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当前位置: 首页 > 产品中心 > acid_base_buffer_solution > StressMarq/Anti-HSP70/HSC70 Antibody [N27F3-4]/SMC-104B/200-µg
商品详细StressMarq/Anti-HSP70/HSC70 Antibody [N27F3-4]/SMC-104B/200-µg
StressMarq/Anti-HSP70/HSC70 Antibody [N27F3-4]/SMC-104B/200-µg
StressMarq/Anti-HSP70/HSC70 Antibody [N27F3-4]/SMC-104B/200-µg
商品编号: SMC-104B
市场价: ¥6400.00
美元价: 3840.00
产地: 美国(厂家直采)
公司:
产品分类: 酸碱缓冲液
公司分类: acid_base_buffer_solution
联系Q Q: 3392242852
电话号码: 4000-520-616
电子邮箱: info@ebiomall.com
商品介绍

Overview:

Product Name HSP70/HSC70 Antibody
Description

Mouse Anti-Human HSP70/HSC70 Monoclonal IgG1

Species Reactivity Dog, Human, Monkey, Mouse, Rat, African clawed frog (Xenopus laevis), Beluga, Bovine, Chicken, Cucumber, Fish, Fruit Fly (Drosophila melanogaster), Guinea Pig (Cavia porcellus), Hamster, Nematode (Caenorhabditis elegans), Pea (Pisum sativum), Pig, Plant, Rabbit, Sheep
Applications WB, IHC, ICC/IF, IP, FCM, IEM
Antibody Dilution WB (1:1000), IHC (1:100), ICC/IF (1:50); optimal dilutions for assays should be determined by the user.
Host Species Mouse
Immunogen Species Human
Immunogen Recombinant HSP70/HSC70
Concentration 1 mg/ml
Conjugates Alkaline Phosphatase, APC, ATTO 390, ATTO 488, ATTO 565, ATTO 594, ATTO 633, ATTO 655, ATTO 680, ATTO 700, Biotin, FITC, HRP, PE/ATTO 594, PerCP, RPE, Streptavidin, Unconjugated

Properties

Storage Buffer PBS pH7.2, 50% glycerol, 0.09% sodium azide
Storage Temperature -20ºC
Shipping Temperature Blue Ice or 4ºC
Purification Protein G Purified
Clonality Monoclonal
Clone Number N27F3-4
Isotype IgG1
Specificity Detects ~72 (Hsp) and ~73kDa (Hsc).
Cite This Product StressMarq Biosciences Cat# SMC-104, RRID: AB_2120301
Certificate of Analysis 1 µg/ml of SMC-104 was sufficient for detection of HSP70/HSC70 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Biological Description

Alternative Names HSP70 1 Antibody, HSP70 2 Antibody, HSP70.1 Antibody, HSP72 Antibody, HSPA1 Antibody, HSPA1A Antibody, HSPA1B Antibody
Research Areas Cancer, Heat Shock
Cellular Localization Cytoplasm
Accession Number NP_005336.3
Gene ID 3303
Swiss Prot P08107
Scientific Background HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. For more information visit our HSP70 Scientific Resource Guide at http://www.HSP70.com.
References 1. Welch W.J. and Suhan J.P. (1986) J.Cell Biol. 103: 2035-2050.
2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993), J. Mol. Evol.38 (1): 1-17.
3. Rothman J. (1989) Cell 59: 591 -601.
4. DeLuca-Flaherty et al. (1990), Cell 62: 875-887.
5. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad. Sci. USA 89: 7290-7294.
6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.
7. Polanonka-Grabowska R. et. al. (1997) Blood 90: 1516-1526.
8. Schnell D.J. et. al. (1994) Science 266: 1007-1012.
9. Kabakov A.E., et. al. (2002) Am. J.Physiol. 283(2): C521-C534.
10. Ricart J. et. al. (1997) Biochem. J. 324: 635-643.
11. Hang H. and Fox M.H. (1995) Cytometry 19(2): 119-125.

