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Merck
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Key Documents

AB6016

Sigma-Aldrich

Anti-F-actin-capping protein subunit alpha-1 Antibody

from rabbit, purified by affinity chromatography

别名:

capping protein (actin filament) muscle Z-line, alpha 1, CapZ alpha-1, F-actin-capping protein subunit alpha-1

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About This Item

分類程式碼代碼:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物源

rabbit

品質等級

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

純化經由

affinity chromatography

物種活性

pig, mouse, human, rat

物種活性(以同源性預測)

rhesus macaque (based on 100% sequence homology), bovine (based on 100% sequence homology), primate (based on 100% sequence homology), canine (based on 100% sequence homology), porcine (based on 100% sequence homology)

技術

immunocytochemistry: suitable
western blot: suitable

UniProt登錄號

運輸包裝

wet ice

目標翻譯後修改

unmodified

基因資訊

bovine ... Capza1(534656)
dog ... Capza1(475857)
human ... CAPZA1(829)
mouse ... Capza1(12340)
pig ... Capza1(100037957)
rat ... Capza1(691149)
rhesus monkey ... Capza1(705653)

一般說明

F-actin capping protein subunit alpha (CapZ alpha) belongs to the F-actin capping protein family, which are characteristic heterodimers, consisting of an α subunit (31-36 kDa) and a β subunit (28-32 kDa), that cap the barbed end of actin filaments within all eukaryotes. Their ability to bind the actin filaments is in a manner independent of Ca2++ and requires the C-terminal end of both subunits for optimal binding. CapZ is contained within the Z-discs of striated muscle, where it functions to inhibit the polymerization and depolymerization of actin. Within vertebrates, there are three isoforms for each of CapZ’s subunits. All three alpha subunit isoforms are components of the WASH complex. Little is known about isoforms 1 and 2; however, isoform 3 is thought to be involved in spermatid morphogenesis and is exclusively observed within sperm and testis, with highest expression within the neck region of sperm.

免疫原

GST-tagged recombinant protein corres-ponding to human F-actin-capping protein subunit alpha-1.

應用

Detect F-actin-capping protein subunit alpha-1 using this Anti-F-actin-capping protein subunit alpha-1 Antibody validated for use in WB & IC.
Research Category
Cell Structure
Research Sub Category
Cytoskeleton
Western Blot (Snap i.d.) Analysis: 1 µg/mL from a previous lot detected F-actin-capping protein subunit alpha-1 on 10 µg of HeLa cell lysate.
Immunocytochemistry Analysis: A 1:500 dilution from a previous lot detected F-actin-capping protein subunit alpha-1 in NIH/3T3, HeLa, and A431 cells.

品質

Evaluated by Western Blot in HeLa cell lysate.
Western Blot Analysis: 0.1 µg/mL of this antibody detected F-actin-capping protein subunit alpha-1 on 10 µg of HeLa cell lysate.

標靶描述

~35 kDa

外觀

Affinity purified
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

儲存和穩定性

Stable for 1 year at 2-8°C from date of receipt.

分析報告

Control
HeLa cell lysate

其他說明

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

免責聲明

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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儲存類別代碼

12 - Non 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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Helicobacter pylori-derived CagA, a type IV secretion system effector, plays a role as an oncogenic driver in gastric epithelial cells. However, upon delivery into gastric epithelial cells, CagA is usually degraded by macroautophagy/autophagy. Hence, the induction of autophagy in H.
Romain Roncagalli et al.
The Journal of experimental medicine, 213(11), 2437-2457 (2016-11-05)
The RLTPR cytosolic protein, also known as CARMIL2, is essential for CD28 co-stimulation in mice, but its importance in human T cells and mode of action remain elusive. Here, using affinity purification followed by mass spectrometry analysis, we showed that

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