MBL International

Anti-His-tag

Background:

The His-tag (6xHis-tag) is one of the most common tags used to facilitate the purification of recombinant proteins. Metal chelate affinity chromatography is widely used for purification of His-tagged proteins.　This specific antibody is useful tool for monitoring of the His-tagged proteins, and recognizes His-tags placed at N-terminal, C-terminal, and internal regions of the recombinant proteins.

Size:

200 µL

Application:

Product Type:

Primary Antibody

Host Species:

Mouse

Isotype:

IgG2a k

Storage Temp. (°C):

-20

Shipping Temp. (°C):

Pictures:

Intended Use:

For Research use only. Not for use in diagnostic procedure.

Anti-mouse NP95

Datasheet:

D289-3_ver1.pdf

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Background:

DNA methylation inheritance is the process of copying pre-existing methylation patterns onto newly replicated DNA strand after DNA replication. Dnmt1 is the DNA methyltransferase that methylate hemi-methylated CpG region, which occurs after DNA repairs and replication steps. The Np95 also known as UHRF1 and ICBP90 is nuclear protein, which contains an ubiquitin-like domain, a methyl DNA binding domain, the SRA (SET- and RING-associated) domain, a cyclinA/E-cdk2 phosphorylation site, a Rb binding motif, and a ring finger domain. Np95 forms complexes with Dnmt1 and PCNA at replicating heterochromatic regions, and recruits Dnmt1 to hemimethylated DNA to maintenance of DNA methylation. Np95 interacts with Dnmt1, is essential for the maintenance and the epigenetic inheritance of DNA methylation.

Size:

100 µL

Application:

Product Type:

Primary Antibody

Host Species:

Rat

Isotype:

IgG2a k

Storage Temp. (°C):

-20

Shipping Temp. (°C):

Pictures:

References:

1) Sharif, J., et al., Nature 450, 908-912 (2007)
2) Muto, M., et al., Radiat. Res. 166, 723-733 (2006)
3) Muto, M., et al., J. Biol. Chem. 277, 34549-34555 (2002)
4) Bonapace, I. M., et al., J. Cell Biol. 157, 909-914 (2002)
5) Fujimori, A., et al., Mamm. Genome 9, 1032-1035 (1998)
6) Muto, M., et al., Cell Prolif. 28, 645-657 (1995)

Intended Use:

For Research use only. Not for use in diagnostic procedure.

Pin1, human recombinant

Datasheet:

CY-R2148.pdf

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Background:

The unique prolyl isomerase, Pin1, has been found to regulate mitosis through a simple conformational change (1) the cis-trans isomerization of phosphorylated Ser/Thr-Pro amide bonds in a variety of key cell cycle regulatory phosphoproteins, including the Cdc25 phosphatase, the p53 oncogene, and the c-Myc oncogene (1-3). Importantly, Pin1-catalyzed post-phosphorylation conformational changes can have profound effects on many key proteins in diverse cellular processes (4). Cells depleted of Pin1 are characterized by premature entry into mitosis, followed by mitotic arrest, nuclear fragmentation, and apoptosis, while overexpression of Pin1 inhibits the G2 to M transition (2, 5). Hence, Pin1 acts as a negative regulator for mitotic activity in G2, preventing lethal premature entry into mitosis. Pin1 is present at higher concentrations during mitosis (6), making it a potential target in the continuously dividing cells of cancer. The central role Pin1 plays in the cell cycle makes it an interesting target for inhibition, both for potential anticancer activity and for elucidation of the mechanism of mitosis.

Size:

100 ?g

Application:

Product Type:

Reagent

Species Reactivities:

Storage Temp. (°C):

-70

Shipping Temp. (°C):

Dry Ice

References:

1. Yaffe MB, Schutkowski M, Shen M, Zhou XZ, Stukenberg PT, Rahfeld JU, Xu J, Kuang J, Kirschner MW, Fischer G, Cantley LC, Lu KP. Science 278: 1957, 1997

2. Shen M, Stukenberg PT, Kirschner MW, Lu KP. Genes Dev 12: 706, 1998

3. Yeh E, Cunningham M, Arnold H, Chasse D, Monteith T, Ivaldi G, Hahn WC, Stukenberg PT, Shenolikar S, Uchida T, Counter CM, Nevins JR, Means AR, Sears R. Nat Cell Biol 6: 308, 2004

