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Proteintech rab22a rabbit polyclonal antibody

<t>RAB22A</t> increases cell‐surface EGFR expression. (a, c) Representative Western blot showing cell surface EGFR protein level on HeLa cells treated with vehicle, 25 µM Dyngo‐4a (a), or 150 µM primaquine (c). (b, d) Representative Western blot showing EGFR level on MV from HeLa cells treated with vehicle, 25 µM Dyngo‐4a (b), or 150 µM primaquine (d). (e) Representative Western blot showing EGFR level on MV from HeLa cells expressing Vector, HA‐RAB11A, HA‐RAB11A Q70L or HA‐RAB11A S25N . (f) Representative Western blot showing cell surface EGFR level on HeLa cells expressing vector or FLAG‐RAB22A. (g) Representative Western blot showing cell surface EGFR level on HeLa cells with or without RAB22A knockout. (h–j) Cell surface EGFR level in A549 (h), NCI‐H1975 (i) and NCI‐H820 (j) cell lines which was transduced with control small interfering RNA (si#NC) or siRNA targeting RAB22A (si#1 and si#2) for 48 h was analysed by flow cytometry. Data represent mean ± s.e.m.; p < 0.05 was considered significant; two‐tailed unpaired t ‐test. FLOT2 was used as a loading control.

Rab22a Rabbit Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 22 article reviews

rab22a rabbit polyclonal antibody - by Bioz Stars, 2026-10

93/100 stars

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1) Product Images from "RAB22A sorts epithelial growth factor receptor (EGFR) from early endosomes to recycling endosomes for microvesicles release"

Article Title: RAB22A sorts epithelial growth factor receptor (EGFR) from early endosomes to recycling endosomes for microvesicles release

Journal: Journal of Extracellular Vesicles

doi: 10.1002/jev2.12494

RAB22A increases cell‐surface EGFR expression. (a, c) Representative Western blot showing cell surface EGFR protein level on HeLa cells treated with vehicle, 25 µM Dyngo‐4a (a), or 150 µM primaquine (c). (b, d) Representative Western blot showing EGFR level on MV from HeLa cells treated with vehicle, 25 µM Dyngo‐4a (b), or 150 µM primaquine (d). (e) Representative Western blot showing EGFR level on MV from HeLa cells expressing Vector, HA‐RAB11A, HA‐RAB11A Q70L or HA‐RAB11A S25N . (f) Representative Western blot showing cell surface EGFR level on HeLa cells expressing vector or FLAG‐RAB22A. (g) Representative Western blot showing cell surface EGFR level on HeLa cells with or without RAB22A knockout. (h–j) Cell surface EGFR level in A549 (h), NCI‐H1975 (i) and NCI‐H820 (j) cell lines which was transduced with control small interfering RNA (si#NC) or siRNA targeting RAB22A (si#1 and si#2) for 48 h was analysed by flow cytometry. Data represent mean ± s.e.m.; p < 0.05 was considered significant; two‐tailed unpaired t ‐test. FLOT2 was used as a loading control.

Figure Legend Snippet: RAB22A increases cell‐surface EGFR expression. (a, c) Representative Western blot showing cell surface EGFR protein level on HeLa cells treated with vehicle, 25 µM Dyngo‐4a (a), or 150 µM primaquine (c). (b, d) Representative Western blot showing EGFR level on MV from HeLa cells treated with vehicle, 25 µM Dyngo‐4a (b), or 150 µM primaquine (d). (e) Representative Western blot showing EGFR level on MV from HeLa cells expressing Vector, HA‐RAB11A, HA‐RAB11A Q70L or HA‐RAB11A S25N . (f) Representative Western blot showing cell surface EGFR level on HeLa cells expressing vector or FLAG‐RAB22A. (g) Representative Western blot showing cell surface EGFR level on HeLa cells with or without RAB22A knockout. (h–j) Cell surface EGFR level in A549 (h), NCI‐H1975 (i) and NCI‐H820 (j) cell lines which was transduced with control small interfering RNA (si#NC) or siRNA targeting RAB22A (si#1 and si#2) for 48 h was analysed by flow cytometry. Data represent mean ± s.e.m.; p < 0.05 was considered significant; two‐tailed unpaired t ‐test. FLOT2 was used as a loading control.

