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Western blotAntibody data
- Antibody Data
- Antigen structure
- References [5]
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- Validations
- Western blot [1]
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- Product number
- AF5345 - Provider product page
- Provider
- R&D Systems
- Product name
- Human Girdin Antibody
- Antibody type
- Polyclonal
- Description
- Immunogen affinity purified. Detects endogenous human Girdin in Western blots.
- Reactivity
- Human
- Host
- Sheep
- Conjugate
- Unconjugated
- Antigen sequence
Q3V6T2- Isotype
- IgG
- Vial size
- 100 ug
- Concentration
- LYOPH
- Storage
- Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Submitted references Akt-Girdin signaling in cancer-associated fibroblasts contributes to tumor progression.
Loss of Dlg5 expression promotes the migration and invasion of prostate cancer cells via Girdin phosphorylation.
Speed control for neuronal migration in the postnatal brain by Gmip-mediated local inactivation of RhoA.
Girdin and its phosphorylation dynamically regulate neonatal vascular development and pathological neovascularization in the retina.
Proteomic analysis of Girdin-interacting proteins in migrating new neurons in the postnatal mouse brain.
Yamamura Y, Asai N, Enomoto A, Kato T, Mii S, Kondo Y, Ushida K, Niimi K, Tsunoda N, Nagino M, Ichihara S, Furukawa K, Maeda K, Murohara T, Takahashi M
Cancer research 2015 Mar 1;75(5):813-23
Cancer research 2015 Mar 1;75(5):813-23
Loss of Dlg5 expression promotes the migration and invasion of prostate cancer cells via Girdin phosphorylation.
Tomiyama L, Sezaki T, Matsuo M, Ueda K, Kioka N
Oncogene 2015 Feb 26;34(9):1141-9
Oncogene 2015 Feb 26;34(9):1141-9
Speed control for neuronal migration in the postnatal brain by Gmip-mediated local inactivation of RhoA.
Ota H, Hikita T, Sawada M, Nishioka T, Matsumoto M, Komura M, Ohno A, Kamiya Y, Miyamoto T, Asai N, Enomoto A, Takahashi M, Kaibuchi K, Sobue K, Sawamoto K
Nature communications 2014 Jul 30;5:4532
Nature communications 2014 Jul 30;5:4532
Girdin and its phosphorylation dynamically regulate neonatal vascular development and pathological neovascularization in the retina.
Ito T, Komeima K, Yasuma T, Enomoto A, Asai N, Asai M, Iwase S, Takahashi M, Terasaki H
The American journal of pathology 2013 Feb;182(2):586-96
The American journal of pathology 2013 Feb;182(2):586-96
Proteomic analysis of Girdin-interacting proteins in migrating new neurons in the postnatal mouse brain.
Ota H, Hikita T, Nishioka T, Matsumoto M, Ito J, Asai N, Enomoto A, Takahashi M, Kaibuchi K, Sobue K, Sawamoto K
Biochemical and biophysical research communications 2013 Dec 6;442(1-2):16-21
Biochemical and biophysical research communications 2013 Dec 6;442(1-2):16-21
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Supportive validation
- Submitted by
- R&D Systems (provider)
- Main image
- Experimental details
- Detection of Human Girdin by Western Blot. Western blot shows lysates of H69AR human small cell lung cancer cell line, MRC-5 human embryonic lung fibroblast cell line, and A431 human epithelial carcinoma cell line. PVDF membrane was probed with 1 µg/mL of Human Girdin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5345) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Girdin at approximately 200 to 220 kDa (as indicated). This experiment was conducted using Immunoblot Buffer Group 1.