4. Lu KP, Zhou XZ. Nat Rev Mol Cell Biol 8: 904, 2007

5. Rippmann JF, Hobbie S, Daiber C, Guilliard B, Bauer M, Birk J, Nar H, Garin-Chesa P, Rettig WJ, Schnapp A. Cell Growth Differ 11: 409, 2000

6. Bao L, Kimzey A, Sauter G, Sowadski JM, Lu KP, Wang DG. Am J Pathol 164: 1727, 2004

Intended Use:

For Research use only. Not for use in diagnostic procedure.

Rpn13-Pru domain, human recombinant

Datasheet:

CY-R2072.pdf

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Background:

The novel proteasome subunit Rpn13 binds to Lys48-linked diubiquitin with high affinity through a novel ubiquitin-binding domain (pleckstrin-like receptor for ubiquitin: Pru) and to ubiquitin-like (UBL) domains of UBL-ubiquitin-associated (UBA) proteins as well as to de-ubiquitinating enzyme Uch37/UCHL5.

Size:

100 ?g

Application:

Product Type:

Reagent

Species Reactivities:

Storage Temp. (°C):

-70

Shipping Temp. (°C):

Dry Ice

References:

1. Husnjak, K. et al. Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453, 481-488, 2008

2. Schreiner, P. et al. Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature 453, 548-552, 2008

3. Hicke, L., Schubert, H. L. & Hill, C. P. Ubiquitin-binding domains. Nature Rev. Mol. Cell Biol. 6, 610-621, 2005

Intended Use:

For Research use only. Not for use in diagnostic procedure.

anti-S100A2

Datasheet:

CY-P1040.pdf

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Background:

S100A2 is a member of the subfamily of S100 Ca2+-binding proteins, characterized by two distinct EF-hand structural motifs. It is a homodimeric protein that upon binding of calcium undergoes a conformational change (1). The S100A2 protein has been first detected in lung and kidney and is mainly expressed in a subset of tissues and cells such as breast epithelia and liver (2- 4). Interestingly the cDNA coding for the S100A2 protein was identified as a novel tumor suppressor gene by subtractive hybridization between normal and tumor derived human mammary epithelial cells (5). Expression studies showed that the S100A2 gene is markedly down-regulated in several tumor tissues of various origins like melanomas (6) and breast carcinoma (7). Moreover, growth factors were reported to alter the S100A2 gene expression at late G1/S-phase, indicating that S100A2 is cell cycle-regulated (8). Site-specific DNA methylation of the S100A2 gene promoter region in normal versus tumorigenic breast cancer cell lines indicated repression of gene expression in tumor cells, thus suggesting a role for S100A2 in suppression of tumor cell growth and possibly inhibition of tumor progression (7). By contrast, S100A2 overexpression was recently found to correlate with prognosis in ovarian, gastric, and lung cancers (9-11). Taken together, the role of S100A2 in carcinogenesis remains controversial.

Size:

50 ?g

Application:

Product Type:

Primary Antibody

Host Species:

Rabbit

Species Reactivities:

Isotype:

IgG

Storage Temp. (°C):

-20

References:

1. Bhattacharya, S., Bunick, C. G., and Chazin, W. J. (2004) Biochim. Biophys. Acta 1742: 69ﾖ79

2. Heizmann, C., Fritz, G., and Schafer, B. (2002) Front. Biosci. 7: d1356ﾖd1368

3. Glenney, J. R., Jr., Kindy, M. S., and Zokas, L. (1989) J. Cell Biol. 108: 569-578

4. Zhang, T., Woods, T. L., and Elder, J. T. (2002) J. Invest. Dermatol. 119: 1196-1201

5. Lee SW, Tomasetto C, Sager R. (1991) PNAS 88: 2825-9

6. Maelandsmo GM, Florenes VA, Mellingsaeter T, Hovig E, Kerbel RS, Fodstad O. (1997) Int J Cancer 74: 464-9

7. R Wicki, C Franz, FA Scholl, CW Heizmann, and BW Schafer (1997) Cell Calcium 22: 243-54.

8. SW Lee, C Tomasetto, K Swisshelm, K Keyomarsi, and R Sager (1992) PNAS 89: 2504-2508.

9. Hough CD, Cho KR, Zonderman AB, Schwartz DR, Morin PJ. (2001) Cancer Res. 61: 3869-76.

10. El-Rifai W, Moskaluk CA, Abdrabbo MK, et al. (2002) Cancer Res. 62: 6823-6.

11. Diederichs S, Bulk E, Steffen B, et al. (2004) Cancer Res. 64: 5564-9.

Intended Use:

For Research use only. Not for use in diagnostic procedure.