Techniques Used: Expressing, Western Blot, Plasmid Preparation, Knock-Out, Transduction, Control, Small Interfering RNA, Flow Cytometry, Two Tailed Test

RAB22A engages SH3BP5L to activate RAB11A. (a) Localisation of FLAG‐RAB22A, EGFR‐HA and EGFP‐RAB11A in HeLa cells stably expressing FLAG‐RAB22A. Cells were co‐transfected with EGFR‐HA and EGFP‐RAB11A for 48 h. Pearson's correlation coefficients were calculated in the histogram, n = 30 cells. (b) Localisation of RAB22A, EGFR and RAB11A probed by anti‐RAB22A, anti‐EGFR and anti‐RAB11A antibodies respectively in NCI‐H1975 cells. Pearson's correlation coefficients were calculated in the histogram, n = 18 (EGFR/RAB11), 30 (RAB22A/RAB11) cells. (c) Whole cell lysate from HeLa cells stably expressing Vector or FLAG‐RAB22A was incubated with guanosine 5′‐triphosphate–agarose for 1.5 h, then the proteins were analysed by Western blot. (d) Whole cell lysate from HeLa cells with or without RAB22A knockout was incubated with guanosine 5′‐triphosphate–agarose for 1.5 h, then the proteins were analysed by Western blot. (e) HEK‐293T cells were transfected with the indicated plasmids. 48 h later, cells were lysed with RIPA and the lysate was incubated with anti‐HA agarose. Proteins were analysed by Western blot. (f) Localisation of HA‐SH3BP5 and HA‐SH3BP5L in HeLa cells stably expressing FLAG‐RAB22A. Cells were transiently transfected with HA‐SH3BP5 or HA‐SH3BP5L plasmid for 48 h. Pearson's correlation coefficients were calculated in the histogram, n = 32 (SH3BP5), 33 (SH3BP5L) cells. Data represent mean ± s.e.m.; p < 0.05 was considered significant; two‐tailed unpaired t ‐test. (g) Whole cell lysate from indicated cell lines were incubated with GST‐FIP3RBD‐coated beads and the proteins were analysed by Western blot. (h) HEK‐293T was transiently co‐transfected with FLAG‐RAB22A and indicated truncated mutants of SH3BP5L for 48 h. Cells were lysed with RIPA and the lysate was incubated with anti‐HA agarose. Proteins were analysed by Western blot.

Figure Legend Snippet: RAB22A engages SH3BP5L to activate RAB11A. (a) Localisation of FLAG‐RAB22A, EGFR‐HA and EGFP‐RAB11A in HeLa cells stably expressing FLAG‐RAB22A. Cells were co‐transfected with EGFR‐HA and EGFP‐RAB11A for 48 h. Pearson's correlation coefficients were calculated in the histogram, n = 30 cells. (b) Localisation of RAB22A, EGFR and RAB11A probed by anti‐RAB22A, anti‐EGFR and anti‐RAB11A antibodies respectively in NCI‐H1975 cells. Pearson's correlation coefficients were calculated in the histogram, n = 18 (EGFR/RAB11), 30 (RAB22A/RAB11) cells. (c) Whole cell lysate from HeLa cells stably expressing Vector or FLAG‐RAB22A was incubated with guanosine 5′‐triphosphate–agarose for 1.5 h, then the proteins were analysed by Western blot. (d) Whole cell lysate from HeLa cells with or without RAB22A knockout was incubated with guanosine 5′‐triphosphate–agarose for 1.5 h, then the proteins were analysed by Western blot. (e) HEK‐293T cells were transfected with the indicated plasmids. 48 h later, cells were lysed with RIPA and the lysate was incubated with anti‐HA agarose. Proteins were analysed by Western blot. (f) Localisation of HA‐SH3BP5 and HA‐SH3BP5L in HeLa cells stably expressing FLAG‐RAB22A. Cells were transiently transfected with HA‐SH3BP5 or HA‐SH3BP5L plasmid for 48 h. Pearson's correlation coefficients were calculated in the histogram, n = 32 (SH3BP5), 33 (SH3BP5L) cells. Data represent mean ± s.e.m.; p < 0.05 was considered significant; two‐tailed unpaired t ‐test. (g) Whole cell lysate from indicated cell lines were incubated with GST‐FIP3RBD‐coated beads and the proteins were analysed by Western blot. (h) HEK‐293T was transiently co‐transfected with FLAG‐RAB22A and indicated truncated mutants of SH3BP5L for 48 h. Cells were lysed with RIPA and the lysate was incubated with anti‐HA agarose. Proteins were analysed by Western blot.

