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Catalog Number: (10388-328)
Supplier: Bioss
Description: JMJD1B (jumonji domain containing 1B), also known as KDM3B, 5qNCA (5q Nuclear Co-Activator) or C5orf7, is a member of the JHDM2 histone demethylase family of proteins. Expressed in a wide variety of tissues, JMJD1B localizes to the nucleus and contains one JMJC domain and a C-terminal zinc finger motif. JMJD1B functions as a histone demethylase and, using iron as a cofactor, demethylates lysine-9 of Histone H3. This suggests that JMJD1B plays a central role in the histone code. The gene encoding human JMJD1B is located within the 5q region of the genome that is often deleted in myeloid leukemias and myelodysplasias. This implies that JMJD1B may function as a tumor suppressor of myeloid leukemia. Eptopic expression of JMJD1B exhibits growth suppressive activities, further supporting a role for JMJD1B in tumor suppression.


Catalog Number: (10751-156)
Supplier: Prosci
Description: ZIP1 Antibody: ZIP1, also known as ZIRTL (zinc-iron regulated transporter-like), is the first mammalian member of a family of divalent ion transporters. Zinc is an essential ion for cells and plays significant roles in the growth, development, and differentiation. ZIP1 expression is markedly downregulated in a number of cancerous tissues and is thought to function as a tumor suppressor gene in prostate cancer. More recent studies have shown that overexpression of ZIP1 and concomitant increased levels of intracellular zinc in PC-3 cells cause a significant inhibition of NF-kappa B, leading to down-regulation of the antiapoptotic protein Bcl-2, Bcl-XL, and the apoptosis inhibitor XIAP, reducing the malignant potential of prostate cancer cells in vitro and in vivo.


Catalog Number: (470230-270)
Supplier: Wards
Description: Loop apparatus ideal for studying Lenz Law and Faraday's Law.


Catalog Number: (94025-822)
Supplier: Master Appliance
Description: Master butane torches are perfect for any task at hand. They are self-contained, butane-powered, heavy-duty, general industrial torches.


Catalog Number: (CA97013-308)
Supplier: PerkinElmer
Description: Series N30502XX Lumina™ 2" (50 mm) diameter multi-element lamps are designed to be used with the PinAAcle™ and AAnalyst™ Atomic Absorption spectrometer series of instruments.


Catalog Number: (89322-630)
Supplier: Genetex
Description: Purity: Purified by antigen-affinity chromatography. Species Reactivity: Human Tested Applications: WB Pkg Size: 100 ul


Catalog Number: (CA97013-302)
Supplier: PerkinElmer
Description: Series N30502XX Lumina™ 2" (50 mm) diameter multi-element lamps are designed to be used with the PinAAcle™ and AAnalyst™ Atomic Absorption spectrometer series of instruments.


Supplier: Wesco
Description: Welded steel frame with reinforced outriggers securely holds and transports 208.2 L (55gal.) or 322 L (85gal.) drums

Catalog Number: (10463-036)
Supplier: Bioss
Description: The 2'- 5'- oligoadenylate synthetase (OAS) family is comprised of four members: OAS1, OAS2, OAS3 and OASL. These proteins are induced by interferons and function to convert ATP into 2'- 5'- linked oligomers of adenosine in the presence of double-stranded RNA and magnesium ions. Copper, iron and zinc ions strongly inhibit the OAS enzymatic activity, while manganese ions can replace magnesium ions as an activator. The OAS family plays a significant role in the inhibition of cellular protein synthesis, apoptosis and growth, and its members are important factors in viral infection resistance. OAS3, also referred to as p100, contains three adjacent OAS1-like domains and maps to the human chromosome 12q24.2


Catalog Number: (10395-236)
Supplier: Bioss
Description: Cotransporter which plays a role in lipoprotein, vitamin and iron metabolism, by facilitating their uptake. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the GIF-cobalamin complex. The binding of all ligands requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. Interaction with LRP2 mediates its trafficking throughout vesicles and facilitates the uptake of specific ligands like GC, hemoglobin, ALB, TF and SCGB1A1. Interaction with AMN controls its trafficking to the plasma membrane and facilitates endocytosis of ligands. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface.


Catalog Number: (10395-002)
Supplier: Bioss
Description: JMJD1B (jumonji domain containing 1B), also known as KDM3B, 5qNCA (5q Nuclear Co-Activator) or C5orf7, is a member of the JHDM2 histone demethylase family of proteins. Expressed in a wide variety of tissues, JMJD1B localizes to the nucleus and contains one JMJC domain and a C-terminal zinc finger motif. JMJD1B functions as a histone demethylase and, using iron as a cofactor, demethylates lysine-9 of Histone H3. This suggests that JMJD1B plays a central role in the histone code. The gene encoding human JMJD1B is located within the 5q region of the genome that is often deleted in myeloid leukemias and myelodysplasias. This implies that JMJD1B may function as a tumor suppressor of myeloid leukemia. Eptopic expression of JMJD1B exhibits growth suppressive activities, further supporting a role for JMJD1B in tumor suppression.


Catalog Number: (10100-398)
Supplier: Prosci
Description: Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. NARF binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. NARF is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases.Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. The protein encoded by this gene binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene, including one with a novel exon that is generated by RNA editing.


Catalog Number: (76119-356)
Supplier: Bioss
Description: The 2'- 5'- oligoadenylate synthetase (OAS) family is comprised of four members: OAS1, OAS2, OAS3 and OASL. These proteins are induced by interferons and function to convert ATP into 2'- 5'- linked oligomers of adenosine in the presence of double-stranded RNA and magnesium ions. Copper, iron and zinc ions strongly inhibit the OAS enzymatic activity, while manganese ions can replace magnesium ions as an activator. The OAS family plays a significant role in the inhibition of cellular protein synthesis, apoptosis and growth, and its members are important factors in viral infection resistance. OAS3, also referred to as p100, contains three adjacent OAS1-like domains and maps to the human chromosome 12q24.2


Catalog Number: (10084-602)
Supplier: Proteintech
Description: CISD2 gene encodes a 15 kDa CDGSH iron-sulfur domain-containing protein 2, which is also named Miner1 or NAF-1, this protein was reported on endoplasmic reticulum membrane or mitochondrion outer membrane. Defects in CISD2 are the cause of Wolfram syndrome type 2 (WFS2), a rare disorder characterized by juvenile-onset insulin-dependent diabetes mellitus with optic atrophy. CISD2 regulates autophagy program by interacting BCL2, contributing to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum.


Catalog Number: (10490-582)
Supplier: Bioss
Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.


Catalog Number: (10490-568)
Supplier: Bioss
Description: 5-aminolevulinate synthase 1 (ALAS-H) and 2 (ALAS-E) are two isoforms of ALAS, an enzyme catalyzing the first step of the heme biosynthetic pathway in mammals. The erythroid-specific isoenzyme, ALAS-E, regulates the first step of hematopoietic cell differentation and iron metabolism in the liver. ALAS-H is a housekeeping protein which mediates synthesis of early heme in the mitochondria of most cells. Succinyl CoA associates with ALAS-E in protein conformation change and translocation of ALAS-E into the mitochondria and does not interact with ALAS-H. The ALAS-E 5'-flanking region contains binding sites for nuclear activators such as GATA-1, NF-E2 and EKLF. Since the ALAS gene maps to the X chromosome, mutation of the gene leads to the pyridoxine-refractory X-linked sideroblastic anemia.


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