alpha Tubulin Antikörper (Internal Region)

Produktnummer ABIN129653

Produktdetails anti-alpha Tubulin Antikörper

Target: alpha Tubulin (TUBA1)

Bindungsspezifität: Internal Region

Reaktivität: Human, Maus, Ratte, Huhn, Rind (Kuh)

Wirt: Kaninchen

Klonalität: Polyklonal

Konjugat: Dieser alpha Tubulin Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), ELISA

Spezifität: Anti-Tubulin Loading Control Antibody is directed against human alpha Tubulin protein. The Loading Control Antibody was affinity purified from monospecific antiserum by immunoaffinity purification. A BLAST analysis was used to suggest that this antibody would react with alpha Tubulin from a wide range of organisms, including avian, mammalian aquatic, parasitic and alga sources based on 100% homology for the immunogen sequence. Cross reactivity will occur with all isoforms of alpha tubulin. Such broad reactivity makes this antibody useful as an excellent loading control.

Produktmerkmale: Tubulin Loading Control Antibody recognizes microtubules which are involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintenance of cell shape. Tubulin itself is a globular protein consisting of two polypeptides (alpha and beta tubulin). Alpha and beta tubulin dimers are assembled to 13 protofilaments that form a microtubule of 22-nm diameter. Tyrosine ligase adds a C-terminal tyrosine to monomeric alpha tubulin. Assembled microtubules can again be detyrosinated by a cytoskeleton-associated carboxypeptidase. Detyrosinated alpha tubulin is referred to as Glu-tubulin. Another post-translational modification of detyrosinated alpha tubulin is C-terminal polyglutamylation, which is characteristic of microtubules in neuronal cells and the mitotic spindle. This antibody makes an excellent loading control.

Sterilität: Sterile filtered

Immunogen: Anti-Tubulin Loading Control Antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to amino acids 427-441 of Human alpha Tubulin.
Immunogen Type: Peptide

Isotyp: IgG

Anwendungsinformationen

Applikationshinweise: Anti-Tubulin Antibody has been tested for use in ELISA and western blot. Specific conditions for reactivity should be optimized by the end user. Expect a band at ~50 kDa in size corresponding to alpha tubulin by western blotting in most cell lysates or extracts.

Kommentare:

Gene Name: TUBA1B

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Konzentration: 1.1 mg/mL

Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

Konservierungsmittel: Sodium azide

Vorsichtsmaßnahmen: This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Lagerung: 4 °C/-20 °C

Informationen zur Lagerung: Store vial at 4 °C prior to restoration. For extended storage aliquot contents and freeze at -20 °C or below. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4 °C as an undiluted liquid. Dilute only prior to immediate use. Expiration date is one (1) year from date of opening.

Haltbarkeit: 12 months

Referenzen für anti-alpha Tubulin Antikörper (ABIN129653)

Garland, Comet, Wu, Radzisheuskaya, Rib, Vitting-Seerup, Lloret-Llinares, Sandelin, Helin, Jensen: "A Functional Link between Nuclear RNA Decay and Transcriptional Control Mediated by the Polycomb Repressive Complex 2." in: Cell reports, Vol. 29, Issue 7, pp. 1800-1811.e6, (2019) (PubMed).

Kim, Kim: "Effect of HIV-1 Tat on the formation of the mitotic spindle by interaction with ribosomal protein S3." in: Scientific reports, Vol. 8, Issue 1, pp. 8680, (2018) (PubMed).

Brown, Dayan, Wong, Kaczmarek, Hope, Pederson, Arnet, Goodall, Russell, Sadlon, Barry: "FOXP3 and miR-155 cooperate to control the invasive potential of human breast cancer cells by down regulating ZEB2 independently of ZEB1." in: Oncotarget, Vol. 9, Issue 45, pp. 27708-27727, (2018) (PubMed).

Lloret-Llinares, Karadoulama, Chen, Wojenski, Villafano, Bornholdt, Andersson, Core, Sandelin, Jensen: "The RNA exosome contributes to gene expression regulation during stem cell differentiation." in: Nucleic acids research, Vol. 46, Issue 21, pp. 11502-11513, (2018) (PubMed).

Ghosh, Abdelwahab, Reeber, Reidel, Marklew, Garrison, Lee, Dang, Herring, Glish, Kesimer, Tarran: "Little Cigars are More Toxic than Cigarettes and Uniquely Change the Airway Gene and Protein Expression." in: Scientific reports, Vol. 7, pp. 46239, (2018) (PubMed).

Kapadia, Bijelić, Zhao, Ma, Stojanovich, Milošević, Andjus, Šakić: "Effects of sustained i.c.v. infusion of lupus CSF and autoantibodies on behavioral phenotype and neuronal calcium signaling." in: Acta neuropathologica communications, Vol. 5, Issue 1, pp. 70, (2018) (PubMed).

Liao, Ren, Peterson, Marshak, Yau, Gamlin, Dacey: "Melanopsin-expressing ganglion cells on macaque and human retinas form two morphologically distinct populations." in: The Journal of comparative neurology, Vol. 524, Issue 14, pp. 2845-72, (2017) (PubMed).