Techniques Used: Stable Transfection, Expressing, Transfection, Plasmid Preparation, Incubation, Western Blot, Knock-Out, Two Tailed Test

Tyr136 in RAB22A is phosphorylated by EGFR. (a) Representative Western blot of RAB22A tyrosine phosphorylation (pY) by EGFR and its mutants. HEK‐293T cells were transiently co‐transfected with the indicated plasmids, 42 h later, the medium was replaced with serum‐free DMEM and cells were cultured for another 6 h. (b) Localisation of EGFR pY1068 and EGFR T790M/L858R (EGFR M2 ‐HA) in HeLa cells stably expressing FLAG‐RAB22A. (c) Representative Western blot of tyrosine phosphorylation of RABB22A (pY) by EGFR M2 ‐HA in HEK‐293T. Cells were co‐transfected with the indicated plasmids. After 42 h, the medium was replaced with serum‐free DMEM in the absence and presence of 1 µM specific TKIs for another 6 h. (d) Representative Western blot to identify tyrosine in RAB22A phosphorylated by EGFR and its active mutants. HEK‐293T cells were co‐transfected with the indicated plasmids, 42 h later, the medium was replaced with serum‐free DMEM and cells were cultured for another 6 h. (e) In vitro kinase assay.

Figure Legend Snippet: Tyr136 in RAB22A is phosphorylated by EGFR. (a) Representative Western blot of RAB22A tyrosine phosphorylation (pY) by EGFR and its mutants. HEK‐293T cells were transiently co‐transfected with the indicated plasmids, 42 h later, the medium was replaced with serum‐free DMEM and cells were cultured for another 6 h. (b) Localisation of EGFR pY1068 and EGFR T790M/L858R (EGFR M2 ‐HA) in HeLa cells stably expressing FLAG‐RAB22A. (c) Representative Western blot of tyrosine phosphorylation of RABB22A (pY) by EGFR M2 ‐HA in HEK‐293T. Cells were co‐transfected with the indicated plasmids. After 42 h, the medium was replaced with serum‐free DMEM in the absence and presence of 1 µM specific TKIs for another 6 h. (d) Representative Western blot to identify tyrosine in RAB22A phosphorylated by EGFR and its active mutants. HEK‐293T cells were co‐transfected with the indicated plasmids, 42 h later, the medium was replaced with serum‐free DMEM and cells were cultured for another 6 h. (e) In vitro kinase assay.

Techniques Used: Western Blot, Phospho-proteomics, Transfection, Cell Culture, Stable Transfection, Expressing, In Vitro, Kinase Assay

Phosphorylation of Tyr136 in RAB22A by EGFR promotes EGFR‐containing MV formation. (a) Representative Western blot of MV sample released by HeLa cells with RAB22A and wild‐type or constitutively active form of EGFR overexpression. (b) Representative Western blot of MV sample released by HeLa cells with RAB22A and wild‐type or kinase dead form of EGFR overexpression. (c) Representative Western blot of MV from HeLa cells in the presence or absence of 1 µM Afatinib for 48 h. (d) Representative Western blot of MV from HeLa cells stably expressing EGFR M2 ‐HA and V5‐RAB22A or its Y136F mutant. (e) Representative Western blot of MV from NCI‐H1975 cells with or without RAB22A knockout followed by RAB22A or its Y136F mutant re‐expression. FLOT2 was used as a loading control.

Figure Legend Snippet: Phosphorylation of Tyr136 in RAB22A by EGFR promotes EGFR‐containing MV formation. (a) Representative Western blot of MV sample released by HeLa cells with RAB22A and wild‐type or constitutively active form of EGFR overexpression. (b) Representative Western blot of MV sample released by HeLa cells with RAB22A and wild‐type or kinase dead form of EGFR overexpression. (c) Representative Western blot of MV from HeLa cells in the presence or absence of 1 µM Afatinib for 48 h. (d) Representative Western blot of MV from HeLa cells stably expressing EGFR M2 ‐HA and V5‐RAB22A or its Y136F mutant. (e) Representative Western blot of MV from NCI‐H1975 cells with or without RAB22A knockout followed by RAB22A or its Y136F mutant re‐expression. FLOT2 was used as a loading control.

Techniques Used: Phospho-proteomics, Western Blot, Over Expression, Stable Transfection, Expressing, Mutagenesis, Knock-Out, Control

Proposed model by which RAB22A links the endocytosis and recycling pathway to promote MVs release. RAB22A recruits TBC1D2B to inactivate RAB7, and further prevents EGFR from being transported to late endosomes and later lysosomes for degradation, which constructs a reserve pool ready for recycling. RAB22A also engages SH3BP5L to promote RAB11A activation and increase cell‐surface EGFR protein level, which ultimately facilitates the release of EGFR‐containing MVs. Moreover, RAB22A can be phosphorylated by active EGFR, forming a positive feedback loop to promote the release of EGFR‐containing MVs.

Figure Legend Snippet: Proposed model by which RAB22A links the endocytosis and recycling pathway to promote MVs release. RAB22A recruits TBC1D2B to inactivate RAB7, and further prevents EGFR from being transported to late endosomes and later lysosomes for degradation, which constructs a reserve pool ready for recycling. RAB22A also engages SH3BP5L to promote RAB11A activation and increase cell‐surface EGFR protein level, which ultimately facilitates the release of EGFR‐containing MVs. Moreover, RAB22A can be phosphorylated by active EGFR, forming a positive feedback loop to promote the release of EGFR‐containing MVs.