Lipid Phosphatase PTEN(Human, Active)

Background:

PTEN, also known as phosphatase and tensin homolog, is one of the most frequently mutated tumor suppressors in human cancer and acts as both a dual-specificity protein phosphatase and a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate. It is the first phosphatase identified as a tumor suppressor. It may be involved in almost all types of cancer, both solid tumors and hematological malignancies. PTEN negatively regulates intracellular levels of phosphatidylinositol-3,4,5-trisphosphate in cells by serving to counter-balance the effects of PI3 Kinase, which normally generate PtdIns(3,4,5)P3 and acts as a tumor suppressor by negative regulation of AKT/PKB signaling pathway via preventing localization of proteins with pleckstrin homology domains to the cell membrane. Recent results indicate that at least part of its role is to regulate the activity of the serine/threonine kinase AKT/PKB, and thus influence cell survival signaling.

Size:

25 ?g

Application:

Product Type:

Reagent

Species Reactivities:

Storage Temp. (°C):

-70

Shipping Temp. (°C):

Dry Ice

Intended Use:

For Research use only. Not for use in diagnostic procedure.

NAD+/NADH Colorimetric Assay Kit

Datasheet:

CY-1253.pdf

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Background:

Nicotinamide adenine dinucleotide (NAD+) as well as nicotinamide adenine dinucleotide phosphate (NADP+) is an important cofactor found in cells. NADH is the reduced form of NAD+, and NAD+ is the oxidized form of NADH. It has been reported that NAD+ metabolism regulates important biological effects including life span. NAD+, through poly-ADP-ribosyl polymerase (PARP), mono-ADP- ribosyltransferase (ARTs) and recently characterized sirtuin enzymes, exerts potential biological effects. These enzymes modify proteins to regulate their function via ADP-ribosylation or deacetylation in the presence of NAD+. These enzymes are involved in several pathways including apoptosis, DNA repair, senescence and endocrine signaling, suggesting that either the enzymes could be an important therapeutical target for cancer, diabetes atherosclerosis and so on.
The traditional NAD+/NADH and NADP+/NADPH assays are done by monitoring of NADH or NADPH absorption at 340 nm. This method suffers low sensitivity and high interference since the assay is done in the UV range that requires expensive quartz microplate. CycLex NAD+/NADH Colorimetric Assay Kit employs an enzyme cycling reaction, which significantly increases detection sensitivity, and provides a convenient method for sensitive detection of NAD+, NADH and their ratio.

Size:

100 assays

Application:

Product Type:

Kit

Species Reactivities:

Storage Temp. (°C):

-70

Shipping Temp. (°C):

Dry Ice

References:

1. Ziegenhorn J, Senn M, Bucher T. (1976) Molar absorptivities of beta-NADH and beta-NADPH. Clin
Chem. 22: 151.

2. Matsumura, H. and Miyachi S (1980) Cycling assay for nicotinamide adenine dinucleotides. Methods Enzymol. 69: 465-470.

3. Zerez CR, Lee SJ, Tanaka KR (1987) Spectrophotometric determination of oxidized and reduced pyridine nucleotides in erythrocytes using a single extraction procedure. Anal Biochem. 164: 367-73

4. Zhao, Z, Hu, X and Ross CW (1987). Comparison of Tissue Preparation Methods for Assay of Nicotinamide Coenzymes. Plant Physiol. 84: 987-988.

5 Umemura, K and Kimura, H (2005) Determination of oxidized and reduced nicotinamide adenine dinucleotide in cell monolayers using a single extraction procedure and a spectrophotometric assay. Anal Biochem. 338: 131-5.

