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fgfr4 peptide  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology fgfr4 peptide
    FIG. 1. Detection of <t>FGFR4</t> reactivity in pituitary cells. A–D, Immunohistochem- ical localization of FGFR4 in human pi- tuitary adenomas. C-terminal FGFR4 immunoreactivity is seen in the cyto- plasm of tumor cells in varied tumor types. A, GH cell adenoma. B, ACTH cell adenoma. C, FSH/LH adenoma. D, Null cell adenoma. The immunoreactivity of FGFR4 is variable but always very in- tense throughout the cytoplasm (original magnification 50–100). E and F, Im- munohistochemical localization of FGFR4 and ptd-FGFR4 in transfected pituitary cells. Rat pituitary tumor-derived GH4 cells were stably transfected with full- length FGFR4 (E) or ptd-FGFR4 (F). Im- munocytochemical examination was per- formed using an antibody that recognizes the C terminus of FGFR4. Note the pre- dominant cytoplasmic pattern of staining in ptd-FGFR4 transfected cells, com- pared with the membrane reactivity in wild-type FGFR4-transfected cells. G, Western blot detection of FGFR4 in hu- man pituitary adenomas. Protein lysates from seven human gonadotroph adeno- mas were electrophoresed and blotted with an antibody that recognizes the C terminus of FGFR4. The extreme right lane contains a positive control from HEK293 cells transiently transfected with ptd-FGFR4 (upper panel). Preab- sorption of the primary antibody with pu- rified antigen abolishes the lower 65-kDa protein (lower panel). The band migrat- ing just above 65 kDa is a nonspecific species that is not abolished by preab- sorption.
    Fgfr4 Peptide, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 171 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fgfr4+peptide/pm15070963-72-28-30?v=Santa+Cruz+Biotechnology
    Average 94 stars, based on 171 article reviews
    fgfr4 peptide - by Bioz Stars, 2026-07
    94/100 stars

    Images

    1) Product Images from "Cytoplasmic expression of fibroblast growth factor receptor-4 in human pituitary adenomas: relation to tumor type, size, proliferation, and invasiveness."

    Article Title: Cytoplasmic expression of fibroblast growth factor receptor-4 in human pituitary adenomas: relation to tumor type, size, proliferation, and invasiveness.

    Journal: The Journal of clinical endocrinology and metabolism

    doi: 10.1210/jc.2003-031489

    FIG. 1. Detection of FGFR4 reactivity in pituitary cells. A–D, Immunohistochem- ical localization of FGFR4 in human pi- tuitary adenomas. C-terminal FGFR4 immunoreactivity is seen in the cyto- plasm of tumor cells in varied tumor types. A, GH cell adenoma. B, ACTH cell adenoma. C, FSH/LH adenoma. D, Null cell adenoma. The immunoreactivity of FGFR4 is variable but always very in- tense throughout the cytoplasm (original magnification 50–100). E and F, Im- munohistochemical localization of FGFR4 and ptd-FGFR4 in transfected pituitary cells. Rat pituitary tumor-derived GH4 cells were stably transfected with full- length FGFR4 (E) or ptd-FGFR4 (F). Im- munocytochemical examination was per- formed using an antibody that recognizes the C terminus of FGFR4. Note the pre- dominant cytoplasmic pattern of staining in ptd-FGFR4 transfected cells, com- pared with the membrane reactivity in wild-type FGFR4-transfected cells. G, Western blot detection of FGFR4 in hu- man pituitary adenomas. Protein lysates from seven human gonadotroph adeno- mas were electrophoresed and blotted with an antibody that recognizes the C terminus of FGFR4. The extreme right lane contains a positive control from HEK293 cells transiently transfected with ptd-FGFR4 (upper panel). Preab- sorption of the primary antibody with pu- rified antigen abolishes the lower 65-kDa protein (lower panel). The band migrat- ing just above 65 kDa is a nonspecific species that is not abolished by preab- sorption.
    Figure Legend Snippet: FIG. 1. Detection of FGFR4 reactivity in pituitary cells. A–D, Immunohistochem- ical localization of FGFR4 in human pi- tuitary adenomas. C-terminal FGFR4 immunoreactivity is seen in the cyto- plasm of tumor cells in varied tumor types. A, GH cell adenoma. B, ACTH cell adenoma. C, FSH/LH adenoma. D, Null cell adenoma. The immunoreactivity of FGFR4 is variable but always very in- tense throughout the cytoplasm (original magnification 50–100). E and F, Im- munohistochemical localization of FGFR4 and ptd-FGFR4 in transfected pituitary cells. Rat pituitary tumor-derived GH4 cells were stably transfected with full- length FGFR4 (E) or ptd-FGFR4 (F). Im- munocytochemical examination was per- formed using an antibody that recognizes the C terminus of FGFR4. Note the pre- dominant cytoplasmic pattern of staining in ptd-FGFR4 transfected cells, com- pared with the membrane reactivity in wild-type FGFR4-transfected cells. G, Western blot detection of FGFR4 in hu- man pituitary adenomas. Protein lysates from seven human gonadotroph adeno- mas were electrophoresed and blotted with an antibody that recognizes the C terminus of FGFR4. The extreme right lane contains a positive control from HEK293 cells transiently transfected with ptd-FGFR4 (upper panel). Preab- sorption of the primary antibody with pu- rified antigen abolishes the lower 65-kDa protein (lower panel). The band migrat- ing just above 65 kDa is a nonspecific species that is not abolished by preab- sorption.