Techniques Used: Construct, Activation Assay

Expressing:

Article Title: RAB22A sorts epithelial growth factor receptor (EGFR) from early endosomes to recycling endosomes for microvesicles release
Article Snippet: Antibodies purchased from Proteintech Group: RAB22A Rabbit Polyclonal antibody (12125‐1‐AP, 1:500), ARF6 Rabbit Polyclonal antibody (20225‐1‐AP, 1:3000), Tsg101 Antibody (4497‐1‐AP, 1:3000), RAB11A‐Specific Polyclonal Antibody (20229‐1‐AP, 1: 500), RAB7A Antibody (55469‐1‐AP, 1:500).

Western Blot:

Plasmid Preparation:

Knock-Out:

Transduction:

Control:

Small Interfering RNA:

Flow Cytometry:

Two Tailed Test:

Stable Transfection:

Transfection:

Incubation:

Phospho-proteomics:

Cell Culture:

In Vitro:

Kinase Assay:

Over Expression:

Mutagenesis:

Construct:

Activation Assay:

Image Search Results

Journal: Journal of Extracellular Vesicles

Article Title: RAB22A sorts epithelial growth factor receptor (EGFR) from early endosomes to recycling endosomes for microvesicles release

doi: 10.1002/jev2.12494

Figure Lengend Snippet: RAB22A increases cell‐surface EGFR expression. (a, c) Representative Western blot showing cell surface EGFR protein level on HeLa cells treated with vehicle, 25 µM Dyngo‐4a (a), or 150 µM primaquine (c). (b, d) Representative Western blot showing EGFR level on MV from HeLa cells treated with vehicle, 25 µM Dyngo‐4a (b), or 150 µM primaquine (d). (e) Representative Western blot showing EGFR level on MV from HeLa cells expressing Vector, HA‐RAB11A, HA‐RAB11A Q70L or HA‐RAB11A S25N . (f) Representative Western blot showing cell surface EGFR level on HeLa cells expressing vector or FLAG‐RAB22A. (g) Representative Western blot showing cell surface EGFR level on HeLa cells with or without RAB22A knockout. (h–j) Cell surface EGFR level in A549 (h), NCI‐H1975 (i) and NCI‐H820 (j) cell lines which was transduced with control small interfering RNA (si#NC) or siRNA targeting RAB22A (si#1 and si#2) for 48 h was analysed by flow cytometry. Data represent mean ± s.e.m.; p < 0.05 was considered significant; two‐tailed unpaired t ‐test. FLOT2 was used as a loading control.

Article Snippet: Antibodies purchased from Proteintech Group: RAB22A Rabbit Polyclonal antibody (12125‐1‐AP, 1:500), ARF6 Rabbit Polyclonal antibody (20225‐1‐AP, 1:3000), Tsg101 Antibody (4497‐1‐AP, 1:3000), RAB11A‐Specific Polyclonal Antibody (20229‐1‐AP, 1: 500), RAB7A Antibody (55469‐1‐AP, 1:500).

Techniques: Expressing, Western Blot, Plasmid Preparation, Knock-Out, Transduction, Control, Small Interfering RNA, Flow Cytometry, Two Tailed Test

Journal: Journal of Extracellular Vesicles

Article Title: RAB22A sorts epithelial growth factor receptor (EGFR) from early endosomes to recycling endosomes for microvesicles release

doi: 10.1002/jev2.12494

Figure Lengend Snippet: RAB22A engages SH3BP5L to activate RAB11A. (a) Localisation of FLAG‐RAB22A, EGFR‐HA and EGFP‐RAB11A in HeLa cells stably expressing FLAG‐RAB22A. Cells were co‐transfected with EGFR‐HA and EGFP‐RAB11A for 48 h. Pearson's correlation coefficients were calculated in the histogram, n = 30 cells. (b) Localisation of RAB22A, EGFR and RAB11A probed by anti‐RAB22A, anti‐EGFR and anti‐RAB11A antibodies respectively in NCI‐H1975 cells. Pearson's correlation coefficients were calculated in the histogram, n = 18 (EGFR/RAB11), 30 (RAB22A/RAB11) cells. (c) Whole cell lysate from HeLa cells stably expressing Vector or FLAG‐RAB22A was incubated with guanosine 5′‐triphosphate–agarose for 1.5 h, then the proteins were analysed by Western blot. (d) Whole cell lysate from HeLa cells with or without RAB22A knockout was incubated with guanosine 5′‐triphosphate–agarose for 1.5 h, then the proteins were analysed by Western blot. (e) HEK‐293T cells were transfected with the indicated plasmids. 48 h later, cells were lysed with RIPA and the lysate was incubated with anti‐HA agarose. Proteins were analysed by Western blot. (f) Localisation of HA‐SH3BP5 and HA‐SH3BP5L in HeLa cells stably expressing FLAG‐RAB22A. Cells were transiently transfected with HA‐SH3BP5 or HA‐SH3BP5L plasmid for 48 h. Pearson's correlation coefficients were calculated in the histogram, n = 32 (SH3BP5), 33 (SH3BP5L) cells. Data represent mean ± s.e.m.; p < 0.05 was considered significant; two‐tailed unpaired t ‐test. (g) Whole cell lysate from indicated cell lines were incubated with GST‐FIP3RBD‐coated beads and the proteins were analysed by Western blot. (h) HEK‐293T was transiently co‐transfected with FLAG‐RAB22A and indicated truncated mutants of SH3BP5L for 48 h. Cells were lysed with RIPA and the lysate was incubated with anti‐HA agarose. Proteins were analysed by Western blot.