6. Hasmann, M and Schemainda, I (2003) FK866, a Highly Specific Noncompetitive Inhibitor of Nicotinamide Phosphoribosyltransferase, Represents a Novel Mechanism for Induction of Tumor Cell Apoptosis. Cancer Research 63: 7436-7442, 2003

7.Vilcheze, C et al. (2005). Altered NADH/NAD+ Ratio Mediates Coresistance to Isoniazid and Ethionamide in Mycobacteria. Antimicrobial Agents and Chemotherapy. 49: 708-720.

8. Kimura N, Fukuwatari T, Sasaki R, Shibata K. (2006) Comparison of metabolic fates of nicotinamide, NAD+ and NADH administered orally and intraperitoneally; characterization of oral NADH. J Nutr Sci Vitaminol. (Tokyo) 52: 142.

9. O'Donnell JM, et al. (2004) Limited transfer of cytosolic NADH into mitochondria at high cardiac workload. Am J Physiol Heart Circ Physiol. 286: H2237.

10. Richard A. et al. (2008) Characterization of NAD Uptake in Mammalian Cells J. Biol. Chem. 283: 6367-6374.

11. Rongvaux, A et al. (2008) Nicotinamide Phosphoribosyl Transferase/Pre-B Cell Colony-Enhancing Factor/Visfatin Is Required for Lymphocyte Development and Cellular Resistance to Genotoxic Stress J. Immunol. 181: 4685-4695

12. Pogrebniak, A et al. (2006) Chemopotentiating effects of a novel NAD biosynthesis inhibitor, FK866, in combination with antineoplastic agents. Eur J Med Res. 11: 313-21.

Intended Use:

For Research use only. Not for use in diagnostic procedure.

NMNAT2 (Nicotinamide mononucleotide adenylyltransferase 2)Human, recombinant protein expressed in E. coli., Active

Datasheet:

cy-e1252-2.pdf

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Background:

Nicotinamide mononucleotide adenylyltransferase (NMNAT) (EC2.7.7.1) is a central enzyme in NAD+ biosynthesis, transferring the adenylyl moiety of ATP to nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) resulting in the formation of NAD+ or NaAD+ and the release of pyrophosphate. As this reaction is reversible, the enzyme may in principle be used to form ATP and NMN from NAD+ and pyrophosphate.
NMNAT2 is predominantly expressed in human pancreas, insulinoma as well as in the brain, especially in the cerebrum, cerebellum, occipital lobe, frontal lobe, temporal lobe and putamen. Immunofluorescence microscopy localized endogenous NMNAT2 to the Golgi apparatus in human cell line. Endogenous NMNAT2 seem to be a labile axon survival factor, because specific depletion of NMNAT2 is sufficient to induce Wallerian-like degeneration of uninjured axons which endogenous NMNAT1 and NMNAT3 cannot prevent. Thus endogenous NMNAT2 represents an exciting new therapeutic target for axonal disorders.

Size:

50 ?g

Application:

Product Type:

Reagent

Species Reactivities:

Storage Temp. (°C):

-70

Shipping Temp. (°C):

Dry Ice

References:

1. Raffaelli, N.; Sorci, L.; Amici, A.; Emanuelli, M.; Mazzola, F.; Magni, G. : Biochem. Biophys. Res. Commun. 297: 835-840, 2002.

2. Seki, N.; Ohira, M.; Nagase, T.; Ishikawa, K.; Miyajima, N.; Nakajima, D.; Nomura, N.; Ohara, O. : DNA Res. 4: 345-349, 1997.

3. Yalowitz, J. A.; Xiao, S.; Biju, M. P.; Antony, A. C.; Cummings, O. W.; Deeg, M. A.; Jayaram, H. N. : Biochem. J. 377: 317-326, 2004.

4. Zhang, X.; Kurnasov, O. V.; Karthikeyan, S.; Grishin, N. V.; Osterman, A. L.; Zhang, H. : J. Biol. Chem. 278: 13503-13511, 2003.

5. J Gilley and MP Coleman: PLoS Biol. 8: e1000300, 2010

Intended Use:

For Research use only. Not for use in diagnostic procedure.