    Techniques Used: Transfection, Derivative Assay, Stable Transfection, Staining, Membrane, Western Blot, Positive Control

    FIG. 2. Cytoplasmic expression levels of FGFR4 and Ki-67 LI in pituitary ad- enomas. A, The expression levels of FGFR4 in macroadenomas are signifi- cantly higher than those in microadeno- mas (P 0.02). B, The expression level of FGFR4 in invasive adenomas is not significantly different from noninvasive adenomas. C, The mean Ki-67 LI (per- cent) was significantly higher in tumors that express high levels of FGFR4 than in the low FGFR4-expressing group, which in turn was higher than in the FGFR4-negative group of tumors (P 0.03; P 0.002, respectively). D and E, Ki-67 LI was higher in macroadenomas and invasive adenomas than in mi- croadenomas and noninvasive adeno- mas (P 0.05; P 0.01, respectively).
    Figure Legend Snippet: FIG. 2. Cytoplasmic expression levels of FGFR4 and Ki-67 LI in pituitary ad- enomas. A, The expression levels of FGFR4 in macroadenomas are signifi- cantly higher than those in microadeno- mas (P 0.02). B, The expression level of FGFR4 in invasive adenomas is not significantly different from noninvasive adenomas. C, The mean Ki-67 LI (per- cent) was significantly higher in tumors that express high levels of FGFR4 than in the low FGFR4-expressing group, which in turn was higher than in the FGFR4-negative group of tumors (P 0.03; P 0.002, respectively). D and E, Ki-67 LI was higher in macroadenomas and invasive adenomas than in mi- croadenomas and noninvasive adeno- mas (P 0.05; P 0.01, respectively).

    Techniques Used: Expressing



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    fgfr4 peptide  (Santa Cruz Biotechnology)
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    Santa Cruz Biotechnology fgfr4 peptide
    FIG. 1. Detection of <t>FGFR4</t> reactivity in pituitary cells. A–D, Immunohistochem- ical localization of FGFR4 in human pi- tuitary adenomas. C-terminal FGFR4 immunoreactivity is seen in the cyto- plasm of tumor cells in varied tumor types. A, GH cell adenoma. B, ACTH cell adenoma. C, FSH/LH adenoma. D, Null cell adenoma. The immunoreactivity of FGFR4 is variable but always very in- tense throughout the cytoplasm (original magnification 50–100). E and F, Im- munohistochemical localization of FGFR4 and ptd-FGFR4 in transfected pituitary cells. Rat pituitary tumor-derived GH4 cells were stably transfected with full- length FGFR4 (E) or ptd-FGFR4 (F). Im- munocytochemical examination was per- formed using an antibody that recognizes the C terminus of FGFR4. Note the pre- dominant cytoplasmic pattern of staining in ptd-FGFR4 transfected cells, com- pared with the membrane reactivity in wild-type FGFR4-transfected cells. G, Western blot detection of FGFR4 in hu- man pituitary adenomas. Protein lysates from seven human gonadotroph adeno- mas were electrophoresed and blotted with an antibody that recognizes the C terminus of FGFR4. The extreme right lane contains a positive control from HEK293 cells transiently transfected with ptd-FGFR4 (upper panel). Preab- sorption of the primary antibody with pu- rified antigen abolishes the lower 65-kDa protein (lower panel). The band migrat- ing just above 65 kDa is a nonspecific species that is not abolished by preab- sorption.
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    https://www.bioz.com/product/fgfr4+peptide/pm15070963-72-28-30?v=Santa+Cruz+Biotechnology
    Average 94 stars, based on 1 article reviews
    fgfr4 peptide - by Bioz Stars, 2026-07
    94/100 stars
    		  Buy from Supplier

    Image Search Results


    FIG. 1. Detection of FGFR4 reactivity in pituitary cells. A–D, Immunohistochem- ical localization of FGFR4 in human pi- tuitary adenomas. C-terminal FGFR4 immunoreactivity is seen in the cyto- plasm of tumor cells in varied tumor types. A, GH cell adenoma. B, ACTH cell adenoma. C, FSH/LH adenoma. D, Null cell adenoma. The immunoreactivity of FGFR4 is variable but always very in- tense throughout the cytoplasm (original magnification 50–100). E and F, Im- munohistochemical localization of FGFR4 and ptd-FGFR4 in transfected pituitary cells. Rat pituitary tumor-derived GH4 cells were stably transfected with full- length FGFR4 (E) or ptd-FGFR4 (F). Im- munocytochemical examination was per- formed using an antibody that recognizes the C terminus of FGFR4. Note the pre- dominant cytoplasmic pattern of staining in ptd-FGFR4 transfected cells, com- pared with the membrane reactivity in wild-type FGFR4-transfected cells. G, Western blot detection of FGFR4 in hu- man pituitary adenomas. Protein lysates from seven human gonadotroph adeno- mas were electrophoresed and blotted with an antibody that recognizes the C terminus of FGFR4. The extreme right lane contains a positive control from HEK293 cells transiently transfected with ptd-FGFR4 (upper panel). Preab- sorption of the primary antibody with pu- rified antigen abolishes the lower 65-kDa protein (lower panel). The band migrat- ing just above 65 kDa is a nonspecific species that is not abolished by preab- sorption.