Techniques: Stable Transfection, Expressing, Transfection, Plasmid Preparation, Incubation, Western Blot, Knock-Out, Two Tailed Test

Journal: Journal of Extracellular Vesicles

Article Title: RAB22A sorts epithelial growth factor receptor (EGFR) from early endosomes to recycling endosomes for microvesicles release

doi: 10.1002/jev2.12494

Figure Lengend Snippet: Tyr136 in RAB22A is phosphorylated by EGFR. (a) Representative Western blot of RAB22A tyrosine phosphorylation (pY) by EGFR and its mutants. HEK‐293T cells were transiently co‐transfected with the indicated plasmids, 42 h later, the medium was replaced with serum‐free DMEM and cells were cultured for another 6 h. (b) Localisation of EGFR pY1068 and EGFR T790M/L858R (EGFR M2 ‐HA) in HeLa cells stably expressing FLAG‐RAB22A. (c) Representative Western blot of tyrosine phosphorylation of RABB22A (pY) by EGFR M2 ‐HA in HEK‐293T. Cells were co‐transfected with the indicated plasmids. After 42 h, the medium was replaced with serum‐free DMEM in the absence and presence of 1 µM specific TKIs for another 6 h. (d) Representative Western blot to identify tyrosine in RAB22A phosphorylated by EGFR and its active mutants. HEK‐293T cells were co‐transfected with the indicated plasmids, 42 h later, the medium was replaced with serum‐free DMEM and cells were cultured for another 6 h. (e) In vitro kinase assay.

Techniques: Western Blot, Phospho-proteomics, Transfection, Cell Culture, Stable Transfection, Expressing, In Vitro, Kinase Assay

Journal: Journal of Extracellular Vesicles

Article Title: RAB22A sorts epithelial growth factor receptor (EGFR) from early endosomes to recycling endosomes for microvesicles release

doi: 10.1002/jev2.12494

Figure Lengend Snippet: Phosphorylation of Tyr136 in RAB22A by EGFR promotes EGFR‐containing MV formation. (a) Representative Western blot of MV sample released by HeLa cells with RAB22A and wild‐type or constitutively active form of EGFR overexpression. (b) Representative Western blot of MV sample released by HeLa cells with RAB22A and wild‐type or kinase dead form of EGFR overexpression. (c) Representative Western blot of MV from HeLa cells in the presence or absence of 1 µM Afatinib for 48 h. (d) Representative Western blot of MV from HeLa cells stably expressing EGFR M2 ‐HA and V5‐RAB22A or its Y136F mutant. (e) Representative Western blot of MV from NCI‐H1975 cells with or without RAB22A knockout followed by RAB22A or its Y136F mutant re‐expression. FLOT2 was used as a loading control.

Techniques: Phospho-proteomics, Western Blot, Over Expression, Stable Transfection, Expressing, Mutagenesis, Knock-Out, Control

Journal: Journal of Extracellular Vesicles

Article Title: RAB22A sorts epithelial growth factor receptor (EGFR) from early endosomes to recycling endosomes for microvesicles release

doi: 10.1002/jev2.12494

Figure Lengend Snippet: Proposed model by which RAB22A links the endocytosis and recycling pathway to promote MVs release. RAB22A recruits TBC1D2B to inactivate RAB7, and further prevents EGFR from being transported to late endosomes and later lysosomes for degradation, which constructs a reserve pool ready for recycling. RAB22A also engages SH3BP5L to promote RAB11A activation and increase cell‐surface EGFR protein level, which ultimately facilitates the release of EGFR‐containing MVs. Moreover, RAB22A can be phosphorylated by active EGFR, forming a positive feedback loop to promote the release of EGFR‐containing MVs.