Dilworth, Upadhyay, Bonnafous, Edoo, Bourbigot, Pesek-Jardim, Gudavicius, Serpa, Petrotchenko, Borchers, Nelson, Mackereth: "The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module." in: Nucleic acids research, Vol. 45, Issue 20, pp. 11989-12004, (2017) (PubMed).

Lloret-Llinares, Mapendano, Martlev, Lykke-Andersen, Jensen: "Relationships between PROMPT and gene expression." in: RNA biology, Vol. 13, Issue 1, pp. 6-14, (2016) (PubMed).

Li, Dou, Li, Zhang, Zeng, Song: "Nicotinamide ameliorates palmitate-induced ER stress in hepatocytes via cAMP/PKA/CREB pathway-dependent Sirt1 upregulation." in: Biochimica et biophysica acta, Vol. 1853, Issue 11 Pt A, pp. 2929-36, (2015) (PubMed).

Besche, Sha, Kukushkin, Peth, Hock, Kim, Gygi, Gutierrez, Liao, Dick, Goldberg: "Autoubiquitination of the 26S proteasome on Rpn13 regulates breakdown of ubiquitin conjugates." in: The EMBO journal, Vol. 33, Issue 10, pp. 1159-76, (2014) (PubMed).

Gudavicius, Dilworth, Serpa, Sessler, Petrotchenko, Borchers, Nelson: "The prolyl isomerase, FKBP25, interacts with RNA-engaged nucleolin and the pre-60S ribosomal subunit." in: RNA (New York, N.Y.), Vol. 20, Issue 7, pp. 1014-22, (2014) (PubMed).

Jakobsen, Sørensen, Brøndum, Daugaard, Thomsen, Nielsen: "Direct RNA sequencing mediated identification of mRNA localized in protrusions of human MDA-MB-231 metastatic breast cancer cells." in: Journal of molecular signaling, Vol. 8, Issue 1, pp. 9, (2013) (PubMed).

Balamurugan, Sharan, Klarmann, Zhang, Coppola, Summers, Roger, Morrison, Keller, Sterneck: "FBXW7α attenuates inflammatory signalling by downregulating C/EBPδ and its target gene Tlr4." in: Nature communications, Vol. 4, pp. 1662, (2013) (PubMed).

Hawkins, Oliaro, Kallies, Belz, Filby, Hogan, Haynes, Ramsbottom, Van Ham, Kinwell, Seddon, Davies, Tarlinton, Lew, Humbert, Russell: "Regulation of asymmetric cell division and polarity by Scribble is not required for humoral immunity." in: Nature communications, Vol. 4, pp. 1801, (2013) (PubMed).

Grewe, Hoffmann, Ohs, Blissenbach, Brandt, Tippler, Grunwald, Uberla: "Cytoplasmic utilization of human immunodeficiency virus type 1 genomic RNA is not dependent on a nuclear interaction with gag." in: Journal of virology, Vol. 86, Issue 6, pp. 2990-3002, (2012) (PubMed).

Sarkar, Sharan, Wang, Pawar, Cantwell, Johnson, Morrison, Wang, Sterneck: "Identification of a Src tyrosine kinase/SIAH2 E3 ubiquitin ligase pathway that regulates C/EBPδ expression and contributes to transformation of breast tumor cells." in: Molecular and cellular biology, Vol. 32, Issue 2, pp. 320-32, (2012) (PubMed).

Hall, Cowan: "Structural features and restricted expression of a human alpha-tubulin gene." in: Nucleic acids research, Vol. 13, Issue 1, pp. 207-23, (1985) (PubMed).

Details zu alpha Tubulin

Target: alpha Tubulin (TUBA1)

Andere Bezeichnung: alpha-Tubulin (TUBA1 Produkte)

Synonyme: Tuba1 antikoerper, K-ALPHA-1 antikoerper, Tuba-1 antikoerper, cb944 antikoerper, fb22g06 antikoerper, tuba1 antikoerper, wu:fb22g06 antikoerper, Calpha1 antikoerper, tubulin, alpha 1A antikoerper, tubulin alpha 1b antikoerper, tubulin, alpha 1b antikoerper, tubulin, alpha 1B antikoerper, Tuba1a antikoerper, TUBA1B antikoerper, tuba1b antikoerper, Tuba1b antikoerper

Hintergrund: Tubulin Loading Control Antibody recognizes microtubules which are involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintenance of cell shape. Tubulin itself is a globular protein consisting of two polypeptides (alpha and beta tubulin). Alpha and beta tubulin dimers are assembled to 13 protofilaments that form a microtubule of 22-nm diameter. Tyrosine ligase adds a C-terminal tyrosine to monomeric alpha tubulin. Assembled microtubules can again be detyrosinated by a cytoskeleton-associated carboxypeptidase. Detyrosinated alpha tubulin is referred to as Glu-tubulin. Another post-translational modification of detyrosinated alpha tubulin is C-terminal polyglutamylation, which is characteristic of microtubules in neuronal cells and the mitotic spindle. This antibody makes an excellent loading control.
Synonyms: Tubulin alpha-1B chain, Tubulin alpha-ubiquitous chain, Alpha-tubulin ubiquitous Tubulin K-alpha-1, TUBA1B, tubulin loading control

Gen-ID: 17986283

UniProt: P68363

Pathways: Microtubule Dynamics