    Journal: The Journal of clinical endocrinology and metabolism

    Article Title: Cytoplasmic expression of fibroblast growth factor receptor-4 in human pituitary adenomas: relation to tumor type, size, proliferation, and invasiveness.

    doi: 10.1210/jc.2003-031489

    Figure Lengend Snippet: FIG. 1. Detection of FGFR4 reactivity in pituitary cells. A–D, Immunohistochem- ical localization of FGFR4 in human pi- tuitary adenomas. C-terminal FGFR4 immunoreactivity is seen in the cyto- plasm of tumor cells in varied tumor types. A, GH cell adenoma. B, ACTH cell adenoma. C, FSH/LH adenoma. D, Null cell adenoma. The immunoreactivity of FGFR4 is variable but always very in- tense throughout the cytoplasm (original magnification 50–100). E and F, Im- munohistochemical localization of FGFR4 and ptd-FGFR4 in transfected pituitary cells. Rat pituitary tumor-derived GH4 cells were stably transfected with full- length FGFR4 (E) or ptd-FGFR4 (F). Im- munocytochemical examination was per- formed using an antibody that recognizes the C terminus of FGFR4. Note the pre- dominant cytoplasmic pattern of staining in ptd-FGFR4 transfected cells, com- pared with the membrane reactivity in wild-type FGFR4-transfected cells. G, Western blot detection of FGFR4 in hu- man pituitary adenomas. Protein lysates from seven human gonadotroph adeno- mas were electrophoresed and blotted with an antibody that recognizes the C terminus of FGFR4. The extreme right lane contains a positive control from HEK293 cells transiently transfected with ptd-FGFR4 (upper panel). Preab- sorption of the primary antibody with pu- rified antigen abolishes the lower 65-kDa protein (lower panel). The band migrat- ing just above 65 kDa is a nonspecific species that is not abolished by preab- sorption.

    Article Snippet: Furthermore, the specificity of all reactions for FGFR4 was verified by replacing the primary antibody with normal serum, examining negative control tissues, and preabsorbing primary antibody with purified FGFR4 peptide (Santa Cruz, antibody: peptide/6:1).

    Techniques: Transfection, Derivative Assay, Stable Transfection, Staining, Membrane, Western Blot, Positive Control

    FIG. 2. Cytoplasmic expression levels of FGFR4 and Ki-67 LI in pituitary ad- enomas. A, The expression levels of FGFR4 in macroadenomas are signifi- cantly higher than those in microadeno- mas (P 0.02). B, The expression level of FGFR4 in invasive adenomas is not significantly different from noninvasive adenomas. C, The mean Ki-67 LI (per- cent) was significantly higher in tumors that express high levels of FGFR4 than in the low FGFR4-expressing group, which in turn was higher than in the FGFR4-negative group of tumors (P 0.03; P 0.002, respectively). D and E, Ki-67 LI was higher in macroadenomas and invasive adenomas than in mi- croadenomas and noninvasive adeno- mas (P 0.05; P 0.01, respectively).

    Journal: The Journal of clinical endocrinology and metabolism

    Article Title: Cytoplasmic expression of fibroblast growth factor receptor-4 in human pituitary adenomas: relation to tumor type, size, proliferation, and invasiveness.

    doi: 10.1210/jc.2003-031489

    Figure Lengend Snippet: FIG. 2. Cytoplasmic expression levels of FGFR4 and Ki-67 LI in pituitary ad- enomas. A, The expression levels of FGFR4 in macroadenomas are signifi- cantly higher than those in microadeno- mas (P 0.02). B, The expression level of FGFR4 in invasive adenomas is not significantly different from noninvasive adenomas. C, The mean Ki-67 LI (per- cent) was significantly higher in tumors that express high levels of FGFR4 than in the low FGFR4-expressing group, which in turn was higher than in the FGFR4-negative group of tumors (P 0.03; P 0.002, respectively). D and E, Ki-67 LI was higher in macroadenomas and invasive adenomas than in mi- croadenomas and noninvasive adeno- mas (P 0.05; P 0.01, respectively).

    Article Snippet: Furthermore, the specificity of all reactions for FGFR4 was verified by replacing the primary antibody with normal serum, examining negative control tissues, and preabsorbing primary antibody with purified FGFR4 peptide (Santa Cruz, antibody: peptide/6:1).

    Techniques: Expressing