Product Images

<p>Immunohistochemistry analysis using Mouse Anti-Hsp70 Monoclonal Antibody, Clone N27 (SMC-104). Tissue: backskin. Species: Mouse. Fixation: Bouin’s Fixative and paraffin-embedded. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody (SMC-104) at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Epidermis.</p>

Immunohistochemistry analysis using Mouse Anti-Hsp70 Monoclonal Antibody, Clone N27 (SMC-104). Tissue: backskin. Species: Mouse. Fixation: Bouin’s Fixative and paraffin-embedded. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody (SMC-104) at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Epidermis.

<p>Western Blot analysis of Human Cell lysates showing detection of Hsp70 protein using Mouse Anti-Hsp70 Monoclonal Antibody, Clone N27 (SMC-104). Load: 15 µg protein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody (SMC-104) at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.</p>

Western Blot analysis of Human Cell lysates showing detection of Hsp70 protein using Mouse Anti-Hsp70 Monoclonal Antibody, Clone N27 (SMC-104). Load: 15 µg protein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody (SMC-104) at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.

Product Citations (9)

Western Blot

HSP90 Shapes the Consequences of Human Genetic Variation.

Karras, G.I. et al. (2017) Cell. 168(5):856-866.e12.

PubMed ID: 28215707 Reactivity Human Applications: Western Blot

Detection of constitutive and inducible HSP70 proteins in formalin fixed human brain tissue.

Preusse-Prange, A., Modrow, J.H., Schwark, T., von Wurmb-Schwark, N. (2014) Forensic Sci Int. 235:62-7.

PubMed ID: 24447452 Reactivity Human Applications: Western Blot

Highly reliable quantification of proteins such as members of the HSP70 superfamily based on the grey scale index via immune detection stained bands on a Western blot.

Modrow, J. et al. (2012) Forensic Sci Int. 222 (1): 256-258.

PubMed ID: 22831866 Reactivity Human Applications: Western Blot

Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins.

Sun, L., Prince, T., Manjarrez, J.R., Scroggins, B.T., and Matts, R.L. (2012) Biochim Biophys Acta. 1823 (6): 1092-1101.

PubMed ID: 22504172 Reactivity Human Applications: Western Blot

A Novel Neurotrophic Drug for Cognitive Enhancement and Alzheimer's Disease.

Chen, Q. et al. (2011) PLoS One. 6 (12): e27865.

PubMed ID: 22194796 Reactivity Rat Applications: Western Blot

Ultrasound-induced activation of Wnt signaling in human MG-63 osteoblastic cells.

Olkku, A., Leskinen, J.J., Lammi, M.J., Hynynen, K., Mahonen, A. (2010) Bone. 47 (2): 320-330.

PubMed ID: 20435172 Reactivity Human Applications: Western Blot

Immunohistochemistry

Detection of constitutive and inducible HSP70 proteins in formalin fixed human brain tissue.

Preusse-Prange, A., Modrow, J.H., Schwark, T., von Wurmb-Schwark, N. (2014) Forensic Sci Int. 235:62-7.

PubMed ID: 24447452 Reactivity Human Applications: Immunohistochemistry

How one TSH receptor antibody induces thyrocyte proliferation while another induces apoptosis.

Morshed, S.A, Ma, R., Latif, R. and Davies, T.F. (2013) J.Autoimmunity. 47:17-24.

PubMed ID: 23958398 Reactivity Rat Applications: Immunohistochemistry

Immunocytochemistry/Immunofluorescence

Theiler’s murine encephalomyelitis virus infection induces a redistribution of heat shock proteins 70 and 90 in BHK-21 cells, and is inhibited by novobiocin and geldanamycin.

Mutsvunguma, L.Z. et al. (2011) Cell Stress Chaperones. 16 (5): 505-515.dx.

PubMed ID: 21445704 Reactivity Hamster Applications: Immunocytochemistry/Immunofluorescence

品牌介绍
StressMarq Biosciences公司的核心技术领域为细胞应激与离子通道以及载体研究,同时在其他领域也取得了一定成就,包括翻译后修饰,提供甲基化与乙酰基化抗体。其中,细胞应激领域主要包括热休克蛋白(HSP)领域。我们公司不仅在热休克蛋白领域领先全球,而且在氧化应激领域也卓有成就。StressMarq的优势在于提供四种独立的产品系列,分别涉及抗体、蛋白、酶联免疫吸附试验(ELISA)试剂盒及小分子领域。