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ROCK2 Antibody (Internal)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, IF |
|---|---|
| Primary Accession | O75116 |
| Reactivity | Human, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 161kDa |
| Dilution | IHC-P (5 µg/ml), WB (1-2 µg/ml), |
| Gene ID | 9475 |
|---|---|
| Other Names | Rho-associated protein kinase 2, 2.7.11.1, Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase 2, Rho-associated, coiled-coil-containing protein kinase II, ROCK-II, p164 ROCK-2, ROCK2, KIAA0619 |
| Target/Specificity | Human ROCK2. Three isoforms of ROCK2 are known to exist; this antibody recognizes all three isoforms. ROCK2 antibody is predicted to not cross-react with other ROCK protein family members. |
| Reconstitution & Storage | Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. Store undiluted. |
| Precautions | ROCK2 Antibody (Internal) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ROCK2 |
|---|---|
| Synonyms | KIAA0619 |
| Function | Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1- p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation. |
| Cellular Location | Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Cytoplasmic, and associated with actin microfilaments and the plasma membrane. |
| Tissue Location | Expressed in the brain (at protein level). |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation.
References
Takahashi N.,et al.Genomics 55:235-237(1999).
Ishikawa K.,et al.DNA Res. 5:169-176(1998).
Hillier L.W.,et al.Nature 434:724-731(2005).
Kawano Y.,et al.J. Cell Biol. 147:1023-1038(1999).
Sebbagh M.,et al.J. Exp. Med. 201:465-471(2005).
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