Techniques: Construct, Activation Assay

Rab22a is overexpressed in thyroid malignancies. GEPIA database showed the relationship between the expression of RAB22A with tumors ( P = 0.01), BRAF mutations ( P = 0), and stages (Pr = 0.206) (a). Representative images of Rab22a protein expression in papillary thyroid carcinoma, thyroid follicular carcinoma, medullary thyroid carcinoma, and nodular goiter tissues (b, 100×). UALCAN analysis showed that the patients with high RAB22A expression had poorer overall survival (c).

Journal: BioMed Research International

Article Title: Rab22a Promotes Epithelial-Mesenchymal Transition in Papillary Thyroid Carcinoma by Activating PI3K/AKT/mTOR Signaling Pathway

doi: 10.1155/2022/1874550

Figure Lengend Snippet: Rab22a is overexpressed in thyroid malignancies. GEPIA database showed the relationship between the expression of RAB22A with tumors ( P = 0.01), BRAF mutations ( P = 0), and stages (Pr = 0.206) (a). Representative images of Rab22a protein expression in papillary thyroid carcinoma, thyroid follicular carcinoma, medullary thyroid carcinoma, and nodular goiter tissues (b, 100×). UALCAN analysis showed that the patients with high RAB22A expression had poorer overall survival (c).

Article Snippet: The sections were incubated with anti-Rab22a rabbit polyclonal antibody (1 : 500, HPA066920, Sigma-Aldrich, Shanghai, China) at 4°C overnight.

Techniques: Expressing

Association between Rab22a expression and clinical parameters in 101 patients with thyroid disease.

Journal: BioMed Research International

Article Title: Rab22a Promotes Epithelial-Mesenchymal Transition in Papillary Thyroid Carcinoma by Activating PI3K/AKT/mTOR Signaling Pathway

doi: 10.1155/2022/1874550

Figure Lengend Snippet: Association between Rab22a expression and clinical parameters in 101 patients with thyroid disease.

Article Snippet: The sections were incubated with anti-Rab22a rabbit polyclonal antibody (1 : 500, HPA066920, Sigma-Aldrich, Shanghai, China) at 4°C overnight.

Techniques: Expressing

Rab22a promotes malignant biological behaviors in thyroid cancer cells. The level of Rab22a was increased or decreased after transfection with different plasmids or specific interference plasmids of Rab22a, respectively (a). Rab22a promoted the proliferation of TPC1 and K1 cells, as shown by colony formation and CCK8 assays (b and c). Statistical data were the mean ± SD of the three repeated independent trials: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Journal: BioMed Research International

Article Title: Rab22a Promotes Epithelial-Mesenchymal Transition in Papillary Thyroid Carcinoma by Activating PI3K/AKT/mTOR Signaling Pathway

doi: 10.1155/2022/1874550

Figure Lengend Snippet: Rab22a promotes malignant biological behaviors in thyroid cancer cells. The level of Rab22a was increased or decreased after transfection with different plasmids or specific interference plasmids of Rab22a, respectively (a). Rab22a promoted the proliferation of TPC1 and K1 cells, as shown by colony formation and CCK8 assays (b and c). Statistical data were the mean ± SD of the three repeated independent trials: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Article Snippet: The sections were incubated with anti-Rab22a rabbit polyclonal antibody (1 : 500, HPA066920, Sigma-Aldrich, Shanghai, China) at 4°C overnight.

Techniques: Transfection

Rab22a promotes the migration and invasion of thyroid cancer cells. Transwell assays showed that Rab22aWT increased the migration and invasion abilities of TPC1 and K1 cells, and Rab22a knockdown showed the opposite effect (a, 200×). The migration ability of TPC1 and K1 cells was assessed by wound healing assays (b, 200×). Statistical data were the mean ± SD of the three repeated independent trials: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Journal: BioMed Research International

Article Title: Rab22a Promotes Epithelial-Mesenchymal Transition in Papillary Thyroid Carcinoma by Activating PI3K/AKT/mTOR Signaling Pathway

doi: 10.1155/2022/1874550

Figure Lengend Snippet: Rab22a promotes the migration and invasion of thyroid cancer cells. Transwell assays showed that Rab22aWT increased the migration and invasion abilities of TPC1 and K1 cells, and Rab22a knockdown showed the opposite effect (a, 200×). The migration ability of TPC1 and K1 cells was assessed by wound healing assays (b, 200×). Statistical data were the mean ± SD of the three repeated independent trials: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Article Snippet: The sections were incubated with anti-Rab22a rabbit polyclonal antibody (1 : 500, HPA066920, Sigma-Aldrich, Shanghai, China) at 4°C overnight.

