropriate prognostic marker for patient survival.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9033R-A488)
Fournisseur:
Bioss
Description:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2).
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5692R-A750)
Fournisseur:
Bioss
Description:
The NFKB complex consists of NFKB1 or NFKB2 bound to REL, RELA, or RELB. The NFKB complex is inhibited by I kappa B proteins (NFKBIA, or NFKBIB), which inactivate NF kappa B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I kappa B proteins by kinases (IKBKA, or IKBKB,) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF kappa B complex. For some genes, activation requires NFKB interaction with other transcription factors, such as STAT, AP1 (JUN), and NFAT.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1745R-A647)
Fournisseur:
Bioss
Description:
Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1745R-CY5)
Fournisseur:
Bioss
Description:
Factor H functions as a cofactor in the inactivation of C3b by factor I and also increases the rate of dissociation of the C3bBb complex (C3 convertase) and the (C3b)NBB complex (C5 convertase) in the alternative complement pathway.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5693R-CY3)
Fournisseur:
Bioss
Description:
As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER) probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1409R-A647)
Fournisseur:
Bioss
Description:
DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4009R-A350)
Fournisseur:
Bioss
Description:
Cysteine protease ATG4D: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. Cysteine protease ATG4D, mitochondrial: Plays a role as an autophagy regulator that links mitochondrial dysfunction with apoptosis. The mitochondrial import of ATG4D during cellular stress and differentiation may play important roles in the regulation of mitochondrial physiology, ROS, mitophagy and cell viability.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0126R-A680)
Fournisseur:
Bioss
Description:
In cooperation with other chaperones, Hsp7s stabilise 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 recognise 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. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0126R-CY3)
Fournisseur:
Bioss
Description:
In cooperation with other chaperones, Hsp7s 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. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1953R-A555)
Fournisseur:
Bioss
Description:
May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes.
UOM:
1 * 100 µl
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