CircuLex™ Human soluble LOX-1/OLR1 ELISA Kit

Datasheet:

CY-8081.pdf

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Background:

Lectin-like oxidized LDL receptor-1 (LOX-1), a 52-kD type II transmembrane receptor for oxidized low-density lipoproteins (ox-LDL) belonging to the C-type lectin family is present primarily on endothelial cells (1). Accumulating evidences indicate that oxLDL uptake through this receptor induces endothelial dysfunction. oxLDL binding to endothelial LOX-1 generates superoxide anions, decreases nitric oxide production, and activates NF-kB (2, 3). Endothelial LOX-1 expression is induced by various pro-inflammatory cytokines, such as TNF-alpha (4) and TGF-beta (5) as well as by pro-atherogenic factors, such as oxLDL and advanced glycation end products in vitro (6). This receptor is expressed in the aortas of hypertensive, diabetic, and hyperlipidemic animals (6-8) and is upregulated in early human atherosclerotic lesions (9). These results suggest that LOX-1 may be expressed locally and play important roles in atherogenesis by internalizing and degrading oxLDL and in inflammatory responses in vivo. LOX-1 can be cleaved from the cell surface and released as soluble LOX-1 (sLOX-1), and elevated sLOX-1 levels may be indicative of atherosclerotic plaque instability (10).

Size:

96 assays

Application:

Product Type:

Kit

Species Reactivities:

Storage Temp. (°C):

References:

1. Sawamura T, Kume N, Aoyama T, Moriwaki H, Hoshikawa H, Aiba Y, Tanaka T, Miwa S, Katsura Y, Kita T, Masaki T. (1997) Nature 386: 73-77
2. Cominacini L, Pasini AF, Garbin U, Davoli A, Tosetti ML, Campagnola M, Rigoni A, Pastorino AM, Lo Cascio V, Sawamura T. (2000) J Biol Chem. 275: 12633ﾖ12638.
3. Cominacini L, Rigoni A, Pasini AF, Garbin U, Davoli A, Campagnola M, Pastorino AM, Lo Cascio U, Sawamura T. (2001) J Biol Chem. 276: 13750ﾖ13755.
4. Kume N, Murase T, Moriwaki H, Aoyama T, Sawamura T, Masaki T, Kita T. (1998) Circ Res. 83: 322ﾖ327.
5. Draude G and Lorenz R. L. (2000) Am J Physiol Heart Circ Physiol. 278: H1042ﾖH1048.
6. Nagase M, Hirose S, Sawamura T, Masaki T, Fujita T. (1997) Biochem Biophys Res Commun. 237: 496ﾖ498.
7. Chen M, Nagase M, Fujita T, Narumiya S, Masaki T, Sawamura T. (2001) Biochem Biophys Res Commun. 287: 962ﾖ968.
8. Chen M, Kakutani M, Minami M, Kataoka H, Kume N, Narumiya S, Kita T, Sawamura T. (2000) Arterioscler Thromb Vasc Biol. 20: 1107ﾖ1115.
9. Kataoka H, Kume N, Miyamoto S, Minami M, Moriwaki H, Murase T, Sawamura T, Masaki T, Hashimoto N, Kita T. (1999) Circulation 99: 3110 ﾖ3117.
10. Hayashida K, Kume N, Murase T, Minami M, Nakagawa D, Inada T, Tanaka M, Ueda A, Kominami G, Kambara H, Kimura T, Kita T. (2005) Circulation 112: 812-818.

Intended Use:

For Research use only. Not for use in diagnostic procedure.

anti-GM130

Datasheet:

PM061.pdf

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Background:

The Golgi apparatus is a eukaryotic organelle, which is mainly devoted to processing the proteins synthesized in the endoplasmic reticulum (ER). GM130 is a member of the golgin family of coiled-coil proteins that localizes predominantly to the cis-Golgi. GM130 might participate in ER-Golgi traffic.

Size:

100 μL

Application:

Product Type:

Primary Antibody

Host Species:

Rabbit

Species Reactivities:

Isotype:

Ig (aff.)

Storage Temp. (°C):

-20

Shipping Temp. (°C):

Pictures:

References:

Diao, A., et al., J. Biol. Chem. 283, 6957-6967 (2008)
Alvarez, C., et al., J. Biol. Chem. 276, 2693-2700 (2001)

Intended Use:

For Research use only. Not for use in diagnostic procedure.

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