Techniques: Migration

The effect of Rab22a on PI3K/AKT/mTOR signaling pathway. Western blot analysis of the expression of PI3Kp85 α , p-PI3K, AKT, p-AKT (Ser473), mTOR, p-mTOR (Ser2448), p70S6K, p-p70S6K (Ser371), p-p70S6K (Thr389), p-4E-BP1 (Thr37/46), and Rab22a in TPC1 and K1 cells (a and b). Statistical data were the mean ± SD of the three repeated independent trials: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Journal: BioMed Research International

Article Title: Rab22a Promotes Epithelial-Mesenchymal Transition in Papillary Thyroid Carcinoma by Activating PI3K/AKT/mTOR Signaling Pathway

doi: 10.1155/2022/1874550

Figure Lengend Snippet: The effect of Rab22a on PI3K/AKT/mTOR signaling pathway. Western blot analysis of the expression of PI3Kp85 α , p-PI3K, AKT, p-AKT (Ser473), mTOR, p-mTOR (Ser2448), p70S6K, p-p70S6K (Ser371), p-p70S6K (Thr389), p-4E-BP1 (Thr37/46), and Rab22a in TPC1 and K1 cells (a and b). Statistical data were the mean ± SD of the three repeated independent trials: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Article Snippet: The sections were incubated with anti-Rab22a rabbit polyclonal antibody (1 : 500, HPA066920, Sigma-Aldrich, Shanghai, China) at 4°C overnight.

Techniques: Western Blot, Expressing

The influence of Rab22a on PI3K/AKT/mTOR signaling pathway. The western blot analysis results revealed that the expression of p-PI3K, p-AKT (Ser473), p-mTOR (Ser2448), and Rab22a induced by Rab22a overexpression or decreased by PI3K inhibitors in TPC1 and K1 (a and b). Statistical data were the mean ± SD of the three repeated independent trials: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Journal: BioMed Research International

Article Title: Rab22a Promotes Epithelial-Mesenchymal Transition in Papillary Thyroid Carcinoma by Activating PI3K/AKT/mTOR Signaling Pathway

doi: 10.1155/2022/1874550

Figure Lengend Snippet: The influence of Rab22a on PI3K/AKT/mTOR signaling pathway. The western blot analysis results revealed that the expression of p-PI3K, p-AKT (Ser473), p-mTOR (Ser2448), and Rab22a induced by Rab22a overexpression or decreased by PI3K inhibitors in TPC1 and K1 (a and b). Statistical data were the mean ± SD of the three repeated independent trials: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Article Snippet: The sections were incubated with anti-Rab22a rabbit polyclonal antibody (1 : 500, HPA066920, Sigma-Aldrich, Shanghai, China) at 4°C overnight.

Techniques: Western Blot, Expressing, Over Expression

The PI3K inhibitors reduced Rab22a promoting the proliferation of thyroid cancer cells. The TPC1 and K1 cell proliferation were decreased by PI3K inhibitor treatment, as shown by CCK8 and colony formation assays (a and b). Data are shown as mean ± SD of the three independent experiments: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Journal: BioMed Research International

Article Title: Rab22a Promotes Epithelial-Mesenchymal Transition in Papillary Thyroid Carcinoma by Activating PI3K/AKT/mTOR Signaling Pathway

doi: 10.1155/2022/1874550

Figure Lengend Snippet: The PI3K inhibitors reduced Rab22a promoting the proliferation of thyroid cancer cells. The TPC1 and K1 cell proliferation were decreased by PI3K inhibitor treatment, as shown by CCK8 and colony formation assays (a and b). Data are shown as mean ± SD of the three independent experiments: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Article Snippet: The sections were incubated with anti-Rab22a rabbit polyclonal antibody (1 : 500, HPA066920, Sigma-Aldrich, Shanghai, China) at 4°C overnight.

Techniques:

Rab22a promotes the EMT process of thyroid cancer cells. The western blot analysis results revealed the expression of EMT-related proteins induced by Rab22a overexpression or knockdown in TPC1 (a) and K1 cells (b). Statistical data were the mean ± SD of the three repeated independent trials, ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Journal: BioMed Research International

Article Title: Rab22a Promotes Epithelial-Mesenchymal Transition in Papillary Thyroid Carcinoma by Activating PI3K/AKT/mTOR Signaling Pathway

doi: 10.1155/2022/1874550

Figure Lengend Snippet: Rab22a promotes the EMT process of thyroid cancer cells. The western blot analysis results revealed the expression of EMT-related proteins induced by Rab22a overexpression or knockdown in TPC1 (a) and K1 cells (b). Statistical data were the mean ± SD of the three repeated independent trials, ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Article Snippet: The sections were incubated with anti-Rab22a rabbit polyclonal antibody (1 : 500, HPA066920, Sigma-Aldrich, Shanghai, China) at 4°C overnight.

