供货周期: | 一周 |
品牌: | |
规格: | 100ul |
货号: | 2885-1 |
CAS号: |
Alpha-Actinin 4(ACTN4)antibody
Cat.#: 2885-1
Rabbit Monoclonal Antibody
Clone ID: EPR2533(2)
Swiss Prot: O43707
Mol Weight: 100kDa
Size: 100ul
Description
Alpha-actinin is a ubiquitously expressed cytoskeletal protein found in numerous actin structures. It consists of an N-terminal actin-binding domain, a central rod domain, and a C-terminal domain; the protein functions as a homodimer to cross-link actin filaments. The rod domain determines the distance between cross-linked actin filaments and also serves as an interaction site for several cytoskeletal and signaling proteins (1). Alpha-actinin 4 is a non-muscle isoform version of alpha-actinin that is concentrated in the cytoplasm (2). It plays a role in cell motility, invasion, and metastasis of cancer cells (3). Alpha-actinin 4 is commonly expressed in filopodia, lamellipodia, stress fibers, and sites of adhesion (4).
Recommended Applications
WB, IHC, ICC, IP
Applications and Recommended Dilution Factors
WB: 1:1,000 - 10,000
IHC: 1:100 - 250
ICC: 1:100 - 250
IP: 1:10 - 100
Species Reactivity
Human, Mouse, Rat
Mouse cross reactivity tested by western blot and IHC
Rat cross reactivity tested by western blot only
Products Data
Specificity
A synthetic peptide corresponding to residues on the N-terminus in human Alpha-Actinin 4 was used as an immunogen.
Storage Condition and Buffer
Store at -20 °C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
Alternative Names
ACTN4 antibody, ACTININ-4 antibody, DKFZp686K23158 antibody, FSGS antibody, FSGS1 antibody, Alpha-actinin-4 antibody, F-actin cross-linking protein antibody, Non-muscle alpha-actinin 4 antibody
Description References
1. Ylänne et al. Structure. 9(7):597-604, 2001. 2. Entrez Gene: gene-centered information at NCBI. Nucleic Acids Res. 2005 Jan 1;33:D54-8. 3. Yamada et al. Int J Oral Maxillofac Surg. 2009. 4. Otey and Carpen. Cell Motil. Cytoskeleton 58:104-111, 2004.
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