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Merck
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文件

386032

Sigma-Aldrich

Anti-Hsp70 Mouse mAb (C92F3A-5)

liquid, clone C92F3A-5, Calbiochem®

别名:

Anti-Heat Shock Protein 70

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About This Item

分類程式碼代碼:
12352203
NACRES:
NA.41

生物源

mouse

品質等級

抗體表格

purified antibody

抗體產品種類

primary antibodies

無性繁殖

C92F3A-5, monoclonal

形狀

liquid

包含

≤0.1% sodium azide as preservative

物種活性(以同源性預測)

all

製造商/商標名

Calbiochem®

儲存條件

OK to freeze
avoid repeated freeze/thaw cycles

同型

IgG1

運輸包裝

wet ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

human ... HSPA1A(3303)

一般說明

Anti-Hsp70, mouse monoclonal, clone C92F3A-5, recognizes the ~70 kDa Hsp70. Does not cross-react with Hsc70. It is validated for use in ELISA, FC, WB, ICC, IP & IHC (frozen and paraffin sections).
Mouse monoclonal antibody purified by ion-exchange chromatography. Recognizes the ~70 kDa Hsp70 protein.
Recognizes the ~70 kDa Hsp70 protein. Does not cross-react with Hsc70.

免疫原

Hsp70 from HeLa cells
Human

應用

ELISA (see comments)

Flow Cytometry (see comments)

Frozen Sections (5 µg/ml)

Immunoblotting (1 µg/ml)

Immunocytochemistry (5 µg/ml)

Immunoprecipitation (see comments)

Paraffin Sections (5 µg/ml)

包裝

Please refer to vial label for lot-specific concentration.

警告

Toxicity: Standard Handling (A)

外觀

In PBS, 50% glycerol, pH 7.2.

重構

Following iniital thaw, aliquot and freeze (-20°C).

分析報告

Positive Control
L929 cells, Human colon cancer tissue

其他說明

Does not cross-react with Hsc70. Because Hsp70 is not expressed constitutively in most cells, this antibody is suitable for ascertaining whether a stress-response has occurred in the cell. Increased levels of Hsp70 expression occurs following stress even in cells that constitutively express Hsp70. This antibody has also been reported to work for ELISA, flow cytometry, and immunoprecipitation. Variables associated with assay conditions will dictate the optimal working dilution.
Hang, H., and Fox, M.H. 1995. Cytometry19, 119.
Kilgore, J.L., et al. 1994. J. Appl. Physiol.76, 589.
Heufelder, A.E., et al. 1992. J. Clin. Endocrinol. Metab.74, 724.
Gower, D.J., et al. 1989. J. Neurosurg.70, 605.
Milarski, K., et al. 1989.J. Cell Biol.108, 413.
Vass, K., et al. 1988. Acta Neuropathologica77, 128.
Welch, W.J., and Suhan, J.P. 1986. J. Cell Biol.103, 2035.

法律資訊

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Aigang Lu et al.
Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism, 22(2), 183-195 (2002-02-02)
Estradiol reduces brain injury from many diseases, including stroke and trauma. To investigate the molecular mechanisms of this protection, the effects of 17-beta-estradiol on heat shock protein (HSP) expression were studied in normal male and female rats and in male
Daniel Laubitz et al.
Experimental physiology, 91(5), 867-875 (2006-05-27)
The heat shock response is associated with the intracellular expression of a number of highly conserved heat shock proteins (Hsps). According to their molecular size, Hsps have been divided into several groups, which are strongly conserved and show high homology
Rosario Barranco et al.
International journal of legal medicine, 133(5), 1461-1467 (2019-06-22)
The diagnosis of drowning is one of the most difficult in forensic medicine. The aim of this study was to analyze pulmonary tissue reactions in death by drowning. In particular, we focused on the immunohistochemical expression of P-selectin, SP-A, HSP70
Anne K Voss et al.
The EMBO journal, 25(15), 3652-3663 (2006-07-22)
The mechanisms regulating the size of the cerebral cortex are poorly understood. Here, we demonstrate that the Rap1 guanine nucleotide exchange factor, C3G (Grf2, Rapgef1), controls the size of the cerebral precursor population. Mice lacking C3G show overproliferation of the
James H Ahn et al.
Assay and drug development technologies, 9(3), 236-246 (2010-12-08)
Heat shock protein 70 (Hsp70) is a chaperone protein that helps protect against cellular stress, a function that may be co-opted to fight human diseases. In particular, the upregulation of Hsp70 can suppress the neurotoxicity of misfolded proteins, suggesting possible

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