Techniques: Western Blot, Expressing, Over Expression

Rab22a regulated the EMT process of thyroid cancer cells via PI3K/AKT/mTOR signaling pathway. Western blot analysis showed that the expression of EMT-related proteins upon Rab22a transfection was changed after treatment with PI3K inhibitors (a, b). Statistical data were the mean ± SD of the three repeated independent trials: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Journal: BioMed Research International

Article Title: Rab22a Promotes Epithelial-Mesenchymal Transition in Papillary Thyroid Carcinoma by Activating PI3K/AKT/mTOR Signaling Pathway

doi: 10.1155/2022/1874550

Figure Lengend Snippet: Rab22a regulated the EMT process of thyroid cancer cells via PI3K/AKT/mTOR signaling pathway. Western blot analysis showed that the expression of EMT-related proteins upon Rab22a transfection was changed after treatment with PI3K inhibitors (a, b). Statistical data were the mean ± SD of the three repeated independent trials: ∗∗∗ P < 0.001, ∗∗ P < 0.01, and ∗ P < 0.05.

Article Snippet: The sections were incubated with anti-Rab22a rabbit polyclonal antibody (1 : 500, HPA066920, Sigma-Aldrich, Shanghai, China) at 4°C overnight.

Techniques: Western Blot, Expressing, Transfection

In vitro antitumor activity of HA-mExo-miR204. ( A ) Cancer cells were incubated with mExo-miR204 or HA-mExo-miR204 for 6 h, and the anti-proliferation effect was determined by CCK-8 assays. ( B ) Cells were grown at a low density for 8 days and the anti-proliferation effect of mExo-miR204 and HA-mExo-miR204 on single tumorigenic cells was determined by a colony formation assay. MDA-MB-231 ( C ) and MCF-7 ( D ) cells were treated with PBS or HA-mExo-miR204 for 12 h and the expressions of BCL2 and RAB22A were determined by Western blotting. * p < 0.05, *** p < 0.001, **** p < 0.0001.

Journal: Cells

Article Title: Hyaluronic Acid-Coated Bovine Milk Exosomes for Achieving Tumor-Specific Intracellular Delivery of miRNA-204

doi: 10.3390/cells11193065

Figure Lengend Snippet: In vitro antitumor activity of HA-mExo-miR204. ( A ) Cancer cells were incubated with mExo-miR204 or HA-mExo-miR204 for 6 h, and the anti-proliferation effect was determined by CCK-8 assays. ( B ) Cells were grown at a low density for 8 days and the anti-proliferation effect of mExo-miR204 and HA-mExo-miR204 on single tumorigenic cells was determined by a colony formation assay. MDA-MB-231 ( C ) and MCF-7 ( D ) cells were treated with PBS or HA-mExo-miR204 for 12 h and the expressions of BCL2 and RAB22A were determined by Western blotting. * p < 0.05, *** p < 0.001, **** p < 0.0001.

Article Snippet: Anti-RAB22A rabbit polyclonal antibody (IgG, 12125-1-AP) was purchased from Proteintech (Chicago, IL, USA).

Techniques: In Vitro, Activity Assay, Incubation, CCK-8 Assay, Colony Assay, Western Blot

IHC analysis of RAB22A and BCL2 protein expressions in xenograft tumor. Sections of tumor tissues from mice were stained with RAB22A and BCL2 antibodies. Black boxed regions are enlarged in the right images. Scale bars: 100 μm (left); 20 μm (right).

Journal: Cells

Article Title: Hyaluronic Acid-Coated Bovine Milk Exosomes for Achieving Tumor-Specific Intracellular Delivery of miRNA-204

doi: 10.3390/cells11193065

Figure Lengend Snippet: IHC analysis of RAB22A and BCL2 protein expressions in xenograft tumor. Sections of tumor tissues from mice were stained with RAB22A and BCL2 antibodies. Black boxed regions are enlarged in the right images. Scale bars: 100 μm (left); 20 μm (right).

Article Snippet: Anti-RAB22A rabbit polyclonal antibody (IgG, 12125-1-AP) was purchased from Proteintech (Chicago, IL, USA).

Techniques: Staining

Review

rab22a rabbit polyclonal antibody (Proteintech)

Structured Review

Images

1) Product Images from "RAB22A sorts epithelial growth factor receptor (EGFR) from early endosomes to recycling endosomes for microvesicles release"

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Expressing:

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Transduction:

Control:

Small Interfering RNA:

Flow Cytometry:

Two Tailed Test:

Stable Transfection:

Transfection:

Incubation:

Phospho-proteomics:

Cell Culture:

In Vitro:

Kinase Assay:

Over Expression:

Mutagenesis:

Construct:

Activation Assay:

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